HEADER TRANSPORT PROTEIN 26-JUN-24 9FVE TITLE CRYSTAL STRUCTURE OF VCSIAP W73A MUTANT IN COMPLEX WITH SIALIC ACID TITLE 2 AND A VHH ANTIBODY (VHH_VCP#2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SIALIC ACID-BINDING PERIPLASMIC PROTEIN SIAP; COMPND 3 CHAIN: A, C, E, G, I, K, M, O, Q, U, W, Y; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VHH_VCP#2; COMPND 7 CHAIN: B, D, F, H, J, L, N, P, R, T, V, X; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 3 ORGANISM_COMMON: ALPACA; SOURCE 4 ORGANISM_TAXID: 30538; SOURCE 5 GENE: SIAP, VC_1779; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 10 ORGANISM_COMMON: ALPACA; SOURCE 11 ORGANISM_TAXID: 30538; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SUBSTRATE BINDING PROTEIN, SIALIC ACID, TRAP TRANSPORTER, VHH KEYWDS 2 ANTIBODY, NANOBODY, COMPLEX, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR N.SCHNEBERGER,G.HAGELUEKEN REVDAT 1 06-NOV-24 9FVE 0 JRNL AUTH N.SCHNEBERGER,P.HENDRICKS,G.HAGELUEKEN JRNL TITL ALLOSTERIC SUBSTRATE RELEASE BY SIALIC ACID TRAP TRANSPORTER JRNL TITL 2 SBPS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.81 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.24 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 171247 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.234 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.267 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.170 REMARK 3 FREE R VALUE TEST SET COUNT : 2008 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 34.2400 - 6.7500 0.99 12271 147 0.2098 0.2575 REMARK 3 2 6.7500 - 5.3600 0.98 12015 143 0.2431 0.2723 REMARK 3 3 5.3600 - 4.6900 0.99 12121 143 0.2030 0.2104 REMARK 3 4 4.6900 - 4.2600 0.99 12143 145 0.1898 0.1887 REMARK 3 5 4.2600 - 3.9600 1.00 12150 145 0.2085 0.2620 REMARK 3 6 3.9500 - 3.7200 1.00 12111 144 0.2294 0.2611 REMARK 3 7 3.7200 - 3.5400 1.00 12220 144 0.2345 0.3150 REMARK 3 8 3.5400 - 3.3800 0.98 11803 144 0.2418 0.2455 REMARK 3 9 3.3800 - 3.2500 0.99 12087 141 0.2608 0.2794 REMARK 3 10 3.2500 - 3.1400 0.99 12087 144 0.2767 0.3273 REMARK 3 11 3.1400 - 3.0400 0.99 12094 141 0.2747 0.3457 REMARK 3 12 3.0400 - 2.9500 0.99 12011 140 0.2811 0.3299 REMARK 3 13 2.9500 - 2.8800 0.99 12054 143 0.2975 0.3452 REMARK 3 14 2.8800 - 2.8100 0.99 12072 144 0.3083 0.3583 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.388 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.455 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 51.31 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.14 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.017 40765 REMARK 3 ANGLE : 1.813 55152 REMARK 3 CHIRALITY : 0.098 6072 REMARK 3 PLANARITY : 0.016 7163 REMARK 3 DIHEDRAL : 8.375 5483 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "A" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "C" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 1 through 299 or REMARK 3 resid 301)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "G" and (resid 1 through 299 or REMARK 3 resid 301)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "I" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 6 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "K" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 7 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "M" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 8 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "O" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 9 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "Q" and (resid 1 through 299 or REMARK 3 resid 301)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 10 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "U" and (resid 1 through 299 or REMARK 3 resid 301)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 11 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "W" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 12 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "Y" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "D" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "F" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "J" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 6 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 7 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "N" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 8 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "P" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 9 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "R" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 10 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "T" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 11 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "V" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 12 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "X" and resid 1 through 121) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9FVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1292139767. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-JUN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY REMARK 200 BEAMLINE : P13 (MX1) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97626 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 171247 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.810 REMARK 200 RESOLUTION RANGE LOW (A) : 34.240 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 0.0646 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.81 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.91 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.34280 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.36 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM HEPES, PH 7.0, AMMONIUM REMARK 280 SULFATE, VAPOR DIFFUSION, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 111.78500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.55650 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 111.78500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 76.55650 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 24-MERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, T, REMARK 350 AND CHAINS: U, V, W, X, Y REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -3 REMARK 465 ALA A -2 REMARK 465 MET A -1 REMARK 465 GLY A 0 REMARK 465 GLY B -1 REMARK 465 GLY C -3 REMARK 465 ALA C -2 REMARK 465 MET C -1 REMARK 465 GLY C 0 REMARK 465 GLY D -1 REMARK 465 SER D 0 REMARK 465 GLY E -3 REMARK 465 ALA E -2 REMARK 465 GLY G -3 REMARK 465 ALA G -2 REMARK 465 MET G -1 REMARK 465 GLY G 0 REMARK 465 GLY I -3 REMARK 465 ALA I -2 REMARK 465 MET I -1 REMARK 465 GLY I 0 REMARK 465 GLY K -3 REMARK 465 ALA K -2 REMARK 465 MET K -1 REMARK 465 GLY K 0 REMARK 465 GLY M -3 REMARK 465 ALA M -2 REMARK 465 MET M -1 REMARK 465 GLY M 0 REMARK 465 GLY O -3 REMARK 465 ALA O -2 REMARK 465 MET O -1 REMARK 465 GLY O 0 REMARK 465 GLY Q -3 REMARK 465 ALA Q -2 REMARK 465 MET Q -1 REMARK 465 GLY Q 0 REMARK 465 GLY U -3 REMARK 465 ALA U -2 REMARK 465 MET U -1 REMARK 465 GLY U 0 REMARK 465 GLY W -3 REMARK 465 ALA W -2 REMARK 465 MET W -1 REMARK 465 GLY W 0 REMARK 465 GLY Y -3 REMARK 465 ALA Y -2 REMARK 465 MET Y -1 REMARK 465 GLY Y 0 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 MET E -1 CG SD CE REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 HE3 LYS D 43 HZ1 LYS G 282 1.10 REMARK 500 C GLY E 0 H ALA E 1 1.21 REMARK 500 OE2 GLU I 275 HE21 GLN I 278 1.26 REMARK 500 HD2 ARG N 45 HZ1 LYS N 107 1.34 REMARK 500 HG11 VAL A 255 HZ2 LYS A 259 1.34 REMARK 500 HD2 ARG N 45 NZ LYS N 107 1.48 REMARK 500 HE21 GLN H 39 O LYS H 43 1.49 REMARK 500 O GLN W 237 H GLY W 240 1.51 REMARK 500 HH12 ARG N 67 OD2 ASP N 90 1.51 REMARK 500 H LEU A 144 O SER A 162 1.51 REMARK 500 HZ1 LYS K 282 OE2 GLU K 283 1.51 REMARK 500 O LEU C 27 HG SER C 31 1.52 REMARK 500 OE2 GLU A 66 HO8 SLB A 301 1.55 REMARK 500 O LYS K 191 H LYS K 194 1.55 REMARK 500 O ILE W 232 H VAL W 236 1.55 REMARK 500 O THR A 26 H MET A 30 1.55 REMARK 500 HH12 ARG G 69 O ASN G 148 1.56 REMARK 500 O PHE B 37 H TYR B 95 1.56 REMARK 500 O LYS F 43 HA GLU F 44 1.57 REMARK 500 O GLN M 237 H GLY M 240 1.57 REMARK 500 HE21 GLN T 39 O LYS T 43 1.57 REMARK 500 HH12 ARG K 69 O ASN K 148 1.58 REMARK 500 O THR E 127 H ALA E 203 1.58 REMARK 500 O THR W 127 H ALA W 203 1.58 REMARK 500 O ALA A 65 H MET A 213 1.58 REMARK 500 O CYS B 96 H GLY B 112 1.59 REMARK 500 O PHE N 37 H TYR N 95 1.59 REMARK 500 O GLN H 13 H GLY H 16 1.60 REMARK 500 O PHE L 37 H TYR L 95 1.60 REMARK 500 OG1 THR W 128 OE1 GLN W 199 1.83 REMARK 500 OH TYR K 172 OE1 GLU K 197 1.99 REMARK 500 OG SER I 14 OE1 GLU I 16 2.01 REMARK 500 NH2 ARG O 131 O ASP O 138 2.02 REMARK 500 O SER A 31 OE1 GLU A 34 2.04 REMARK 500 OE2 GLU I 275 NE2 GLN I 278 2.06 REMARK 500 O ALA A 242 OG1 THR A 246 2.08 REMARK 500 O GLN W 237 N GLY W 240 2.10 REMARK 500 O GLN A 233 N VAL A 236 2.10 REMARK 500 O PRO W 188 OG1 THR W 192 2.11 REMARK 500 OH TYR E 172 OE2 GLU E 197 2.11 REMARK 500 NH1 ARG O 93 OE1 GLU O 97 2.12 REMARK 500 NE2 GLN M 237 OD2 ASP M 241 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 HG3 GLU O 275 HZ1 LYS T 43 4456 1.18 REMARK 500 HH11 ARG O 274 O GLY T 42 4456 1.22 REMARK 500 HZ2 LYS A 282 OE1 GLU J 44 4446 1.32 REMARK 500 HE22 GLN D 13 OD2 ASP W 59 3455 1.44 REMARK 500 HZ2 LYS N 43 OE2 GLU Y 271 2556 1.47 REMARK 500 OH TYR E 17 HE22 GLN U 290 4455 1.47 REMARK 500 OD1 ASN D 57 HE ARG N 10 3455 1.58 REMARK 500 HZ3 LYS A 282 OE1 GLU J 44 4446 1.60 REMARK 500 NZ LYS A 282 OE1 GLU J 44 4446 1.62 REMARK 500 OH TYR A 17 OE1 GLN I 290 3445 1.90 REMARK 500 NH1 ARG O 274 O GLY T 42 4456 1.90 REMARK 500 O GLY L 42 NZ LYS U 87 2455 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU A 34 CD GLU A 34 OE2 -0.073 REMARK 500 LYS A 140 CE LYS A 140 NZ 0.291 REMARK 500 LYS A 234 CB LYS A 234 CG 0.234 REMARK 500 LYS A 234 CD LYS A 234 CE -0.248 REMARK 500 LYS A 234 CE LYS A 234 NZ -0.184 REMARK 500 LYS A 248 CE LYS A 248 NZ 0.190 REMARK 500 ILE A 263 CB ILE A 263 CG2 0.200 REMARK 500 VAL B 12 CB VAL B 12 CG1 0.160 REMARK 500 VAL B 12 CB VAL B 12 CG2 0.195 REMARK 500 LYS B 43 CG LYS B 43 CD 0.285 REMARK 500 LYS B 43 CD LYS B 43 CE 0.283 REMARK 500 LYS B 107 CE LYS B 107 NZ 0.733 REMARK 500 MET C 22 CB MET C 22 CG 0.204 REMARK 500 MET C 22 CG MET C 22 SD 0.182 REMARK 500 GLU C 253 CD GLU C 253 OE1 0.071 REMARK 500 LEU C 254 CG LEU C 254 CD1 0.225 REMARK 500 GLU C 271 CB GLU C 271 CG 0.132 REMARK 500 LYS C 295 CE LYS C 295 NZ 0.190 REMARK 500 VAL D 12 CB VAL D 12 CG2 0.168 REMARK 500 LYS E 157 CE LYS E 157 NZ 0.181 REMARK 500 LEU E 187 CG LEU E 187 CD1 0.457 REMARK 500 LEU E 187 CG LEU E 187 CD2 0.397 REMARK 500 LYS E 238 CE LYS E 238 NZ 0.191 REMARK 500 VAL E 255 CB VAL E 255 CG1 0.146 REMARK 500 VAL E 255 CB VAL E 255 CG2 0.167 REMARK 500 LYS E 259 CE LYS E 259 NZ 0.178 REMARK 500 GLU E 275 CB GLU E 275 CG 0.140 REMARK 500 GLU E 275 CG GLU E 275 CD -0.093 REMARK 500 GLU F 44 CB GLU F 44 CG 0.222 REMARK 500 LEU G 27 CG LEU G 27 CD2 0.226 REMARK 500 GLU G 34 CG GLU G 34 CD -0.149 REMARK 500 GLU G 34 CD GLU G 34 OE1 -0.127 REMARK 500 GLU G 34 CD GLU G 34 OE2 -0.092 REMARK 500 LYS G 87 CB LYS G 87 CG 0.175 REMARK 500 LYS G 140 CG LYS G 140 CD 0.321 REMARK 500 LYS G 140 CD LYS G 140 CE 0.204 REMARK 500 LYS G 191 CD LYS G 191 CE 0.245 REMARK 500 LYS G 191 CE LYS G 191 NZ 0.330 REMARK 500 LYS G 234 CD LYS G 234 CE 0.221 REMARK 500 LYS G 234 CE LYS G 234 NZ 0.304 REMARK 500 VAL G 239 CB VAL G 239 CG1 0.217 REMARK 500 LYS G 259 CE LYS G 259 NZ 0.278 REMARK 500 VAL H 12 CB VAL H 12 CG1 0.158 REMARK 500 GLU H 44 CD GLU H 44 OE1 0.155 REMARK 500 GLU H 44 CD GLU H 44 OE2 0.154 REMARK 500 LYS I 36 CE LYS I 36 NZ 0.234 REMARK 500 ARG I 131 CB ARG I 131 CG 0.221 REMARK 500 GLU I 137 CB GLU I 137 CG 0.189 REMARK 500 GLU I 253 CB GLU I 253 CG 0.138 REMARK 500 GLU I 271 CB GLU I 271 CG -0.123 REMARK 500 REMARK 500 THIS ENTRY HAS 120 BOND DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU A 23 CB - CG - CD1 ANGL. DEV. = 18.1 DEGREES REMARK 500 LEU A 27 CB - CG - CD1 ANGL. DEV. = 25.3 DEGREES REMARK 500 LEU A 27 CB - CG - CD2 ANGL. DEV. = -16.8 DEGREES REMARK 500 GLU A 34 CB - CA - C ANGL. DEV. = 14.9 DEGREES REMARK 500 GLU A 34 N - CA - CB ANGL. DEV. = -14.3 DEGREES REMARK 500 ILE A 35 CG1 - CB - CG2 ANGL. DEV. = -14.0 DEGREES REMARK 500 ARG A 131 CB - CG - CD ANGL. DEV. = 16.8 DEGREES REMARK 500 ARG A 131 CG - CD - NE ANGL. DEV. = -20.2 DEGREES REMARK 500 LEU A 133 CA - CB - CG ANGL. DEV. = 15.6 DEGREES REMARK 500 LYS A 140 CD - CE - NZ ANGL. DEV. = -20.9 DEGREES REMARK 500 HIS A 206 N - CA - CB ANGL. DEV. = -12.0 DEGREES REMARK 500 SER A 219 N - CA - CB ANGL. DEV. = 9.8 DEGREES REMARK 500 LYS A 234 CB - CA - C ANGL. DEV. = 20.1 DEGREES REMARK 500 LYS A 234 CD - CE - NZ ANGL. DEV. = -15.1 DEGREES REMARK 500 LYS A 248 CB - CG - CD ANGL. DEV. = 28.0 DEGREES REMARK 500 LYS A 248 CD - CE - NZ ANGL. DEV. = 26.5 DEGREES REMARK 500 ILE A 263 CG1 - CB - CG2 ANGL. DEV. = 28.8 DEGREES REMARK 500 LYS A 282 CD - CE - NZ ANGL. DEV. = 16.1 DEGREES REMARK 500 VAL B 12 CG1 - CB - CG2 ANGL. DEV. = 16.4 DEGREES REMARK 500 LYS B 43 CG - CD - CE ANGL. DEV. = 23.1 DEGREES REMARK 500 LYS B 43 CD - CE - NZ ANGL. DEV. = -36.6 DEGREES REMARK 500 LYS B 107 CG - CD - CE ANGL. DEV. = 39.8 DEGREES REMARK 500 LYS C 140 CG - CD - CE ANGL. DEV. = 21.4 DEGREES REMARK 500 LYS C 140 CD - CE - NZ ANGL. DEV. = -16.1 DEGREES REMARK 500 ASN C 148 C - N - CA ANGL. DEV. = 24.4 DEGREES REMARK 500 ASN C 148 CB - CA - C ANGL. DEV. = 19.8 DEGREES REMARK 500 ASN C 148 N - CA - CB ANGL. DEV. = -16.7 DEGREES REMARK 500 GLN C 245 CA - CB - CG ANGL. DEV. = -15.0 DEGREES REMARK 500 LEU C 254 CA - CB - CG ANGL. DEV. = 16.5 DEGREES REMARK 500 ARG C 274 N - CA - CB ANGL. DEV. = -13.0 DEGREES REMARK 500 GLN C 278 N - CA - CB ANGL. DEV. = -15.9 DEGREES REMARK 500 GLN C 278 CA - CB - CG ANGL. DEV. = 15.6 DEGREES REMARK 500 GLN D 3 CA - CB - CG ANGL. DEV. = 15.3 DEGREES REMARK 500 VAL D 12 CG1 - CB - CG2 ANGL. DEV. = 11.5 DEGREES REMARK 500 GLN D 13 CB - CA - C ANGL. DEV. = -15.0 DEGREES REMARK 500 GLN D 13 N - CA - CB ANGL. DEV. = 13.7 DEGREES REMARK 500 GLN D 13 CA - CB - CG ANGL. DEV. = 24.3 DEGREES REMARK 500 LYS D 87 N - CA - CB ANGL. DEV. = 11.7 DEGREES REMARK 500 LYS D 87 CB - CG - CD ANGL. DEV. = -22.7 DEGREES REMARK 500 GLN E 110 CA - CB - CG ANGL. DEV. = 13.9 DEGREES REMARK 500 LEU E 187 CD1 - CG - CD2 ANGL. DEV. = 19.7 DEGREES REMARK 500 LEU E 187 CB - CG - CD1 ANGL. DEV. = 26.2 DEGREES REMARK 500 LEU E 187 CB - CG - CD2 ANGL. DEV. = -22.1 DEGREES REMARK 500 LYS E 234 CB - CG - CD ANGL. DEV. = -18.0 DEGREES REMARK 500 LYS E 234 CD - CE - NZ ANGL. DEV. = 14.4 DEGREES REMARK 500 LYS E 259 CD - CE - NZ ANGL. DEV. = 18.8 DEGREES REMARK 500 GLU F 44 C - N - CA ANGL. DEV. = -26.4 DEGREES REMARK 500 GLU F 44 N - CA - CB ANGL. DEV. = 14.2 DEGREES REMARK 500 GLU F 44 CA - CB - CG ANGL. DEV. = 14.4 DEGREES REMARK 500 ARG F 45 CB - CG - CD ANGL. DEV. = 16.7 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 205 ANGLE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 134 -142.98 54.46 REMARK 500 SER A 260 23.30 -66.35 REMARK 500 ILE A 292 -31.45 -144.33 REMARK 500 GLN B 113 15.94 -141.98 REMARK 500 ASN C 148 45.58 -68.74 REMARK 500 MET C 204 80.49 -68.12 REMARK 500 TYR C 267 74.33 -113.66 REMARK 500 ILE C 292 -25.89 -143.06 REMARK 500 LEU D 86 -174.05 -69.93 REMARK 500 LEU E 133 71.31 -119.16 REMARK 500 ASN E 178 29.91 47.48 REMARK 500 MET E 204 74.49 -54.65 REMARK 500 TYR E 267 73.42 -107.87 REMARK 500 ILE E 292 -29.65 -143.61 REMARK 500 ASN G 148 45.92 -69.75 REMARK 500 ASN G 178 29.82 46.91 REMARK 500 MET G 204 79.36 -57.81 REMARK 500 ILE G 292 -29.29 -144.27 REMARK 500 SER H 7 -25.03 -141.24 REMARK 500 MET I 204 76.62 -55.03 REMARK 500 GLU I 261 38.70 -99.31 REMARK 500 ILE I 292 -31.41 -144.98 REMARK 500 LYS J 107 93.17 24.93 REMARK 500 ASN K 148 47.92 -69.12 REMARK 500 MET K 204 73.43 -48.56 REMARK 500 GLN K 212 71.22 -165.09 REMARK 500 ILE K 292 -32.77 -144.21 REMARK 500 VAL K 293 -70.29 -34.90 REMARK 500 PRO L 41 106.80 -56.13 REMARK 500 LYS L 43 153.71 -31.97 REMARK 500 GLU M 29 -78.70 -25.95 REMARK 500 MET M 204 75.96 -50.87 REMARK 500 GLN M 237 -117.00 -16.88 REMARK 500 LYS M 238 -47.68 -24.54 REMARK 500 GLU M 261 35.23 -98.24 REMARK 500 ILE M 292 -28.88 -143.97 REMARK 500 GLN O 32 66.06 31.04 REMARK 500 ASN O 178 28.28 48.15 REMARK 500 MET O 204 76.75 -50.23 REMARK 500 GLN O 233 1.83 -55.11 REMARK 500 LYS O 234 -38.20 -134.95 REMARK 500 GLU O 261 34.92 -94.52 REMARK 500 ILE O 263 132.15 -20.80 REMARK 500 ILE O 292 -29.53 -143.45 REMARK 500 ASP P 27 -102.02 -79.72 REMARK 500 GLN P 113 -33.97 -139.40 REMARK 500 MET Q 204 74.56 -50.52 REMARK 500 ILE Q 292 -28.98 -143.03 REMARK 500 GLU R 44 128.55 -12.70 REMARK 500 VAL R 48 -60.20 -109.65 REMARK 500 REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLY A 33 GLU A 34 -140.65 REMARK 500 GLN B 113 GLY B 114 146.19 REMARK 500 GLU E 275 ALA E 276 -111.43 REMARK 500 ASN E 287 ILE E 288 -147.10 REMARK 500 GLN J 13 THR J 14 145.36 REMARK 500 ARG J 106 LYS J 107 107.79 REMARK 500 LYS L 107 TYR L 108 149.13 REMARK 500 GLU M 28 GLU M 29 148.06 REMARK 500 ASN M 178 ALA M 179 144.61 REMARK 500 VAL M 236 GLN M 237 133.24 REMARK 500 GLN M 237 LYS M 238 -147.11 REMARK 500 VAL N 12 GLN N 13 -136.53 REMARK 500 PHE O 139 LYS O 140 -144.22 REMARK 500 GLN O 233 LYS O 234 -133.80 REMARK 500 LYS O 234 ALA O 235 136.76 REMARK 500 GLU P 44 ARG P 45 137.22 REMARK 500 GLY P 112 GLN P 113 -122.59 REMARK 500 LYS R 43 GLU R 44 131.52 REMARK 500 GLY T 112 GLN T 113 144.77 REMARK 500 SER U 159 GLY U 160 -141.89 REMARK 500 LEU W 109 GLN W 110 149.33 REMARK 500 SER W 159 GLY W 160 -140.78 REMARK 500 GLU Y 275 ALA Y 276 -119.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 131 0.13 SIDE CHAIN REMARK 500 ARG A 274 0.08 SIDE CHAIN REMARK 500 ASN C 148 0.10 SIDE CHAIN REMARK 500 ARG C 274 0.25 SIDE CHAIN REMARK 500 GLN C 278 0.09 SIDE CHAIN REMARK 500 GLN D 113 0.13 SIDE CHAIN REMARK 500 ASN G 148 0.09 SIDE CHAIN REMARK 500 GLU G 271 0.08 SIDE CHAIN REMARK 500 GLU H 44 0.07 SIDE CHAIN REMARK 500 GLN I 245 0.09 SIDE CHAIN REMARK 500 GLU I 271 0.08 SIDE CHAIN REMARK 500 ASN K 148 0.09 SIDE CHAIN REMARK 500 GLN K 212 0.11 SIDE CHAIN REMARK 500 ARG L 45 0.17 SIDE CHAIN REMARK 500 GLU M 29 0.08 SIDE CHAIN REMARK 500 ASN O 148 0.10 SIDE CHAIN REMARK 500 ARG O 274 0.30 SIDE CHAIN REMARK 500 GLU P 44 0.07 SIDE CHAIN REMARK 500 ARG R 45 0.09 SIDE CHAIN REMARK 500 GLN R 113 0.09 SIDE CHAIN REMARK 500 ARG U 274 0.09 SIDE CHAIN REMARK 500 ARG W 93 0.10 SIDE CHAIN REMARK 500 GLN W 237 0.09 SIDE CHAIN REMARK 500 ARG W 274 0.14 SIDE CHAIN REMARK 500 ARG Y 131 0.13 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 SER A 159 -14.33 REMARK 500 SER A 219 11.21 REMARK 500 LEU D 86 -11.83 REMARK 500 LYS D 87 -10.75 REMARK 500 GLN K 245 13.69 REMARK 500 LYS L 43 -14.99 REMARK 500 LYS O 234 -12.19 REMARK 500 LEU U 173 -14.38 REMARK 500 SER Y 260 10.76 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 SLB A 301 REMARK 610 SLB C 301 REMARK 610 SLB E 301 REMARK 610 SLB G 301 REMARK 610 SLB I 301 REMARK 610 SLB K 301 REMARK 610 SLB M 301 REMARK 610 SLB O 301 REMARK 610 SLB Q 301 REMARK 610 SLB U 301 REMARK 610 SLB W 301 REMARK 610 SLB Y 301 DBREF 9FVE A 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE B -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE C 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE D -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE E 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE F -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE G 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE H -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE I 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE J -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE K 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE L -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE M 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE N -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE O 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE P -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE Q 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE R -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE T -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE U 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE V -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE W 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 DBREF 9FVE X -1 121 PDB 9FVE 9FVE -1 121 DBREF 9FVE Y 0 299 UNP Q9KR64 SIAP_VIBCH 22 321 SEQADV 9FVE GLY A -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA A -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET A -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY A 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA A 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY C -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA C -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET C -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY C 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA C 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY E -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA E -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET E -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY E 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA E 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY G -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA G -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET G -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY G 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA G 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY I -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA I -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET I -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY I 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA I 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY K -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA K -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET K -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY K 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA K 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY M -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA M -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET M -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY M 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA M 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY O -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA O -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET O -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY O 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA O 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY Q -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA Q -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET Q -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY Q 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA Q 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY U -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA U -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET U -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY U 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA U 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY W -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA W -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET W -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY W 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA W 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQADV 9FVE GLY Y -3 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE ALA Y -2 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE MET Y -1 UNP Q9KR64 EXPRESSION TAG SEQADV 9FVE GLY Y 0 UNP Q9KR64 ALA 22 CONFLICT SEQADV 9FVE ALA Y 73 UNP Q9KR64 TRP 95 ENGINEERED MUTATION SEQRES 1 A 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 A 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 A 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 A 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 A 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 A 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 A 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 A 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 A 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 A 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 A 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 A 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 A 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 A 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 A 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 A 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 A 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 A 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 A 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 A 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 A 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 A 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 A 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 A 303 LEU ALA ALA MET SEQRES 1 B 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 B 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 B 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 B 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 B 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 B 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 B 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 B 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 B 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 B 123 GLN VAL THR VAL SER SER SEQRES 1 C 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 C 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 C 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 C 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 C 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 C 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 C 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 C 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 C 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 C 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 C 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 C 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 C 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 C 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 C 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 C 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 C 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 C 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 C 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 C 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 C 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 C 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 C 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 C 303 LEU ALA ALA MET SEQRES 1 D 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 D 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 D 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 D 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 D 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 D 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 D 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 D 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 D 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 D 123 GLN VAL THR VAL SER SER SEQRES 1 E 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 E 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 E 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 E 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 E 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 E 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 E 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 E 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 E 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 E 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 E 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 E 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 E 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 E 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 E 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 E 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 E 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 E 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 E 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 E 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 E 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 E 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 E 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 E 303 LEU ALA ALA MET SEQRES 1 F 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 F 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 F 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 F 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 F 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 F 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 F 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 F 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 F 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 F 123 GLN VAL THR VAL SER SER SEQRES 1 G 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 G 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 G 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 G 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 G 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 G 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 G 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 G 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 G 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 G 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 G 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 G 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 G 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 G 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 G 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 G 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 G 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 G 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 G 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 G 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 G 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 G 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 G 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 G 303 LEU ALA ALA MET SEQRES 1 H 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 H 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 H 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 H 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 H 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 H 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 H 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 H 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 H 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 H 123 GLN VAL THR VAL SER SER SEQRES 1 I 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 I 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 I 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 I 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 I 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 I 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 I 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 I 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 I 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 I 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 I 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 I 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 I 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 I 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 I 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 I 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 I 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 I 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 I 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 I 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 I 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 I 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 I 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 I 303 LEU ALA ALA MET SEQRES 1 J 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 J 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 J 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 J 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 J 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 J 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 J 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 J 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 J 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 J 123 GLN VAL THR VAL SER SER SEQRES 1 K 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 K 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 K 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 K 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 K 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 K 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 K 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 K 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 K 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 K 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 K 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 K 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 K 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 K 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 K 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 K 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 K 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 K 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 K 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 K 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 K 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 K 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 K 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 K 303 LEU ALA ALA MET SEQRES 1 L 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 L 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 L 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 L 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 L 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 L 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 L 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 L 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 L 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 L 123 GLN VAL THR VAL SER SER SEQRES 1 M 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 M 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 M 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 M 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 M 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 M 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 M 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 M 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 M 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 M 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 M 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 M 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 M 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 M 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 M 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 M 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 M 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 M 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 M 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 M 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 M 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 M 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 M 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 M 303 LEU ALA ALA MET SEQRES 1 N 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 N 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 N 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 N 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 N 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 N 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 N 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 N 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 N 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 N 123 GLN VAL THR VAL SER SER SEQRES 1 O 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 O 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 O 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 O 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 O 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 O 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 O 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 O 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 O 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 O 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 O 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 O 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 O 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 O 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 O 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 O 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 O 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 O 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 O 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 O 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 O 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 O 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 O 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 O 303 LEU ALA ALA MET SEQRES 1 P 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 P 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 P 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 P 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 P 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 P 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 P 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 P 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 P 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 P 123 GLN VAL THR VAL SER SER SEQRES 1 Q 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 Q 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 Q 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 Q 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 Q 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 Q 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 Q 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 Q 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 Q 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 Q 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 Q 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 Q 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 Q 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 Q 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 Q 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 Q 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 Q 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 Q 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 Q 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 Q 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 Q 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 Q 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 Q 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 Q 303 LEU ALA ALA MET SEQRES 1 R 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 R 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 R 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 R 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 R 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 R 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 R 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 R 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 R 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 R 123 GLN VAL THR VAL SER SER SEQRES 1 T 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 T 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 T 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 T 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 T 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 T 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 T 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 T 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 T 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 T 123 GLN VAL THR VAL SER SER SEQRES 1 U 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 U 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 U 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 U 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 U 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 U 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 U 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 U 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 U 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 U 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 U 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 U 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 U 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 U 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 U 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 U 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 U 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 U 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 U 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 U 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 U 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 U 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 U 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 U 303 LEU ALA ALA MET SEQRES 1 V 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 V 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 V 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 V 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 V 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 V 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 V 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 V 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 V 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 V 123 GLN VAL THR VAL SER SER SEQRES 1 W 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 W 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 W 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 W 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 W 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 W 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 W 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 W 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 W 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 W 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 W 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 W 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 W 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 W 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 W 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 W 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 W 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 W 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 W 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 W 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 W 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 W 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 W 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 W 303 LEU ALA ALA MET SEQRES 1 X 123 GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY ARG LEU SEQRES 2 X 123 VAL GLN THR GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 X 123 SER GLY ASP THR PHE SER ASN TYR VAL MET GLY TRP PHE SEQRES 4 X 123 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SEQRES 5 X 123 ILE SER TRP THR GLY ALA ASN SER TYR TYR ALA ASP SER SEQRES 6 X 123 VAL ALA GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 X 123 ASN THR VAL ALA LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 X 123 ASP THR ALA ILE TYR TYR CYS ALA ALA ASP HIS PHE HIS SEQRES 9 X 123 VAL THR HIS ARG LYS TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 X 123 GLN VAL THR VAL SER SER SEQRES 1 Y 303 GLY ALA MET GLY ALA THR THR LEU LYS MET GLY MET GLN SEQRES 2 Y 303 ALA SER VAL GLY SER VAL GLU TYR ASN SER ALA LYS MET SEQRES 3 Y 303 LEU ALA ASP THR LEU GLU GLU MET SER GLN GLY GLU ILE SEQRES 4 Y 303 LYS LEU ALA LEU TYR PRO SER ALA GLN LEU GLY ASP ASP SEQRES 5 Y 303 ARG ALA MET LEU GLN GLN LEU THR LEU GLY ASP LEU ASP SEQRES 6 Y 303 ILE THR TYR ALA GLU PHE GLY ARG MET GLY LEU ALA ILE SEQRES 7 Y 303 PRO ARG ALA GLU ALA VAL MET LEU PRO TYR VAL ALA LYS SEQRES 8 Y 303 ASP PHE ASP HIS LEU ARG ARG MET PHE GLU SER ASP PHE SEQRES 9 Y 303 GLY GLN GLY VAL ARG ASP GLU MET LEU GLN LYS PHE ASN SEQRES 10 Y 303 TRP ARG ALA LEU ASP THR TRP TYR ASN GLY THR ARG GLU SEQRES 11 Y 303 THR THR SER ASN ARG PRO LEU ASN SER ILE GLU ASP PHE SEQRES 12 Y 303 LYS GLY LEU LYS LEU ARG VAL PRO ASN ALA LYS GLN ASN SEQRES 13 Y 303 LEU ASN TYR ALA LYS LEU SER GLY ALA SER PRO THR PRO SEQRES 14 Y 303 MET SER PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN SEQRES 15 Y 303 ALA VAL ASP GLY GLN GLU ASN PRO LEU PRO THR ILE LYS SEQRES 16 Y 303 THR MET LYS PHE TYR GLU VAL GLN LYS ASN LEU ALA MET SEQRES 17 Y 303 THR HIS HIS ILE VAL ASN ASP GLN MET VAL ILE ILE SER SEQRES 18 Y 303 GLU SER THR TRP GLN LYS LEU SER ASP THR ASP LYS ASP SEQRES 19 Y 303 ILE ILE GLN LYS ALA VAL GLN LYS VAL GLY ASP ALA HIS SEQRES 20 Y 303 THR GLN THR VAL LYS THR GLN GLU ALA GLU LEU VAL SER SEQRES 21 Y 303 PHE PHE LYS SER GLU GLY ILE ASN VAL THR TYR PRO ASP SEQRES 22 Y 303 LEU GLU PRO PHE ARG GLU ALA MET GLN PRO LEU TYR LYS SEQRES 23 Y 303 GLU PHE ASP SER ASN ILE GLY GLN PRO ILE VAL SER LYS SEQRES 24 Y 303 LEU ALA ALA MET HET SLB A 301 37 HET SLB C 301 37 HET SLB E 301 37 HET GOL E 302 14 HET SLB G 301 37 HET GOL G 302 14 HET SLB I 301 37 HET SLB K 301 37 HET SLB M 301 37 HET SLB O 301 37 HET SLB Q 301 37 HET GOL Q 302 14 HET SLB U 301 37 HET GOL U 302 14 HET GOL U 303 14 HET GOL U 304 14 HET SLB W 301 37 HET SLB Y 301 37 HETNAM SLB N-ACETYL-BETA-NEURAMINIC ACID HETNAM GOL GLYCEROL HETSYN SLB N-ACETYLNEURAMINIC ACID; SIALIC ACID; O-SIALIC ACID; 5- HETSYN 2 SLB N-ACETYL-BETA-D-NEURAMINIC ACID; BETA-SIALIC ACID HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 25 SLB 12(C11 H19 N O9) FORMUL 28 GOL 6(C3 H8 O3) HELIX 1 AA1 SER A 14 GLN A 32 1 19 HELIX 2 AA2 ASP A 47 LEU A 57 1 11 HELIX 3 AA3 PHE A 67 ALA A 73 5 7 HELIX 4 AA4 ILE A 74 LEU A 82 5 9 HELIX 5 AA5 ASP A 88 SER A 98 1 11 HELIX 6 AA6 SER A 98 ASN A 113 1 16 HELIX 7 AA7 SER A 135 LYS A 140 5 6 HELIX 8 AA8 ALA A 149 LEU A 158 1 10 HELIX 9 AA9 SER A 167 SER A 169 5 3 HELIX 10 AB1 GLU A 170 THR A 177 1 8 HELIX 11 AB2 PRO A 186 MET A 193 1 8 HELIX 12 AB3 LYS A 194 VAL A 198 5 5 HELIX 13 AB4 GLU A 218 GLN A 222 1 5 HELIX 14 AB5 SER A 225 SER A 260 1 36 HELIX 15 AB6 LEU A 270 GLY A 289 1 20 HELIX 16 AB7 ILE A 292 MET A 299 1 8 HELIX 17 AB8 THR B 28 TYR B 32 5 5 HELIX 18 AB9 LYS B 87 THR B 91 5 5 HELIX 19 AC1 SER C 14 SER C 31 1 18 HELIX 20 AC2 ASP C 47 LEU C 57 1 11 HELIX 21 AC3 GLU C 66 ALA C 73 5 8 HELIX 22 AC4 ILE C 74 LEU C 82 5 9 HELIX 23 AC5 ASP C 88 SER C 98 1 11 HELIX 24 AC6 SER C 98 ASN C 113 1 16 HELIX 25 AC7 SER C 135 LYS C 140 5 6 HELIX 26 AC8 ALA C 149 GLY C 160 1 12 HELIX 27 AC9 SER C 167 SER C 169 5 3 HELIX 28 AD1 GLU C 170 THR C 177 1 8 HELIX 29 AD2 LEU C 187 MET C 193 1 7 HELIX 30 AD3 LYS C 194 VAL C 198 5 5 HELIX 31 AD4 GLU C 218 GLN C 222 1 5 HELIX 32 AD5 SER C 225 GLU C 261 1 37 HELIX 33 AD6 LEU C 270 GLU C 275 1 6 HELIX 34 AD7 MET C 277 GLY C 289 1 13 HELIX 35 AD8 ILE C 292 MET C 299 1 8 HELIX 36 AD9 THR D 28 TYR D 32 5 5 HELIX 37 AE1 ASP D 62 ALA D 65 5 4 HELIX 38 AE2 LYS D 87 THR D 91 5 5 HELIX 39 AE3 SER E 14 SER E 31 1 18 HELIX 40 AE4 ASP E 47 LEU E 57 1 11 HELIX 41 AE5 GLU E 66 ALA E 73 5 8 HELIX 42 AE6 ILE E 74 LEU E 82 5 9 HELIX 43 AE7 ASP E 88 SER E 98 1 11 HELIX 44 AE8 SER E 98 ASN E 113 1 16 HELIX 45 AE9 SER E 135 LYS E 140 5 6 HELIX 46 AF1 ALA E 149 GLY E 160 1 12 HELIX 47 AF2 SER E 167 SER E 169 5 3 HELIX 48 AF3 GLU E 170 THR E 177 1 8 HELIX 49 AF4 PRO E 186 MET E 193 1 8 HELIX 50 AF5 LYS E 194 GLN E 199 5 6 HELIX 51 AF6 GLU E 218 GLN E 222 1 5 HELIX 52 AF7 SER E 225 GLU E 261 1 37 HELIX 53 AF8 LEU E 270 MET E 277 1 8 HELIX 54 AF9 MET E 277 GLY E 289 1 13 HELIX 55 AG1 ILE E 292 ALA E 298 1 7 HELIX 56 AG2 THR F 28 TYR F 32 5 5 HELIX 57 AG3 LYS F 87 THR F 91 5 5 HELIX 58 AG4 SER G 14 SER G 31 1 18 HELIX 59 AG5 ASP G 47 LEU G 57 1 11 HELIX 60 AG6 GLU G 66 ALA G 73 5 8 HELIX 61 AG7 ILE G 74 LEU G 82 5 9 HELIX 62 AG8 ASP G 88 SER G 98 1 11 HELIX 63 AG9 SER G 98 ASN G 113 1 16 HELIX 64 AH1 SER G 135 LYS G 140 5 6 HELIX 65 AH2 ALA G 149 GLY G 160 1 12 HELIX 66 AH3 SER G 167 SER G 169 5 3 HELIX 67 AH4 GLU G 170 THR G 177 1 8 HELIX 68 AH5 LEU G 187 MET G 193 1 7 HELIX 69 AH6 LYS G 194 VAL G 198 5 5 HELIX 70 AH7 GLU G 218 LEU G 224 1 7 HELIX 71 AH8 SER G 225 GLU G 261 1 37 HELIX 72 AH9 LEU G 270 GLY G 289 1 20 HELIX 73 AI1 ILE G 292 MET G 299 1 8 HELIX 74 AI2 THR H 28 TYR H 32 5 5 HELIX 75 AI3 ASP H 62 ALA H 65 5 4 HELIX 76 AI4 LYS H 87 THR H 91 5 5 HELIX 77 AI5 SER I 14 SER I 31 1 18 HELIX 78 AI6 ASP I 47 LEU I 57 1 11 HELIX 79 AI7 PHE I 67 ALA I 73 5 7 HELIX 80 AI8 ILE I 74 LEU I 82 5 9 HELIX 81 AI9 ASP I 88 SER I 98 1 11 HELIX 82 AJ1 SER I 98 ASN I 113 1 16 HELIX 83 AJ2 SER I 135 LYS I 140 5 6 HELIX 84 AJ3 ALA I 149 GLY I 160 1 12 HELIX 85 AJ4 SER I 167 SER I 169 5 3 HELIX 86 AJ5 GLU I 170 THR I 177 1 8 HELIX 87 AJ6 LEU I 187 MET I 193 1 7 HELIX 88 AJ7 LYS I 194 VAL I 198 5 5 HELIX 89 AJ8 GLU I 218 GLN I 222 1 5 HELIX 90 AJ9 SER I 225 GLU I 261 1 37 HELIX 91 AK1 LEU I 270 MET I 277 1 8 HELIX 92 AK2 MET I 277 GLY I 289 1 13 HELIX 93 AK3 ILE I 292 ALA I 298 1 7 HELIX 94 AK4 THR J 28 TYR J 32 5 5 HELIX 95 AK5 LYS J 87 THR J 91 5 5 HELIX 96 AK6 SER K 14 SER K 31 1 18 HELIX 97 AK7 ASP K 47 LEU K 57 1 11 HELIX 98 AK8 GLU K 66 ALA K 73 5 8 HELIX 99 AK9 ILE K 74 LEU K 82 5 9 HELIX 100 AL1 ASP K 88 SER K 98 1 11 HELIX 101 AL2 SER K 98 ASN K 113 1 16 HELIX 102 AL3 SER K 135 LYS K 140 5 6 HELIX 103 AL4 ALA K 149 GLY K 160 1 12 HELIX 104 AL5 SER K 167 SER K 169 5 3 HELIX 105 AL6 GLU K 170 THR K 177 1 8 HELIX 106 AL7 LEU K 187 MET K 193 1 7 HELIX 107 AL8 LYS K 194 GLN K 199 5 6 HELIX 108 AL9 GLU K 218 GLN K 222 1 5 HELIX 109 AM1 SER K 225 GLU K 261 1 37 HELIX 110 AM2 LEU K 270 MET K 277 1 8 HELIX 111 AM3 MET K 277 GLY K 289 1 13 HELIX 112 AM4 ILE K 292 ALA K 298 1 7 HELIX 113 AM5 THR L 28 TYR L 32 5 5 HELIX 114 AM6 LYS L 87 THR L 91 5 5 HELIX 115 AM7 SER M 14 SER M 31 1 18 HELIX 116 AM8 ASP M 47 LEU M 57 1 11 HELIX 117 AM9 GLU M 66 ALA M 73 5 8 HELIX 118 AN1 ILE M 74 LEU M 82 5 9 HELIX 119 AN2 ASP M 88 SER M 98 1 11 HELIX 120 AN3 SER M 98 ASN M 113 1 16 HELIX 121 AN4 SER M 135 LYS M 140 5 6 HELIX 122 AN5 ALA M 149 GLY M 160 1 12 HELIX 123 AN6 SER M 167 SER M 169 5 3 HELIX 124 AN7 GLU M 170 THR M 177 1 8 HELIX 125 AN8 LEU M 187 MET M 193 1 7 HELIX 126 AN9 LYS M 194 VAL M 198 5 5 HELIX 127 AO1 GLU M 218 LEU M 224 1 7 HELIX 128 AO2 SER M 225 GLU M 261 1 37 HELIX 129 AO3 LEU M 270 MET M 277 1 8 HELIX 130 AO4 MET M 277 GLY M 289 1 13 HELIX 131 AO5 ILE M 292 ALA M 298 1 7 HELIX 132 AO6 THR N 28 TYR N 32 5 5 HELIX 133 AO7 LYS N 87 THR N 91 5 5 HELIX 134 AO8 SER O 14 SER O 31 1 18 HELIX 135 AO9 ASP O 47 LEU O 57 1 11 HELIX 136 AP1 GLU O 66 ALA O 73 5 8 HELIX 137 AP2 ILE O 74 LEU O 82 5 9 HELIX 138 AP3 ASP O 88 SER O 98 1 11 HELIX 139 AP4 SER O 98 ASN O 113 1 16 HELIX 140 AP5 SER O 135 LYS O 140 5 6 HELIX 141 AP6 ALA O 149 GLY O 160 1 12 HELIX 142 AP7 SER O 167 SER O 169 5 3 HELIX 143 AP8 GLU O 170 THR O 177 1 8 HELIX 144 AP9 LEU O 187 MET O 193 1 7 HELIX 145 AQ1 LYS O 194 VAL O 198 5 5 HELIX 146 AQ2 GLU O 218 GLN O 222 1 5 HELIX 147 AQ3 SER O 225 GLU O 261 1 37 HELIX 148 AQ4 LEU O 270 MET O 277 1 8 HELIX 149 AQ5 MET O 277 GLY O 289 1 13 HELIX 150 AQ6 ILE O 292 ALA O 298 1 7 HELIX 151 AQ7 THR P 28 TYR P 32 5 5 HELIX 152 AQ8 ASP P 62 ALA P 65 5 4 HELIX 153 AQ9 LYS P 87 THR P 91 5 5 HELIX 154 AR1 SER Q 14 SER Q 31 1 18 HELIX 155 AR2 ASP Q 47 LEU Q 57 1 11 HELIX 156 AR3 GLU Q 66 ALA Q 73 5 8 HELIX 157 AR4 ILE Q 74 LEU Q 82 5 9 HELIX 158 AR5 ASP Q 88 SER Q 98 1 11 HELIX 159 AR6 SER Q 98 ASN Q 113 1 16 HELIX 160 AR7 SER Q 135 LYS Q 140 5 6 HELIX 161 AR8 ALA Q 149 SER Q 159 1 11 HELIX 162 AR9 SER Q 167 SER Q 169 5 3 HELIX 163 AS1 GLU Q 170 THR Q 177 1 8 HELIX 164 AS2 LEU Q 187 MET Q 193 1 7 HELIX 165 AS3 LYS Q 194 VAL Q 198 5 5 HELIX 166 AS4 GLU Q 218 LYS Q 223 1 6 HELIX 167 AS5 SER Q 225 GLU Q 261 1 37 HELIX 168 AS6 LEU Q 270 GLY Q 289 1 20 HELIX 169 AS7 ILE Q 292 ALA Q 298 1 7 HELIX 170 AS8 THR R 28 TYR R 32 5 5 HELIX 171 AS9 ASP R 62 ALA R 65 5 4 HELIX 172 AT1 LYS R 87 THR R 91 5 5 HELIX 173 AT2 THR T 28 TYR T 32 5 5 HELIX 174 AT3 ASP T 62 ALA T 65 5 4 HELIX 175 AT4 LYS T 87 THR T 91 5 5 HELIX 176 AT5 SER U 14 SER U 31 1 18 HELIX 177 AT6 ASP U 47 LEU U 57 1 11 HELIX 178 AT7 GLU U 66 ALA U 73 5 8 HELIX 179 AT8 ILE U 74 LEU U 82 5 9 HELIX 180 AT9 ASP U 88 SER U 98 1 11 HELIX 181 AU1 SER U 98 ASN U 113 1 16 HELIX 182 AU2 SER U 135 LYS U 140 5 6 HELIX 183 AU3 ALA U 149 GLY U 160 1 12 HELIX 184 AU4 SER U 167 SER U 169 5 3 HELIX 185 AU5 GLU U 170 THR U 177 1 8 HELIX 186 AU6 LEU U 187 MET U 193 1 7 HELIX 187 AU7 LYS U 194 GLN U 199 5 6 HELIX 188 AU8 GLU U 218 GLN U 222 1 5 HELIX 189 AU9 SER U 225 GLU U 261 1 37 HELIX 190 AV1 ASP U 269 MET U 277 1 9 HELIX 191 AV2 MET U 277 GLY U 289 1 13 HELIX 192 AV3 ILE U 292 ALA U 298 1 7 HELIX 193 AV4 THR V 28 TYR V 32 5 5 HELIX 194 AV5 LYS V 87 THR V 91 5 5 HELIX 195 AV6 SER W 14 SER W 31 1 18 HELIX 196 AV7 ASP W 47 LEU W 57 1 11 HELIX 197 AV8 PHE W 67 ALA W 73 5 7 HELIX 198 AV9 ILE W 74 LEU W 82 5 9 HELIX 199 AW1 ASP W 88 SER W 98 1 11 HELIX 200 AW2 SER W 98 ASN W 113 1 16 HELIX 201 AW3 SER W 135 LYS W 140 5 6 HELIX 202 AW4 ALA W 149 GLY W 160 1 12 HELIX 203 AW5 SER W 167 SER W 169 5 3 HELIX 204 AW6 GLU W 170 THR W 177 1 8 HELIX 205 AW7 LEU W 187 MET W 193 1 7 HELIX 206 AW8 LYS W 194 VAL W 198 5 5 HELIX 207 AW9 GLU W 218 GLN W 222 1 5 HELIX 208 AX1 SER W 225 GLU W 261 1 37 HELIX 209 AX2 LEU W 270 GLY W 289 1 20 HELIX 210 AX3 ILE W 292 ALA W 298 1 7 HELIX 211 AX4 THR X 28 TYR X 32 5 5 HELIX 212 AX5 ASP X 62 ALA X 65 5 4 HELIX 213 AX6 LYS X 87 THR X 91 5 5 HELIX 214 AX7 SER Y 14 SER Y 31 1 18 HELIX 215 AX8 ASP Y 47 LEU Y 57 1 11 HELIX 216 AX9 GLU Y 66 ALA Y 73 5 8 HELIX 217 AY1 ILE Y 74 LEU Y 82 5 9 HELIX 218 AY2 ASP Y 88 SER Y 98 1 11 HELIX 219 AY3 SER Y 98 ASN Y 113 1 16 HELIX 220 AY4 SER Y 135 LYS Y 140 5 6 HELIX 221 AY5 ALA Y 149 GLY Y 160 1 12 HELIX 222 AY6 SER Y 167 SER Y 169 5 3 HELIX 223 AY7 GLU Y 170 THR Y 177 1 8 HELIX 224 AY8 LEU Y 187 MET Y 193 1 7 HELIX 225 AY9 LYS Y 194 GLN Y 199 5 6 HELIX 226 AZ1 GLU Y 218 GLN Y 222 1 5 HELIX 227 AZ2 SER Y 225 SER Y 260 1 36 HELIX 228 AZ3 ASP Y 269 MET Y 277 1 9 HELIX 229 AZ4 MET Y 277 GLY Y 289 1 13 HELIX 230 AZ5 ILE Y 292 ALA Y 298 1 7 SHEET 1 AA1 5 ILE A 35 TYR A 40 0 SHEET 2 AA1 5 THR A 2 GLY A 7 1 N LEU A 4 O ALA A 38 SHEET 3 AA1 5 ILE A 62 ALA A 65 1 O ILE A 62 N GLY A 7 SHEET 4 AA1 5 VAL A 209 SER A 217 -1 O MET A 213 N ALA A 65 SHEET 5 AA1 5 TRP A 114 THR A 124 -1 N GLY A 123 O ASN A 210 SHEET 1 AA2 2 GLU A 126 SER A 129 0 SHEET 2 AA2 2 GLY A 182 ASN A 185 -1 O ASN A 185 N GLU A 126 SHEET 1 AA3 2 LYS A 143 VAL A 146 0 SHEET 2 AA3 2 SER A 162 PRO A 165 1 O SER A 162 N LEU A 144 SHEET 1 AA4 2 ASN A 201 LEU A 202 0 SHEET 2 AA4 2 ASN A 264 VAL A 265 1 O ASN A 264 N LEU A 202 SHEET 1 AA5 8 VAL B 2 SER B 7 0 SHEET 2 AA5 8 SER B 17 GLY B 26 -1 O ALA B 23 N VAL B 5 SHEET 3 AA5 8 ASN L 57 TYR L 60 -1 O SER L 58 N SER B 17 SHEET 4 AA5 8 GLU L 46 ILE L 51 -1 N ALA L 50 O TYR L 59 SHEET 5 AA5 8 VAL L 33 GLN L 39 -1 N TRP L 36 O ALA L 49 SHEET 6 AA5 8 ALA L 92 ASP L 99 -1 O TYR L 95 N PHE L 37 SHEET 7 AA5 8 THR L 115 SER L 120 -1 O VAL L 117 N ALA L 92 SHEET 8 AA5 8 LEU L 11 GLN L 13 1 N VAL L 12 O SER L 120 SHEET 1 AA6 8 PHE B 68 ASP B 73 0 SHEET 2 AA6 8 THR B 78 MET B 83 -1 O ALA B 80 N SER B 71 SHEET 3 AA6 8 SER B 17 GLY B 26 -1 N LEU B 18 O MET B 83 SHEET 4 AA6 8 ASN L 57 TYR L 60 -1 O SER L 58 N SER B 17 SHEET 5 AA6 8 GLU L 46 ILE L 51 -1 N ALA L 50 O TYR L 59 SHEET 6 AA6 8 VAL L 33 GLN L 39 -1 N TRP L 36 O ALA L 49 SHEET 7 AA6 8 ALA L 92 ASP L 99 -1 O TYR L 95 N PHE L 37 SHEET 8 AA6 8 TYR L 110 TRP L 111 -1 O TYR L 110 N ALA L 98 SHEET 1 AA7 6 LEU B 11 GLN B 13 0 SHEET 2 AA7 6 THR B 115 SER B 120 1 O SER B 120 N VAL B 12 SHEET 3 AA7 6 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 115 SHEET 4 AA7 6 VAL B 33 GLN B 39 -1 N PHE B 37 O TYR B 95 SHEET 5 AA7 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA7 6 SER B 58 TYR B 60 -1 O TYR B 59 N ALA B 50 SHEET 1 AA8 4 LEU B 11 GLN B 13 0 SHEET 2 AA8 4 THR B 115 SER B 120 1 O SER B 120 N VAL B 12 SHEET 3 AA8 4 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 115 SHEET 4 AA8 4 TYR B 110 TRP B 111 -1 O TYR B 110 N ALA B 98 SHEET 1 AA9 6 ILE C 35 TYR C 40 0 SHEET 2 AA9 6 THR C 2 GLY C 7 1 N LEU C 4 O LYS C 36 SHEET 3 AA9 6 ILE C 62 ALA C 65 1 O ILE C 62 N GLY C 7 SHEET 4 AA9 6 VAL C 209 SER C 217 -1 O MET C 213 N ALA C 65 SHEET 5 AA9 6 TRP C 114 SER C 129 -1 N GLY C 123 O ASN C 210 SHEET 6 AA9 6 GLY C 182 PRO C 186 -1 O GLN C 183 N THR C 128 SHEET 1 AB1 7 ILE C 35 TYR C 40 0 SHEET 2 AB1 7 THR C 2 GLY C 7 1 N LEU C 4 O LYS C 36 SHEET 3 AB1 7 ILE C 62 ALA C 65 1 O ILE C 62 N GLY C 7 SHEET 4 AB1 7 VAL C 209 SER C 217 -1 O MET C 213 N ALA C 65 SHEET 5 AB1 7 TRP C 114 SER C 129 -1 N GLY C 123 O ASN C 210 SHEET 6 AB1 7 ASN C 201 ALA C 203 -1 O ALA C 203 N THR C 127 SHEET 7 AB1 7 ASN C 264 THR C 266 1 O THR C 266 N LEU C 202 SHEET 1 AB2 2 LYS C 143 VAL C 146 0 SHEET 2 AB2 2 SER C 162 PRO C 165 1 O THR C 164 N LEU C 144 SHEET 1 AB3 4 VAL D 2 SER D 7 0 SHEET 2 AB3 4 LEU D 18 GLY D 26 -1 O SER D 21 N SER D 7 SHEET 3 AB3 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AB3 4 PHE D 68 ASP D 73 -1 N SER D 71 O ALA D 80 SHEET 1 AB4 6 LEU D 11 GLN D 13 0 SHEET 2 AB4 6 THR D 115 SER D 120 1 O THR D 118 N VAL D 12 SHEET 3 AB4 6 ALA D 92 ASP D 99 -1 N TYR D 94 O THR D 115 SHEET 4 AB4 6 VAL D 33 GLN D 39 -1 N PHE D 37 O TYR D 95 SHEET 5 AB4 6 GLU D 46 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AB4 6 SER D 58 TYR D 60 -1 O TYR D 59 N ALA D 50 SHEET 1 AB5 4 LEU D 11 GLN D 13 0 SHEET 2 AB5 4 THR D 115 SER D 120 1 O THR D 118 N VAL D 12 SHEET 3 AB5 4 ALA D 92 ASP D 99 -1 N TYR D 94 O THR D 115 SHEET 4 AB5 4 TYR D 110 TRP D 111 -1 O TYR D 110 N ALA D 98 SHEET 1 AB6 6 ILE E 35 TYR E 40 0 SHEET 2 AB6 6 THR E 2 GLY E 7 1 N LEU E 4 O LYS E 36 SHEET 3 AB6 6 ILE E 62 ALA E 65 1 O ILE E 62 N LYS E 5 SHEET 4 AB6 6 ASN E 201 SER E 217 -1 O MET E 213 N ALA E 65 SHEET 5 AB6 6 TRP E 114 SER E 129 -1 N THR E 127 O ALA E 203 SHEET 6 AB6 6 GLY E 182 ASN E 185 -1 O GLN E 183 N THR E 128 SHEET 1 AB7 5 ILE E 35 TYR E 40 0 SHEET 2 AB7 5 THR E 2 GLY E 7 1 N LEU E 4 O LYS E 36 SHEET 3 AB7 5 ILE E 62 ALA E 65 1 O ILE E 62 N LYS E 5 SHEET 4 AB7 5 ASN E 201 SER E 217 -1 O MET E 213 N ALA E 65 SHEET 5 AB7 5 ASN E 264 THR E 266 1 O ASN E 264 N LEU E 202 SHEET 1 AB8 2 LYS E 143 VAL E 146 0 SHEET 2 AB8 2 SER E 162 PRO E 165 1 O THR E 164 N LEU E 144 SHEET 1 AB9 4 VAL F 2 SER F 7 0 SHEET 2 AB9 4 LEU F 18 GLY F 26 -1 O SER F 21 N SER F 7 SHEET 3 AB9 4 THR F 78 MET F 83 -1 O MET F 83 N LEU F 18 SHEET 4 AB9 4 PHE F 68 ASP F 73 -1 N SER F 71 O ALA F 80 SHEET 1 AC1 6 LEU F 11 GLN F 13 0 SHEET 2 AC1 6 THR F 115 SER F 120 1 O THR F 118 N VAL F 12 SHEET 3 AC1 6 ALA F 92 ASP F 99 -1 N TYR F 94 O THR F 115 SHEET 4 AC1 6 VAL F 33 GLN F 39 -1 N PHE F 37 O TYR F 95 SHEET 5 AC1 6 GLU F 46 ILE F 51 -1 O ALA F 49 N TRP F 36 SHEET 6 AC1 6 SER F 58 TYR F 60 -1 O TYR F 59 N ALA F 50 SHEET 1 AC2 4 LEU F 11 GLN F 13 0 SHEET 2 AC2 4 THR F 115 SER F 120 1 O THR F 118 N VAL F 12 SHEET 3 AC2 4 ALA F 92 ASP F 99 -1 N TYR F 94 O THR F 115 SHEET 4 AC2 4 TYR F 110 TRP F 111 -1 O TYR F 110 N ALA F 98 SHEET 1 AC3 6 ILE G 35 TYR G 40 0 SHEET 2 AC3 6 THR G 2 GLY G 7 1 N LEU G 4 O ALA G 38 SHEET 3 AC3 6 ILE G 62 ALA G 65 1 O ILE G 62 N LYS G 5 SHEET 4 AC3 6 ASN G 201 SER G 217 -1 O MET G 213 N ALA G 65 SHEET 5 AC3 6 TRP G 114 SER G 129 -1 N THR G 127 O ALA G 203 SHEET 6 AC3 6 GLY G 182 PRO G 186 -1 O ASN G 185 N GLU G 126 SHEET 1 AC4 5 ILE G 35 TYR G 40 0 SHEET 2 AC4 5 THR G 2 GLY G 7 1 N LEU G 4 O ALA G 38 SHEET 3 AC4 5 ILE G 62 ALA G 65 1 O ILE G 62 N LYS G 5 SHEET 4 AC4 5 ASN G 201 SER G 217 -1 O MET G 213 N ALA G 65 SHEET 5 AC4 5 ASN G 264 THR G 266 1 O THR G 266 N LEU G 202 SHEET 1 AC5 2 LYS G 143 VAL G 146 0 SHEET 2 AC5 2 SER G 162 PRO G 165 1 O THR G 164 N LEU G 144 SHEET 1 AC6 4 VAL H 2 GLU H 6 0 SHEET 2 AC6 4 LEU H 18 GLY H 26 -1 O SER H 25 N GLN H 3 SHEET 3 AC6 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AC6 4 PHE H 68 ASP H 73 -1 N SER H 71 O ALA H 80 SHEET 1 AC7 6 LEU H 11 GLN H 13 0 SHEET 2 AC7 6 THR H 115 SER H 120 1 O SER H 120 N VAL H 12 SHEET 3 AC7 6 ALA H 92 ASP H 99 -1 N ALA H 92 O VAL H 117 SHEET 4 AC7 6 VAL H 33 GLN H 39 -1 N PHE H 37 O TYR H 95 SHEET 5 AC7 6 GLU H 46 ILE H 51 -1 O ALA H 49 N TRP H 36 SHEET 6 AC7 6 SER H 58 TYR H 60 -1 O TYR H 59 N ALA H 50 SHEET 1 AC8 4 LEU H 11 GLN H 13 0 SHEET 2 AC8 4 THR H 115 SER H 120 1 O SER H 120 N VAL H 12 SHEET 3 AC8 4 ALA H 92 ASP H 99 -1 N ALA H 92 O VAL H 117 SHEET 4 AC8 4 TYR H 110 TRP H 111 -1 O TYR H 110 N ALA H 98 SHEET 1 AC9 6 ILE I 35 TYR I 40 0 SHEET 2 AC9 6 THR I 2 GLY I 7 1 N LEU I 4 O LYS I 36 SHEET 3 AC9 6 ILE I 62 ALA I 65 1 O ILE I 62 N LYS I 5 SHEET 4 AC9 6 ASN I 201 SER I 217 -1 O MET I 213 N ALA I 65 SHEET 5 AC9 6 TRP I 114 SER I 129 -1 N THR I 127 O ALA I 203 SHEET 6 AC9 6 GLY I 182 PRO I 186 -1 O ASN I 185 N GLU I 126 SHEET 1 AD1 5 ILE I 35 TYR I 40 0 SHEET 2 AD1 5 THR I 2 GLY I 7 1 N LEU I 4 O LYS I 36 SHEET 3 AD1 5 ILE I 62 ALA I 65 1 O ILE I 62 N LYS I 5 SHEET 4 AD1 5 ASN I 201 SER I 217 -1 O MET I 213 N ALA I 65 SHEET 5 AD1 5 ASN I 264 THR I 266 1 O THR I 266 N LEU I 202 SHEET 1 AD2 2 LYS I 143 VAL I 146 0 SHEET 2 AD2 2 SER I 162 PRO I 165 1 O THR I 164 N LEU I 144 SHEET 1 AD3 4 VAL J 2 SER J 7 0 SHEET 2 AD3 4 LEU J 18 GLY J 26 -1 O SER J 25 N GLN J 3 SHEET 3 AD3 4 THR J 78 MET J 83 -1 O MET J 83 N LEU J 18 SHEET 4 AD3 4 PHE J 68 ASP J 73 -1 N THR J 69 O GLN J 82 SHEET 1 AD4 6 LEU J 11 GLN J 13 0 SHEET 2 AD4 6 THR J 115 SER J 120 1 O SER J 120 N VAL J 12 SHEET 3 AD4 6 ALA J 92 ASP J 99 -1 N TYR J 94 O THR J 115 SHEET 4 AD4 6 VAL J 33 GLN J 39 -1 N PHE J 37 O TYR J 95 SHEET 5 AD4 6 GLU J 46 ILE J 51 -1 O GLU J 46 N ARG J 38 SHEET 6 AD4 6 SER J 58 TYR J 60 -1 O TYR J 59 N ALA J 50 SHEET 1 AD5 4 LEU J 11 GLN J 13 0 SHEET 2 AD5 4 THR J 115 SER J 120 1 O SER J 120 N VAL J 12 SHEET 3 AD5 4 ALA J 92 ASP J 99 -1 N TYR J 94 O THR J 115 SHEET 4 AD5 4 TYR J 110 TRP J 111 -1 O TYR J 110 N ALA J 98 SHEET 1 AD6 8 ILE K 35 TYR K 40 0 SHEET 2 AD6 8 THR K 2 GLY K 7 1 N LEU K 4 O LYS K 36 SHEET 3 AD6 8 ILE K 62 ALA K 65 1 O ILE K 62 N LYS K 5 SHEET 4 AD6 8 ASN K 201 SER K 217 -1 O ILE K 215 N THR K 63 SHEET 5 AD6 8 TRP K 114 SER K 129 -1 N THR K 127 O ALA K 203 SHEET 6 AD6 8 GLY K 182 PRO K 186 -1 O ASN K 185 N GLU K 126 SHEET 7 AD6 8 LYS K 143 VAL K 146 1 N ARG K 145 O GLY K 182 SHEET 8 AD6 8 SER K 162 PRO K 165 1 O THR K 164 N LEU K 144 SHEET 1 AD7 5 ILE K 35 TYR K 40 0 SHEET 2 AD7 5 THR K 2 GLY K 7 1 N LEU K 4 O LYS K 36 SHEET 3 AD7 5 ILE K 62 ALA K 65 1 O ILE K 62 N LYS K 5 SHEET 4 AD7 5 ASN K 201 SER K 217 -1 O ILE K 215 N THR K 63 SHEET 5 AD7 5 ASN K 264 THR K 266 1 O THR K 266 N LEU K 202 SHEET 1 AD8 4 VAL L 2 SER L 7 0 SHEET 2 AD8 4 LEU L 18 GLY L 26 -1 O SER L 25 N GLN L 3 SHEET 3 AD8 4 THR L 78 MET L 83 -1 O MET L 83 N LEU L 18 SHEET 4 AD8 4 THR L 69 ASP L 73 -1 N SER L 71 O ALA L 80 SHEET 1 AD9 6 ILE M 35 TYR M 40 0 SHEET 2 AD9 6 THR M 2 GLY M 7 1 N LEU M 4 O LYS M 36 SHEET 3 AD9 6 ILE M 62 ALA M 65 1 O ILE M 62 N LYS M 5 SHEET 4 AD9 6 ASN M 201 SER M 217 -1 O MET M 213 N ALA M 65 SHEET 5 AD9 6 TRP M 114 SER M 129 -1 N THR M 127 O ALA M 203 SHEET 6 AD9 6 GLY M 182 PRO M 186 -1 O GLN M 183 N THR M 128 SHEET 1 AE1 5 ILE M 35 TYR M 40 0 SHEET 2 AE1 5 THR M 2 GLY M 7 1 N LEU M 4 O LYS M 36 SHEET 3 AE1 5 ILE M 62 ALA M 65 1 O ILE M 62 N LYS M 5 SHEET 4 AE1 5 ASN M 201 SER M 217 -1 O MET M 213 N ALA M 65 SHEET 5 AE1 5 ASN M 264 THR M 266 1 O THR M 266 N LEU M 202 SHEET 1 AE2 2 LYS M 143 VAL M 146 0 SHEET 2 AE2 2 SER M 162 PRO M 165 1 O THR M 164 N LEU M 144 SHEET 1 AE3 4 VAL N 2 SER N 7 0 SHEET 2 AE3 4 LEU N 18 GLY N 26 -1 O SER N 21 N SER N 7 SHEET 3 AE3 4 THR N 78 MET N 83 -1 O MET N 83 N LEU N 18 SHEET 4 AE3 4 THR N 69 ASP N 73 -1 N SER N 71 O ALA N 80 SHEET 1 AE4 8 LEU N 11 GLN N 13 0 SHEET 2 AE4 8 THR N 115 SER N 120 1 O THR N 118 N VAL N 12 SHEET 3 AE4 8 ALA N 92 ASP N 99 -1 N TYR N 94 O THR N 115 SHEET 4 AE4 8 VAL N 33 GLN N 39 -1 N PHE N 37 O TYR N 95 SHEET 5 AE4 8 GLU N 46 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AE4 8 ASN N 57 TYR N 60 -1 O TYR N 59 N ALA N 50 SHEET 7 AE4 8 SER X 17 SER X 25 -1 O SER X 17 N SER N 58 SHEET 8 AE4 8 GLN X 3 SER X 7 -1 N GLN X 3 O SER X 25 SHEET 1 AE5 8 TYR N 110 TRP N 111 0 SHEET 2 AE5 8 ALA N 92 ASP N 99 -1 N ALA N 98 O TYR N 110 SHEET 3 AE5 8 VAL N 33 GLN N 39 -1 N PHE N 37 O TYR N 95 SHEET 4 AE5 8 GLU N 46 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 5 AE5 8 ASN N 57 TYR N 60 -1 O TYR N 59 N ALA N 50 SHEET 6 AE5 8 SER X 17 SER X 25 -1 O SER X 17 N SER N 58 SHEET 7 AE5 8 THR X 78 MET X 83 -1 O MET X 83 N LEU X 18 SHEET 8 AE5 8 PHE X 68 ASP X 73 -1 N THR X 69 O GLN X 82 SHEET 1 AE6 6 ILE O 35 TYR O 40 0 SHEET 2 AE6 6 THR O 2 GLY O 7 1 N LEU O 4 O LYS O 36 SHEET 3 AE6 6 ILE O 62 ALA O 65 1 O ILE O 62 N LYS O 5 SHEET 4 AE6 6 ASN O 201 SER O 217 -1 O MET O 213 N ALA O 65 SHEET 5 AE6 6 TRP O 114 SER O 129 -1 N THR O 127 O ALA O 203 SHEET 6 AE6 6 GLY O 182 PRO O 186 -1 O ASN O 185 N GLU O 126 SHEET 1 AE7 5 ILE O 35 TYR O 40 0 SHEET 2 AE7 5 THR O 2 GLY O 7 1 N LEU O 4 O LYS O 36 SHEET 3 AE7 5 ILE O 62 ALA O 65 1 O ILE O 62 N LYS O 5 SHEET 4 AE7 5 ASN O 201 SER O 217 -1 O MET O 213 N ALA O 65 SHEET 5 AE7 5 ASN O 264 THR O 266 1 O THR O 266 N LEU O 202 SHEET 1 AE8 2 LYS O 143 VAL O 146 0 SHEET 2 AE8 2 SER O 162 PRO O 165 1 O THR O 164 N LEU O 144 SHEET 1 AE9 8 VAL P 2 SER P 7 0 SHEET 2 AE9 8 SER P 17 GLY P 26 -1 O SER P 21 N SER P 7 SHEET 3 AE9 8 ASN T 57 TYR T 60 -1 O SER T 58 N SER P 17 SHEET 4 AE9 8 GLU T 46 ILE T 51 -1 N ALA T 50 O TYR T 59 SHEET 5 AE9 8 VAL T 33 GLN T 39 -1 N TRP T 36 O ALA T 49 SHEET 6 AE9 8 ALA T 92 ASP T 99 -1 O TYR T 95 N PHE T 37 SHEET 7 AE9 8 THR T 115 SER T 120 -1 O VAL T 117 N ALA T 92 SHEET 8 AE9 8 LEU T 11 GLN T 13 1 N VAL T 12 O THR T 118 SHEET 1 AF1 8 PHE P 68 ASP P 73 0 SHEET 2 AF1 8 THR P 78 MET P 83 -1 O GLN P 82 N THR P 69 SHEET 3 AF1 8 SER P 17 GLY P 26 -1 N LEU P 20 O LEU P 81 SHEET 4 AF1 8 ASN T 57 TYR T 60 -1 O SER T 58 N SER P 17 SHEET 5 AF1 8 GLU T 46 ILE T 51 -1 N ALA T 50 O TYR T 59 SHEET 6 AF1 8 VAL T 33 GLN T 39 -1 N TRP T 36 O ALA T 49 SHEET 7 AF1 8 ALA T 92 ASP T 99 -1 O TYR T 95 N PHE T 37 SHEET 8 AF1 8 TYR T 110 TRP T 111 -1 O TYR T 110 N ALA T 98 SHEET 1 AF2 6 LEU P 11 GLN P 13 0 SHEET 2 AF2 6 THR P 115 SER P 120 1 O THR P 118 N VAL P 12 SHEET 3 AF2 6 ALA P 92 ASP P 99 -1 N TYR P 94 O THR P 115 SHEET 4 AF2 6 VAL P 33 GLN P 39 -1 N PHE P 37 O TYR P 95 SHEET 5 AF2 6 ARG P 45 ILE P 51 -1 O GLU P 46 N ARG P 38 SHEET 6 AF2 6 SER P 58 TYR P 60 -1 O TYR P 59 N ALA P 50 SHEET 1 AF3 4 LEU P 11 GLN P 13 0 SHEET 2 AF3 4 THR P 115 SER P 120 1 O THR P 118 N VAL P 12 SHEET 3 AF3 4 ALA P 92 ASP P 99 -1 N TYR P 94 O THR P 115 SHEET 4 AF3 4 TYR P 110 TRP P 111 -1 O TYR P 110 N ALA P 98 SHEET 1 AF4 6 ILE Q 35 TYR Q 40 0 SHEET 2 AF4 6 THR Q 2 GLY Q 7 1 N LEU Q 4 O LYS Q 36 SHEET 3 AF4 6 ILE Q 62 ALA Q 65 1 O ILE Q 62 N LYS Q 5 SHEET 4 AF4 6 VAL Q 209 SER Q 217 -1 O MET Q 213 N ALA Q 65 SHEET 5 AF4 6 TRP Q 114 SER Q 129 -1 N LEU Q 117 O VAL Q 214 SHEET 6 AF4 6 GLY Q 182 PRO Q 186 -1 O GLN Q 183 N THR Q 128 SHEET 1 AF5 7 ILE Q 35 TYR Q 40 0 SHEET 2 AF5 7 THR Q 2 GLY Q 7 1 N LEU Q 4 O LYS Q 36 SHEET 3 AF5 7 ILE Q 62 ALA Q 65 1 O ILE Q 62 N LYS Q 5 SHEET 4 AF5 7 VAL Q 209 SER Q 217 -1 O MET Q 213 N ALA Q 65 SHEET 5 AF5 7 TRP Q 114 SER Q 129 -1 N LEU Q 117 O VAL Q 214 SHEET 6 AF5 7 ASN Q 201 ALA Q 203 -1 O ALA Q 203 N THR Q 127 SHEET 7 AF5 7 ASN Q 264 THR Q 266 1 O THR Q 266 N LEU Q 202 SHEET 1 AF6 2 LYS Q 143 VAL Q 146 0 SHEET 2 AF6 2 SER Q 162 PRO Q 165 1 O THR Q 164 N LEU Q 144 SHEET 1 AF7 8 VAL R 2 SER R 7 0 SHEET 2 AF7 8 SER R 17 GLY R 26 -1 O SER R 21 N SER R 7 SHEET 3 AF7 8 ASN V 57 TYR V 60 -1 O SER V 58 N SER R 17 SHEET 4 AF7 8 ARG V 45 ILE V 51 -1 N ALA V 50 O TYR V 59 SHEET 5 AF7 8 VAL V 33 GLN V 39 -1 N ARG V 38 O GLU V 46 SHEET 6 AF7 8 ALA V 92 ASP V 99 -1 O TYR V 95 N PHE V 37 SHEET 7 AF7 8 THR V 115 SER V 120 -1 O VAL V 117 N ALA V 92 SHEET 8 AF7 8 LEU V 11 GLN V 13 1 N VAL V 12 O THR V 118 SHEET 1 AF8 8 PHE R 68 ASP R 73 0 SHEET 2 AF8 8 THR R 78 MET R 83 -1 O GLN R 82 N THR R 69 SHEET 3 AF8 8 SER R 17 GLY R 26 -1 N LEU R 18 O MET R 83 SHEET 4 AF8 8 ASN V 57 TYR V 60 -1 O SER V 58 N SER R 17 SHEET 5 AF8 8 ARG V 45 ILE V 51 -1 N ALA V 50 O TYR V 59 SHEET 6 AF8 8 VAL V 33 GLN V 39 -1 N ARG V 38 O GLU V 46 SHEET 7 AF8 8 ALA V 92 ASP V 99 -1 O TYR V 95 N PHE V 37 SHEET 8 AF8 8 TYR V 110 TRP V 111 -1 O TYR V 110 N ALA V 98 SHEET 1 AF9 6 LEU R 11 GLN R 13 0 SHEET 2 AF9 6 THR R 115 SER R 120 1 O SER R 120 N VAL R 12 SHEET 3 AF9 6 ALA R 92 ASP R 99 -1 N ALA R 92 O VAL R 117 SHEET 4 AF9 6 VAL R 33 GLN R 39 -1 N PHE R 37 O TYR R 95 SHEET 5 AF9 6 GLU R 46 ILE R 51 -1 O ALA R 49 N TRP R 36 SHEET 6 AF9 6 SER R 58 TYR R 60 -1 O TYR R 59 N ALA R 50 SHEET 1 AG1 4 LEU R 11 GLN R 13 0 SHEET 2 AG1 4 THR R 115 SER R 120 1 O SER R 120 N VAL R 12 SHEET 3 AG1 4 ALA R 92 ASP R 99 -1 N ALA R 92 O VAL R 117 SHEET 4 AG1 4 TYR R 110 TRP R 111 -1 O TYR R 110 N ALA R 98 SHEET 1 AG2 4 VAL T 2 SER T 7 0 SHEET 2 AG2 4 LEU T 18 GLY T 26 -1 O SER T 21 N SER T 7 SHEET 3 AG2 4 THR T 78 MET T 83 -1 O MET T 83 N LEU T 18 SHEET 4 AG2 4 PHE T 68 ASP T 73 -1 N THR T 69 O GLN T 82 SHEET 1 AG3 6 ILE U 35 TYR U 40 0 SHEET 2 AG3 6 THR U 2 GLY U 7 1 N LEU U 4 O ALA U 38 SHEET 3 AG3 6 ILE U 62 ALA U 65 1 O ILE U 62 N LYS U 5 SHEET 4 AG3 6 ASN U 201 SER U 217 -1 O MET U 213 N ALA U 65 SHEET 5 AG3 6 TRP U 114 SER U 129 -1 N THR U 127 O ALA U 203 SHEET 6 AG3 6 GLY U 182 PRO U 186 -1 O ASN U 185 N GLU U 126 SHEET 1 AG4 5 ILE U 35 TYR U 40 0 SHEET 2 AG4 5 THR U 2 GLY U 7 1 N LEU U 4 O ALA U 38 SHEET 3 AG4 5 ILE U 62 ALA U 65 1 O ILE U 62 N LYS U 5 SHEET 4 AG4 5 ASN U 201 SER U 217 -1 O MET U 213 N ALA U 65 SHEET 5 AG4 5 ASN U 264 THR U 266 1 O THR U 266 N LEU U 202 SHEET 1 AG5 2 LYS U 143 VAL U 146 0 SHEET 2 AG5 2 SER U 162 PRO U 165 1 O THR U 164 N LEU U 144 SHEET 1 AG6 4 VAL V 2 SER V 7 0 SHEET 2 AG6 4 LEU V 18 GLY V 26 -1 O SER V 25 N GLN V 3 SHEET 3 AG6 4 THR V 78 MET V 83 -1 O MET V 83 N LEU V 18 SHEET 4 AG6 4 PHE V 68 ASP V 73 -1 N SER V 71 O ALA V 80 SHEET 1 AG7 6 LYS W 36 TYR W 40 0 SHEET 2 AG7 6 THR W 3 GLY W 7 1 N LEU W 4 O ALA W 38 SHEET 3 AG7 6 ILE W 62 ALA W 65 1 O ILE W 62 N LYS W 5 SHEET 4 AG7 6 VAL W 209 SER W 217 -1 O MET W 213 N ALA W 65 SHEET 5 AG7 6 TRP W 114 SER W 129 -1 N LEU W 117 O VAL W 214 SHEET 6 AG7 6 GLY W 182 PRO W 186 -1 O GLN W 183 N THR W 128 SHEET 1 AG8 7 LYS W 36 TYR W 40 0 SHEET 2 AG8 7 THR W 3 GLY W 7 1 N LEU W 4 O ALA W 38 SHEET 3 AG8 7 ILE W 62 ALA W 65 1 O ILE W 62 N LYS W 5 SHEET 4 AG8 7 VAL W 209 SER W 217 -1 O MET W 213 N ALA W 65 SHEET 5 AG8 7 TRP W 114 SER W 129 -1 N LEU W 117 O VAL W 214 SHEET 6 AG8 7 ASN W 201 ALA W 203 -1 O ALA W 203 N THR W 127 SHEET 7 AG8 7 ASN W 264 VAL W 265 1 O ASN W 264 N LEU W 202 SHEET 1 AG9 2 LYS W 143 VAL W 146 0 SHEET 2 AG9 2 SER W 162 PRO W 165 1 O THR W 164 N LEU W 144 SHEET 1 AH1 6 LEU X 11 GLN X 13 0 SHEET 2 AH1 6 THR X 115 SER X 120 1 O THR X 118 N VAL X 12 SHEET 3 AH1 6 ALA X 92 ASP X 99 -1 N ALA X 92 O VAL X 117 SHEET 4 AH1 6 VAL X 33 GLN X 39 -1 N PHE X 37 O TYR X 95 SHEET 5 AH1 6 GLU X 46 ILE X 51 -1 O GLU X 46 N ARG X 38 SHEET 6 AH1 6 SER X 58 TYR X 60 -1 O TYR X 59 N ALA X 50 SHEET 1 AH2 4 LEU X 11 GLN X 13 0 SHEET 2 AH2 4 THR X 115 SER X 120 1 O THR X 118 N VAL X 12 SHEET 3 AH2 4 ALA X 92 ASP X 99 -1 N ALA X 92 O VAL X 117 SHEET 4 AH2 4 TYR X 110 TRP X 111 -1 O TYR X 110 N ALA X 98 SHEET 1 AH3 6 ILE Y 35 TYR Y 40 0 SHEET 2 AH3 6 THR Y 2 GLY Y 7 1 N LEU Y 4 O LYS Y 36 SHEET 3 AH3 6 ILE Y 62 ALA Y 65 1 O ILE Y 62 N LYS Y 5 SHEET 4 AH3 6 ASN Y 201 SER Y 217 -1 O MET Y 213 N ALA Y 65 SHEET 5 AH3 6 TRP Y 114 SER Y 129 -1 N THR Y 127 O ALA Y 203 SHEET 6 AH3 6 GLY Y 182 PRO Y 186 -1 O GLN Y 183 N THR Y 128 SHEET 1 AH4 5 ILE Y 35 TYR Y 40 0 SHEET 2 AH4 5 THR Y 2 GLY Y 7 1 N LEU Y 4 O LYS Y 36 SHEET 3 AH4 5 ILE Y 62 ALA Y 65 1 O ILE Y 62 N LYS Y 5 SHEET 4 AH4 5 ASN Y 201 SER Y 217 -1 O MET Y 213 N ALA Y 65 SHEET 5 AH4 5 ASN Y 264 THR Y 266 1 O ASN Y 264 N LEU Y 202 SHEET 1 AH5 2 LYS Y 143 VAL Y 146 0 SHEET 2 AH5 2 SER Y 162 PRO Y 165 1 O THR Y 164 N LEU Y 144 SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.04 SSBOND 2 CYS D 22 CYS D 96 1555 1555 2.04 SSBOND 3 CYS F 22 CYS F 96 1555 1555 2.04 SSBOND 4 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 5 CYS J 22 CYS J 96 1555 1555 2.04 SSBOND 6 CYS L 22 CYS L 96 1555 1555 2.04 SSBOND 7 CYS N 22 CYS N 96 1555 1555 2.04 SSBOND 8 CYS P 22 CYS P 96 1555 1555 2.04 SSBOND 9 CYS R 22 CYS R 96 1555 1555 2.03 SSBOND 10 CYS T 22 CYS T 96 1555 1555 2.04 SSBOND 11 CYS V 22 CYS V 96 1555 1555 2.04 SSBOND 12 CYS X 22 CYS X 96 1555 1555 2.04 CRYST1 223.570 153.113 210.487 90.00 90.00 90.00 C 1 2 1 48 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.004473 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006531 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004751 0.00000 MTRIX1 1 -0.521828 0.738052 0.427756 -161.16017 1 MTRIX2 1 -0.672434 -0.047336 -0.738642 -3.10197 1 MTRIX3 1 -0.524908 -0.673081 0.520993 -61.86872 1 MTRIX1 2 0.534726 -0.763743 -0.361613 44.64077 1 MTRIX2 2 -0.575587 -0.015884 -0.817586 13.11108 1 MTRIX3 2 0.618682 0.645325 -0.448094 171.76835 1 MTRIX1 3 -0.457440 -0.743925 -0.487158 -112.04403 1 MTRIX2 3 0.772521 -0.061134 -0.632040 147.60232 1 MTRIX3 3 0.440408 -0.665461 0.602663 -10.78812 1 MTRIX1 4 0.451181 0.718765 0.528972 -3.80499 1 MTRIX2 4 0.787366 -0.041576 -0.615082 155.48845 1 MTRIX3 4 -0.420108 0.694009 -0.584689 119.02634 1 MTRIX1 5 0.344225 -0.650822 0.676713 -137.83605 1 MTRIX2 5 -0.849484 0.091070 0.519695 -159.76287 1 MTRIX3 5 -0.399858 -0.753749 -0.521514 3.72792 1 MTRIX1 6 -0.388903 0.682166 -0.619197 18.49671 1 MTRIX2 6 -0.790550 0.098011 0.604504 -156.27965 1 MTRIX3 6 0.473060 0.724599 0.501169 109.49553 1 MTRIX1 7 0.624137 0.636958 -0.452479 64.77594 1 MTRIX2 7 0.555438 0.045572 0.830308 -19.53491 1 MTRIX3 7 0.549492 -0.769550 -0.325347 150.02177 1 MTRIX1 8 -0.611235 -0.630260 0.478711 -175.89192 1 MTRIX2 8 0.592624 0.036437 0.804655 -20.61872 1 MTRIX3 8 -0.524584 0.775529 0.351235 -43.69011 1 MTRIX1 9 0.129471 -0.104101 -0.986104 5.36406 1 MTRIX2 9 -0.050289 -0.993883 0.098320 -98.68497 1 MTRIX3 9 -0.990307 0.036861 -0.133914 -100.86723 1 MTRIX1 10 -0.980209 0.030800 -0.195556 -97.85484 1 MTRIX2 10 0.059305 0.988142 -0.141629 14.59834 1 MTRIX3 10 0.188875 -0.150424 -0.970412 118.55963 1 MTRIX1 11 -0.151255 0.051804 0.987136 -121.51556 1 MTRIX2 11 -0.044930 -0.997954 0.045487 -88.61673 1 MTRIX3 11 0.987473 -0.037472 0.153273 204.33495 1 MTRIX1 12 -0.512854 0.716101 0.473477 -164.42665 1 MTRIX2 12 -0.707760 -0.040553 -0.705288 -9.41124 1 MTRIX3 12 -0.485856 -0.696818 0.527625 -59.00627 1 MTRIX1 13 0.475693 -0.796380 -0.373491 38.20662 1 MTRIX2 13 -0.599095 0.017565 -0.800485 10.01309 1 MTRIX3 13 0.644051 0.604542 -0.468751 174.88004 1 MTRIX1 14 -0.477295 -0.749559 -0.458641 -116.60785 1 MTRIX2 14 0.748205 -0.072929 -0.659447 146.69291 1 MTRIX3 14 0.460846 -0.657908 0.595632 -7.56456 1 MTRIX1 15 0.475864 0.715395 0.511629 0.43313 1 MTRIX2 15 0.754966 -0.033827 -0.654891 155.41167 1 MTRIX3 15 -0.451199 0.697901 -0.556196 113.41517 1 MTRIX1 16 0.394747 -0.657052 0.642228 -129.68752 1 MTRIX2 16 -0.801500 0.095476 0.590324 -159.89274 1 MTRIX3 16 -0.449191 -0.747775 -0.488938 -4.20031 1 MTRIX1 17 -0.377796 0.699514 -0.606589 19.04849 1 MTRIX2 17 -0.760019 0.139884 0.634668 -154.07514 1 MTRIX3 17 0.528811 0.700794 0.478797 116.65928 1 MTRIX1 18 0.593185 0.635145 -0.494694 64.72697 1 MTRIX2 18 0.614989 0.039052 0.787568 -9.49516 1 MTRIX3 18 0.519538 -0.771405 -0.367442 150.09875 1 MTRIX1 19 -0.577697 -0.625947 0.523886 -175.61907 1 MTRIX2 19 0.643857 0.045051 0.763818 -11.30507 1 MTRIX3 19 -0.501712 0.778563 0.376995 -43.20184 1 MTRIX1 20 -0.095278 0.065761 0.993276 -115.35828 1 MTRIX2 20 -0.071464 -0.995693 0.059065 -92.30234 1 MTRIX3 20 0.992882 -0.065356 0.099567 208.45075 1 MTRIX1 21 0.076076 -0.104272 -0.991635 -0.13627 1 MTRIX2 21 -0.058393 -0.993276 0.099965 -99.60979 1 MTRIX3 21 -0.995391 0.050300 -0.081653 -105.24119 1 MTRIX1 22 -0.988753 0.043623 -0.143057 -102.68972 1 MTRIX2 22 0.064180 0.987727 -0.142394 15.13634 1 MTRIX3 22 0.135089 -0.149973 -0.979418 113.29309 1