HEADER IMMUNE SYSTEM 20-OCT-23 8UP2 TITLE MURINE FAB JAR 4 BOUND TO MENINGOCOCCAL FACTOR H BINDING PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUMAN-MOUSE CHIMERIC IMMUNOGLOBULIN HEAVY CHAIN, FD COMPND 3 FRAGMENT; COMPND 4 CHAIN: A, D; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HUMAN-MOUSE CHIMERIC IMMUNOGLOBULIN, KAPPA LIGHT CHAIN; COMPND 8 CHAIN: B, E; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: FACTOR H BINDING PROTEIN, SEQUENCE VARIANT ID 1; COMPND 12 CHAIN: C, F; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_COMMON: MOUSE; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS; SOURCE 15 ORGANISM_TAXID: 487; SOURCE 16 GENE: FHBP; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, FAB, ANTIGEN, FACTOR H BINDING PROTEIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR P.T.BEERNINK,B.P.BEERNINK REVDAT 1 16-OCT-24 8UP2 0 JRNL AUTH P.T.BEERNINK,B.P.BEERNINK JRNL TITL STRUCTURE OF MURINE FAB JAR 4 BOUND TO FHBP AT JRNL TITL 2 1.60-ANGSTROMS RESOLUTION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.43 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 218452 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.188 REMARK 3 R VALUE (WORKING SET) : 0.187 REMARK 3 FREE R VALUE : 0.212 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.920 REMARK 3 FREE R VALUE TEST SET COUNT : 2014 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 74.4300 - 3.8600 1.00 15811 151 0.1552 0.1402 REMARK 3 2 3.8600 - 3.0700 1.00 15575 147 0.1729 0.1830 REMARK 3 3 3.0700 - 2.6800 1.00 15533 144 0.1842 0.2483 REMARK 3 4 2.6800 - 2.4300 1.00 15521 143 0.1974 0.2341 REMARK 3 5 2.4300 - 2.2600 1.00 15412 144 0.1881 0.2516 REMARK 3 6 2.2600 - 2.1300 1.00 15440 141 0.1975 0.2553 REMARK 3 7 2.1300 - 2.0200 1.00 15408 148 0.1899 0.2238 REMARK 3 8 2.0200 - 1.9300 1.00 15388 143 0.1997 0.2048 REMARK 3 9 1.9300 - 1.8600 1.00 15369 143 0.2071 0.2905 REMARK 3 10 1.8600 - 1.7900 1.00 15435 141 0.2382 0.3385 REMARK 3 11 1.7900 - 1.7400 1.00 15380 144 0.2302 0.2769 REMARK 3 12 1.7400 - 1.6900 1.00 15359 143 0.2372 0.2732 REMARK 3 13 1.6900 - 1.6400 1.00 15390 139 0.2384 0.2695 REMARK 3 14 1.6400 - 1.6000 0.99 15417 143 0.2653 0.2968 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.172 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.418 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.87 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.87 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 : 0.011 10396 REMARK 3 ANGLE : 1.102 14069 REMARK 3 CHIRALITY : 0.064 1576 REMARK 3 PLANARITY : 0.019 1805 REMARK 3 DIHEDRAL : 14.860 3776 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 : 3 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 1 through 9 or REMARK 3 resid 11 through 53 or resid 55 through REMARK 3 218)) 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" and (resid 1 through 9 or REMARK 3 resid 11 through 53 or resid 55 through REMARK 3 218)) 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 216) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "E" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 14 through 32 or REMARK 3 resid 34 through 256 or resid 302)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "F" and (resid 14 through 32 or REMARK 3 resid 34 through 301)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8UP2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-23. REMARK 100 THE DEPOSITION ID IS D_1000277217. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-JUN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.3.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.116 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 218509 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 74.430 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 9.400 REMARK 200 R MERGE (I) : 0.16420 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.8400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5 REMARK 200 DATA REDUNDANCY IN SHELL : 6.10 REMARK 200 R MERGE FOR SHELL (I) : 1.36600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.320 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M NAOAC 20% PEG 4,000 0.085M TRIS REMARK 280 CL, PH 8.5 15% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 33.72000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F 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 SER A 132 REMARK 465 SER A 133 REMARK 465 LYS A 134 REMARK 465 SER A 135 REMARK 465 THR A 136 REMARK 465 SER A 137 REMARK 465 GLY A 138 REMARK 465 GLY A 139 REMARK 465 THR A 140 REMARK 465 LYS A 219 REMARK 465 SER A 220 REMARK 465 CYS A 221 REMARK 465 ASP A 222 REMARK 465 LYS A 223 REMARK 465 GLU B 218 REMARK 465 CYS B 219 REMARK 465 SER B 220 REMARK 465 MET C 7 REMARK 465 VAL C 8 REMARK 465 ALA C 9 REMARK 465 ALA C 10 REMARK 465 ASP C 11 REMARK 465 ILE C 12 REMARK 465 GLU C 118 REMARK 465 HIS C 119 REMARK 465 SER C 120 REMARK 465 GLU C 257 REMARK 465 HIS C 258 REMARK 465 HIS C 259 REMARK 465 HIS C 260 REMARK 465 HIS C 261 REMARK 465 HIS C 262 REMARK 465 HIS C 263 REMARK 465 SER D 132 REMARK 465 SER D 133 REMARK 465 LYS D 134 REMARK 465 SER D 135 REMARK 465 THR D 136 REMARK 465 SER D 137 REMARK 465 GLY D 138 REMARK 465 GLY D 139 REMARK 465 THR D 140 REMARK 465 LYS D 219 REMARK 465 SER D 220 REMARK 465 CYS D 221 REMARK 465 ASP D 222 REMARK 465 LYS D 223 REMARK 465 GLY E 217 REMARK 465 GLU E 218 REMARK 465 CYS E 219 REMARK 465 SER E 220 REMARK 465 MET F 7 REMARK 465 VAL F 8 REMARK 465 ALA F 9 REMARK 465 ALA F 10 REMARK 465 ASP F 11 REMARK 465 ILE F 12 REMARK 465 GLU F 118 REMARK 465 HIS F 119 REMARK 465 SER F 120 REMARK 465 GLU F 257 REMARK 465 HIS F 258 REMARK 465 HIS F 259 REMARK 465 HIS F 260 REMARK 465 HIS F 261 REMARK 465 HIS F 262 REMARK 465 HIS F 263 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 OD1 ASP B 175 HG1 THR B 177 1.59 REMARK 500 OE2 GLU C 92 OG1 THR C 111 2.13 REMARK 500 O HOH C 545 O HOH C 552 2.17 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 ASP A 99 122.16 -36.34 REMARK 500 ASP A 149 61.47 69.68 REMARK 500 THR A 196 -60.73 -92.70 REMARK 500 VAL B 56 -49.38 75.22 REMARK 500 ASN B 143 65.47 63.66 REMARK 500 ASN B 157 -0.98 75.78 REMARK 500 ASN C 43 1.72 80.97 REMARK 500 GLN C 216 -3.49 63.58 REMARK 500 LYS C 219 17.30 -142.86 REMARK 500 ALA D 92 169.44 179.76 REMARK 500 ASP D 99 123.24 -37.25 REMARK 500 ASP D 149 61.83 72.29 REMARK 500 THR D 196 -64.30 -94.58 REMARK 500 VAL E 56 -49.36 73.71 REMARK 500 ASN E 143 63.50 61.88 REMARK 500 ASN F 43 -2.47 79.13 REMARK 500 GLN F 101 -169.52 -113.52 REMARK 500 LYS F 219 21.15 -143.83 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 C 41 0.28 SIDE CHAIN REMARK 500 ARG E 82 0.10 SIDE CHAIN REMARK 500 ARG F 41 0.30 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 8UP2 A 1 223 PDB 8UP2 8UP2 1 223 DBREF 8UP2 B 1 220 PDB 8UP2 8UP2 1 220 DBREF 8UP2 C 8 255 UNP Q6VRZ6 Q6VRZ6_NEIME 8 255 DBREF 8UP2 D 1 223 PDB 8UP2 8UP2 1 223 DBREF 8UP2 E 1 220 PDB 8UP2 8UP2 1 220 DBREF 8UP2 F 8 255 UNP Q6VRZ6 Q6VRZ6_NEIME 8 255 SEQADV 8UP2 MET C 7 UNP Q6VRZ6 INITIATING METHIONINE SEQADV 8UP2 LEU C 256 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 GLU C 257 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS C 258 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS C 259 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS C 260 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS C 261 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS C 262 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS C 263 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 MET F 7 UNP Q6VRZ6 INITIATING METHIONINE SEQADV 8UP2 LEU F 256 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 GLU F 257 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS F 258 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS F 259 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS F 260 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS F 261 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS F 262 UNP Q6VRZ6 EXPRESSION TAG SEQADV 8UP2 HIS F 263 UNP Q6VRZ6 EXPRESSION TAG SEQRES 1 A 223 GLU VAL GLN LEU GLN GLN SER GLY PRO VAL LEU VAL LYS SEQRES 2 A 223 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 A 223 TYR THR PHE THR ASP TYR TYR MET ASN TRP VAL LYS GLN SEQRES 4 A 223 SER HIS GLY LYS SER LEU GLU TRP ILE GLY ARG VAL ASN SEQRES 5 A 223 PRO SER ASN GLY ALA THR THR TYR ASN GLN LYS PHE LYS SEQRES 6 A 223 GLY LYS ALA THR VAL THR VAL ASP LYS SER LEU SER THR SEQRES 7 A 223 SER TYR MET GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 A 223 ALA VAL TYR PHE CYS ALA ARG ASP TRP GLU GLY PRO TRP SEQRES 9 A 223 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 A 223 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 A 223 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 A 223 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 A 223 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 A 223 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 A 223 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 A 223 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 A 223 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 A 223 ASP LYS SEQRES 1 B 220 ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SER VAL SEQRES 2 B 220 THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 B 220 GLN THR LEU PHE TYR SER LYS GLY LYS THR TYR LEU ASN SEQRES 4 B 220 TRP LEU PHE GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5 B 220 ILE TYR LEU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 B 220 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 B 220 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 B 220 TYR CYS LEU GLN SER THR HIS PHE PRO TYR THR PHE GLY SEQRES 9 B 220 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 B 220 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 B 220 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 B 220 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 B 220 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 B 220 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 B 220 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 B 220 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 B 220 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SER SEQRES 1 C 257 MET VAL ALA ALA ASP ILE GLY ALA GLY LEU ALA ASP ALA SEQRES 2 C 257 LEU THR ALA PRO LEU ASP HIS LYS ASP LYS GLY LEU GLN SEQRES 3 C 257 SER LEU THR LEU ASP GLN SER VAL ARG LYS ASN GLU LYS SEQRES 4 C 257 LEU LYS LEU ALA ALA GLN GLY ALA GLU LYS THR TYR GLY SEQRES 5 C 257 ASN GLY ASP SER LEU ASN THR GLY LYS LEU LYS ASN ASP SEQRES 6 C 257 LYS VAL SER ARG PHE ASP PHE ILE ARG GLN ILE GLU VAL SEQRES 7 C 257 ASP GLY GLN LEU ILE THR LEU GLU SER GLY GLU PHE GLN SEQRES 8 C 257 VAL TYR LYS GLN SER HIS SER ALA LEU THR ALA PHE GLN SEQRES 9 C 257 THR GLU GLN ILE GLN ASP SER GLU HIS SER GLY LYS MET SEQRES 10 C 257 VAL ALA LYS ARG GLN PHE ARG ILE GLY ASP ILE ALA GLY SEQRES 11 C 257 GLU HIS THR SER PHE ASP LYS LEU PRO GLU GLY GLY ARG SEQRES 12 C 257 ALA THR TYR ARG GLY THR ALA PHE GLY SER ASP ASP ALA SEQRES 13 C 257 GLY GLY LYS LEU THR TYR THR ILE ASP PHE ALA ALA LYS SEQRES 14 C 257 GLN GLY ASN GLY LYS ILE GLU HIS LEU LYS SER PRO GLU SEQRES 15 C 257 LEU ASN VAL ASP LEU ALA ALA ALA ASP ILE LYS PRO ASP SEQRES 16 C 257 GLY LYS ARG HIS ALA VAL ILE SER GLY SER VAL LEU TYR SEQRES 17 C 257 ASN GLN ALA GLU LYS GLY SER TYR SER LEU GLY ILE PHE SEQRES 18 C 257 GLY GLY LYS ALA GLN GLU VAL ALA GLY SER ALA GLU VAL SEQRES 19 C 257 LYS THR VAL ASN GLY ILE ARG HIS ILE GLY LEU ALA ALA SEQRES 20 C 257 LYS GLN LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 1 D 223 GLU VAL GLN LEU GLN GLN SER GLY PRO VAL LEU VAL LYS SEQRES 2 D 223 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 D 223 TYR THR PHE THR ASP TYR TYR MET ASN TRP VAL LYS GLN SEQRES 4 D 223 SER HIS GLY LYS SER LEU GLU TRP ILE GLY ARG VAL ASN SEQRES 5 D 223 PRO SER ASN GLY ALA THR THR TYR ASN GLN LYS PHE LYS SEQRES 6 D 223 GLY LYS ALA THR VAL THR VAL ASP LYS SER LEU SER THR SEQRES 7 D 223 SER TYR MET GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 D 223 ALA VAL TYR PHE CYS ALA ARG ASP TRP GLU GLY PRO TRP SEQRES 9 D 223 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 D 223 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 D 223 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 D 223 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 D 223 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 D 223 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 D 223 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 D 223 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 D 223 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 D 223 ASP LYS SEQRES 1 E 220 ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SER VAL SEQRES 2 E 220 THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 E 220 GLN THR LEU PHE TYR SER LYS GLY LYS THR TYR LEU ASN SEQRES 4 E 220 TRP LEU PHE GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5 E 220 ILE TYR LEU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 E 220 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 E 220 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 E 220 TYR CYS LEU GLN SER THR HIS PHE PRO TYR THR PHE GLY SEQRES 9 E 220 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 E 220 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 E 220 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 E 220 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 E 220 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 E 220 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 E 220 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 E 220 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 E 220 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SER SEQRES 1 F 257 MET VAL ALA ALA ASP ILE GLY ALA GLY LEU ALA ASP ALA SEQRES 2 F 257 LEU THR ALA PRO LEU ASP HIS LYS ASP LYS GLY LEU GLN SEQRES 3 F 257 SER LEU THR LEU ASP GLN SER VAL ARG LYS ASN GLU LYS SEQRES 4 F 257 LEU LYS LEU ALA ALA GLN GLY ALA GLU LYS THR TYR GLY SEQRES 5 F 257 ASN GLY ASP SER LEU ASN THR GLY LYS LEU LYS ASN ASP SEQRES 6 F 257 LYS VAL SER ARG PHE ASP PHE ILE ARG GLN ILE GLU VAL SEQRES 7 F 257 ASP GLY GLN LEU ILE THR LEU GLU SER GLY GLU PHE GLN SEQRES 8 F 257 VAL TYR LYS GLN SER HIS SER ALA LEU THR ALA PHE GLN SEQRES 9 F 257 THR GLU GLN ILE GLN ASP SER GLU HIS SER GLY LYS MET SEQRES 10 F 257 VAL ALA LYS ARG GLN PHE ARG ILE GLY ASP ILE ALA GLY SEQRES 11 F 257 GLU HIS THR SER PHE ASP LYS LEU PRO GLU GLY GLY ARG SEQRES 12 F 257 ALA THR TYR ARG GLY THR ALA PHE GLY SER ASP ASP ALA SEQRES 13 F 257 GLY GLY LYS LEU THR TYR THR ILE ASP PHE ALA ALA LYS SEQRES 14 F 257 GLN GLY ASN GLY LYS ILE GLU HIS LEU LYS SER PRO GLU SEQRES 15 F 257 LEU ASN VAL ASP LEU ALA ALA ALA ASP ILE LYS PRO ASP SEQRES 16 F 257 GLY LYS ARG HIS ALA VAL ILE SER GLY SER VAL LEU TYR SEQRES 17 F 257 ASN GLN ALA GLU LYS GLY SER TYR SER LEU GLY ILE PHE SEQRES 18 F 257 GLY GLY LYS ALA GLN GLU VAL ALA GLY SER ALA GLU VAL SEQRES 19 F 257 LYS THR VAL ASN GLY ILE ARG HIS ILE GLY LEU ALA ALA SEQRES 20 F 257 LYS GLN LEU GLU HIS HIS HIS HIS HIS HIS HET GOL C 301 14 HET ACT D 301 7 HET GOL F 301 14 HETNAM GOL GLYCEROL HETNAM ACT ACETATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 GOL 2(C3 H8 O3) FORMUL 8 ACT C2 H3 O2 1- FORMUL 10 HOH *1015(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 GLN A 62 LYS A 65 5 4 HELIX 3 AA3 LYS A 74 LEU A 76 5 3 HELIX 4 AA4 THR A 87 SER A 91 5 5 HELIX 5 AA5 SER A 161 ALA A 163 5 3 HELIX 6 AA6 PRO A 190 GLY A 195 5 6 HELIX 7 AA7 LYS A 206 ASN A 209 5 4 HELIX 8 AA8 GLU B 84 LEU B 88 5 5 HELIX 9 AA9 SER B 126 SER B 132 1 7 HELIX 10 AB1 LYS B 188 HIS B 194 1 7 HELIX 11 AB2 GLY C 15 ALA C 22 1 8 HELIX 12 AB3 ASN C 64 LEU C 68 5 5 HELIX 13 AB4 SER C 140 LEU C 144 5 5 HELIX 14 AB5 SER C 186 ASN C 190 5 5 HELIX 15 AB6 THR D 28 TYR D 32 5 5 HELIX 16 AB7 GLN D 62 LYS D 65 5 4 HELIX 17 AB8 LYS D 74 LEU D 76 5 3 HELIX 18 AB9 THR D 87 SER D 91 5 5 HELIX 19 AC1 SER D 161 ALA D 163 5 3 HELIX 20 AC2 PRO D 190 LEU D 194 5 5 HELIX 21 AC3 LYS D 206 ASN D 209 5 4 HELIX 22 AC4 GLU E 84 LEU E 88 5 5 HELIX 23 AC5 SER E 126 SER E 132 1 7 HELIX 24 AC6 LYS E 188 HIS E 194 1 7 HELIX 25 AC7 GLY F 15 ALA F 22 1 8 HELIX 26 AC8 ASN F 64 LEU F 68 5 5 HELIX 27 AC9 SER F 140 LEU F 144 5 5 HELIX 28 AD1 SER F 186 ASN F 190 5 5 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O LEU A 83 N VAL A 18 SHEET 4 AA1 4 ALA A 68 ASP A 73 -1 N ASP A 73 O THR A 78 SHEET 1 AA2 6 VAL A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 112 VAL A 116 1 O THR A 115 N VAL A 12 SHEET 3 AA2 6 ALA A 92 ARG A 98 -1 N ALA A 92 O VAL A 114 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N ASN A 35 O ALA A 97 SHEET 5 AA2 6 LEU A 45 VAL A 51 -1 O GLU A 46 N LYS A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O THR A 59 N ARG A 50 SHEET 1 AA3 4 SER A 125 LEU A 129 0 SHEET 2 AA3 4 ALA A 142 TYR A 150 -1 O GLY A 144 N LEU A 129 SHEET 3 AA3 4 TYR A 181 THR A 188 -1 O LEU A 183 N VAL A 147 SHEET 4 AA3 4 VAL A 168 THR A 170 -1 N HIS A 169 O VAL A 186 SHEET 1 AA4 4 SER A 125 LEU A 129 0 SHEET 2 AA4 4 ALA A 142 TYR A 150 -1 O GLY A 144 N LEU A 129 SHEET 3 AA4 4 TYR A 181 THR A 188 -1 O LEU A 183 N VAL A 147 SHEET 4 AA4 4 VAL A 174 LEU A 175 -1 N VAL A 174 O SER A 182 SHEET 1 AA5 3 THR A 156 TRP A 159 0 SHEET 2 AA5 3 ILE A 200 HIS A 205 -1 O ASN A 202 N SER A 158 SHEET 3 AA5 3 THR A 210 LYS A 215 -1 O VAL A 212 N VAL A 203 SHEET 1 AA6 4 MET B 4 THR B 7 0 SHEET 2 AA6 4 ALA B 19 SER B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA6 4 ASP B 75 ILE B 80 -1 O LEU B 78 N ILE B 21 SHEET 4 AA6 4 PHE B 67 SER B 72 -1 N SER B 68 O LYS B 79 SHEET 1 AA7 6 THR B 10 THR B 14 0 SHEET 2 AA7 6 THR B 107 LYS B 112 1 O GLU B 110 N LEU B 11 SHEET 3 AA7 6 GLY B 89 GLN B 95 -1 N GLY B 89 O LEU B 109 SHEET 4 AA7 6 LEU B 38 GLN B 43 -1 N LEU B 41 O TYR B 92 SHEET 5 AA7 6 LYS B 50 TYR B 54 -1 O LEU B 52 N TRP B 40 SHEET 6 AA7 6 LYS B 58 LEU B 59 -1 O LYS B 58 N TYR B 54 SHEET 1 AA8 4 THR B 10 THR B 14 0 SHEET 2 AA8 4 THR B 107 LYS B 112 1 O GLU B 110 N LEU B 11 SHEET 3 AA8 4 GLY B 89 GLN B 95 -1 N GLY B 89 O LEU B 109 SHEET 4 AA8 4 THR B 102 PHE B 103 -1 O THR B 102 N GLN B 95 SHEET 1 AA9 2 PHE B 30 SER B 32 0 SHEET 2 AA9 2 LYS B 35 THR B 36 -1 O LYS B 35 N SER B 32 SHEET 1 AB1 4 SER B 119 PHE B 123 0 SHEET 2 AB1 4 THR B 134 PHE B 144 -1 O ASN B 142 N SER B 119 SHEET 3 AB1 4 TYR B 178 SER B 187 -1 O LEU B 180 N LEU B 141 SHEET 4 AB1 4 SER B 164 VAL B 168 -1 N SER B 167 O SER B 181 SHEET 1 AB2 4 ALA B 158 LEU B 159 0 SHEET 2 AB2 4 LYS B 150 VAL B 155 -1 N VAL B 155 O ALA B 158 SHEET 3 AB2 4 VAL B 196 THR B 202 -1 O GLU B 200 N GLN B 152 SHEET 4 AB2 4 VAL B 210 ASN B 215 -1 O VAL B 210 N VAL B 201 SHEET 1 AB3 2 LEU C 34 THR C 35 0 SHEET 2 AB3 2 SER C 62 LEU C 63 -1 O LEU C 63 N LEU C 34 SHEET 1 AB4 6 ALA C 53 TYR C 57 0 SHEET 2 AB4 6 LYS C 45 ALA C 50 -1 N LEU C 46 O TYR C 57 SHEET 3 AB4 6 VAL C 73 VAL C 84 -1 O ILE C 79 N LYS C 47 SHEET 4 AB4 6 GLN C 87 LYS C 100 -1 O GLN C 87 N VAL C 84 SHEET 5 AB4 6 SER C 104 ASP C 116 -1 O GLU C 112 N SER C 93 SHEET 6 AB4 6 LYS C 122 GLY C 136 -1 O LYS C 122 N ASP C 116 SHEET 1 AB5 9 ARG C 149 GLY C 158 0 SHEET 2 AB5 9 ASP C 161 ASP C 171 -1 O TYR C 168 N TYR C 152 SHEET 3 AB5 9 GLN C 176 GLU C 182 -1 O GLU C 182 N LYS C 165 SHEET 4 AB5 9 ASP C 192 PRO C 200 -1 O LEU C 193 N GLY C 179 SHEET 5 AB5 9 ALA C 206 TYR C 214 -1 O LEU C 213 N ASP C 192 SHEET 6 AB5 9 ALA C 217 PHE C 227 -1 O LEU C 224 N ILE C 208 SHEET 7 AB5 9 GLU C 233 THR C 242 -1 O ALA C 235 N GLY C 225 SHEET 8 AB5 9 GLY C 245 LYS C 254 -1 O ARG C 247 N VAL C 240 SHEET 9 AB5 9 ARG C 149 GLY C 158 -1 N PHE C 157 O GLY C 250 SHEET 1 AB6 4 GLN D 3 GLN D 6 0 SHEET 2 AB6 4 VAL D 18 SER D 25 -1 O LYS D 23 N GLN D 5 SHEET 3 AB6 4 THR D 78 LEU D 83 -1 O LEU D 83 N VAL D 18 SHEET 4 AB6 4 ALA D 68 ASP D 73 -1 N ASP D 73 O THR D 78 SHEET 1 AB7 6 VAL D 10 VAL D 12 0 SHEET 2 AB7 6 THR D 112 VAL D 116 1 O THR D 115 N VAL D 12 SHEET 3 AB7 6 ALA D 92 ARG D 98 -1 N ALA D 92 O VAL D 114 SHEET 4 AB7 6 MET D 34 GLN D 39 -1 N ASN D 35 O ALA D 97 SHEET 5 AB7 6 LEU D 45 VAL D 51 -1 O GLU D 46 N LYS D 38 SHEET 6 AB7 6 THR D 58 TYR D 60 -1 O THR D 59 N ARG D 50 SHEET 1 AB8 4 SER D 125 LEU D 129 0 SHEET 2 AB8 4 ALA D 142 TYR D 150 -1 O GLY D 144 N LEU D 129 SHEET 3 AB8 4 TYR D 181 THR D 188 -1 O LEU D 183 N VAL D 147 SHEET 4 AB8 4 VAL D 168 THR D 170 -1 N HIS D 169 O VAL D 186 SHEET 1 AB9 4 SER D 125 LEU D 129 0 SHEET 2 AB9 4 ALA D 142 TYR D 150 -1 O GLY D 144 N LEU D 129 SHEET 3 AB9 4 TYR D 181 THR D 188 -1 O LEU D 183 N VAL D 147 SHEET 4 AB9 4 VAL D 174 LEU D 175 -1 N VAL D 174 O SER D 182 SHEET 1 AC1 3 THR D 156 TRP D 159 0 SHEET 2 AC1 3 TYR D 199 HIS D 205 -1 O ASN D 202 N SER D 158 SHEET 3 AC1 3 THR D 210 VAL D 216 -1 O VAL D 212 N VAL D 203 SHEET 1 AC2 4 MET E 4 THR E 7 0 SHEET 2 AC2 4 ALA E 19 SER E 25 -1 O LYS E 24 N THR E 5 SHEET 3 AC2 4 ASP E 75 ILE E 80 -1 O LEU E 78 N ILE E 21 SHEET 4 AC2 4 PHE E 67 SER E 72 -1 N SER E 68 O LYS E 79 SHEET 1 AC3 6 THR E 10 THR E 14 0 SHEET 2 AC3 6 THR E 107 LYS E 112 1 O GLU E 110 N LEU E 11 SHEET 3 AC3 6 GLY E 89 GLN E 95 -1 N GLY E 89 O LEU E 109 SHEET 4 AC3 6 LEU E 38 GLN E 43 -1 N LEU E 41 O TYR E 92 SHEET 5 AC3 6 LYS E 50 TYR E 54 -1 O LEU E 52 N TRP E 40 SHEET 6 AC3 6 LYS E 58 LEU E 59 -1 O LYS E 58 N TYR E 54 SHEET 1 AC4 4 THR E 10 THR E 14 0 SHEET 2 AC4 4 THR E 107 LYS E 112 1 O GLU E 110 N LEU E 11 SHEET 3 AC4 4 GLY E 89 GLN E 95 -1 N GLY E 89 O LEU E 109 SHEET 4 AC4 4 THR E 102 PHE E 103 -1 O THR E 102 N GLN E 95 SHEET 1 AC5 2 PHE E 30 SER E 32 0 SHEET 2 AC5 2 LYS E 35 THR E 36 -1 O LYS E 35 N SER E 32 SHEET 1 AC6 4 SER E 119 PHE E 123 0 SHEET 2 AC6 4 THR E 134 PHE E 144 -1 O LEU E 140 N PHE E 121 SHEET 3 AC6 4 TYR E 178 SER E 187 -1 O LEU E 186 N ALA E 135 SHEET 4 AC6 4 SER E 164 VAL E 168 -1 N SER E 167 O SER E 181 SHEET 1 AC7 4 ALA E 158 LEU E 159 0 SHEET 2 AC7 4 LYS E 150 VAL E 155 -1 N VAL E 155 O ALA E 158 SHEET 3 AC7 4 VAL E 196 THR E 202 -1 O GLU E 200 N GLN E 152 SHEET 4 AC7 4 VAL E 210 ASN E 215 -1 O VAL E 210 N VAL E 201 SHEET 1 AC8 2 LEU F 34 THR F 35 0 SHEET 2 AC8 2 SER F 62 LEU F 63 -1 O LEU F 63 N LEU F 34 SHEET 1 AC9 6 ALA F 53 TYR F 57 0 SHEET 2 AC9 6 LYS F 45 ALA F 50 -1 N LEU F 46 O TYR F 57 SHEET 3 AC9 6 VAL F 73 VAL F 84 -1 O ASP F 77 N ALA F 49 SHEET 4 AC9 6 GLN F 87 LYS F 100 -1 O VAL F 98 N SER F 74 SHEET 5 AC9 6 SER F 104 GLN F 115 -1 O ALA F 108 N GLN F 97 SHEET 6 AC9 6 MET F 123 GLY F 136 -1 O GLY F 132 N THR F 107 SHEET 1 AD1 9 ARG F 149 GLY F 158 0 SHEET 2 AD1 9 ASP F 161 ASP F 171 -1 O TYR F 168 N TYR F 152 SHEET 3 AD1 9 GLN F 176 GLU F 182 -1 O GLU F 182 N LYS F 165 SHEET 4 AD1 9 ASP F 192 PRO F 200 -1 O LEU F 193 N GLY F 179 SHEET 5 AD1 9 ALA F 206 TYR F 214 -1 O VAL F 207 N LYS F 199 SHEET 6 AD1 9 ALA F 217 PHE F 227 -1 O LYS F 219 N VAL F 212 SHEET 7 AD1 9 GLU F 233 THR F 242 -1 O ALA F 235 N GLY F 225 SHEET 8 AD1 9 GLY F 245 LYS F 254 -1 O ARG F 247 N VAL F 240 SHEET 9 AD1 9 ARG F 149 GLY F 158 -1 N PHE F 157 O GLY F 250 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.09 SSBOND 2 CYS A 145 CYS A 201 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 93 1555 1555 2.11 SSBOND 4 CYS B 139 CYS B 199 1555 1555 2.08 SSBOND 5 CYS D 22 CYS D 96 1555 1555 2.08 SSBOND 6 CYS D 145 CYS D 201 1555 1555 2.04 SSBOND 7 CYS E 23 CYS E 93 1555 1555 2.12 SSBOND 8 CYS E 139 CYS E 199 1555 1555 2.08 CISPEP 1 PHE A 151 PRO A 152 0 -5.51 CISPEP 2 GLU A 153 PRO A 154 0 0.27 CISPEP 3 THR B 7 PRO B 8 0 -6.99 CISPEP 4 PHE B 99 PRO B 100 0 -0.68 CISPEP 5 TYR B 145 PRO B 146 0 1.11 CISPEP 6 GLY C 30 LEU C 31 0 0.12 CISPEP 7 PHE D 151 PRO D 152 0 -5.34 CISPEP 8 GLU D 153 PRO D 154 0 -0.44 CISPEP 9 THR E 7 PRO E 8 0 -4.94 CISPEP 10 PHE E 99 PRO E 100 0 0.60 CISPEP 11 TYR E 145 PRO E 146 0 0.83 CISPEP 12 GLY F 30 LEU F 31 0 -0.55 CRYST1 74.430 67.440 168.470 90.00 90.00 90.00 P 1 21 1 4 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 0.013435 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014828 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005936 0.00000 MTRIX1 1 0.999972 -0.000240 -0.007426 -0.01256 1 MTRIX2 1 -0.000225 -0.999998 0.001941 -14.24338 1 MTRIX3 1 -0.007427 -0.001939 -0.999971 84.46309 1 MTRIX1 2 0.999981 0.001973 -0.005756 -0.01524 1 MTRIX2 2 0.001980 -0.999997 0.001142 -14.29000 1 MTRIX3 2 -0.005754 -0.001153 -0.999983 84.36525 1 MTRIX1 3 0.999975 0.000273 0.007113 -0.32340 1 MTRIX2 3 0.000284 -0.999999 -0.001490 -14.24901 1 MTRIX3 3 0.007112 0.001492 -0.999974 83.85087 1