HEADER IMMUNE SYSTEM 24-JUL-25 9PRU TITLE COMPLEX OF THE 3G8 FAB BOUND TO FC GAMMA RECEPTOR 3A / CD16A F158 TITLE 2 ALLOTYPE COMPND MOL_ID: 1; COMPND 2 MOLECULE: 3G8 FAB LIGHT CHAIN; COMPND 3 CHAIN: A, C, E, G; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 3G8 FAB HEAVY CHAIN; COMPND 7 CHAIN: B, D, F, H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LOW AFFINITY IMMUNOGLOBULIN GAMMA FC REGION RECEPTOR III-A; COMPND 11 CHAIN: W, X, Y, Z; COMPND 12 SYNONYM: IGG FC RECEPTOR III-A,CD16-II,CD16A ANTIGEN,FC-GAMMA RIII- COMPND 13 ALPHA,FC-GAMMA RIII,FC-GAMMA RIIIA,FCRIII,FCRIIIA,FCGAMMARIIIA,FCR- COMPND 14 10,IGG FC RECEPTOR III-2; COMPND 15 ENGINEERED: YES; COMPND 16 MUTATION: 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: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: MOUSE; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: FCGR3A, CD16A, FCG3, FCGR3, IGFR3; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIGEN-BINDING FRAGMENT FC GAMMA RECEPTOR N-GLYCAN GLYCOPROTEIN, KEYWDS 2 IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.W.BARB,W.N.LANZILOTTA,P.G.KREMER REVDAT 1 31-DEC-25 9PRU 0 JRNL AUTH P.G.KREMER,W.D.TOLBERT,E.GAZAWAY,B.G.HERNANDEZ, JRNL AUTH 2 M.K.KORZENIOWSKI,Z.A.DYBA,T.GRELSSON,O.C.GRANT, JRNL AUTH 3 W.N.LANZILOTTA,M.PAZGIER,R.J.WOODS,A.W.BARB JRNL TITL THE IMPACT OF N-GLYCAN CONFORMATIONAL ENTROPY ON THE BINDING JRNL TITL 2 AFFINITY OF FC GAMMA RECEPTOR IIIA/CD16A. JRNL REF STRUCTURE 2025 JRNL REFN ISSN 0969-2126 JRNL PMID 41421343 JRNL DOI 10.1016/J.STR.2025.11.015 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 230340 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.230 REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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 0.0000 - 1.9000 1.00 0 0 0.3495 0.3824 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL 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 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9PRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-25. REMARK 100 THE DEPOSITION ID IS D_1000298148. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JAN-25 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.82 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 230340 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 48.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 6.100 REMARK 200 R MERGE (I) : 0.04600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.50100 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: PHENIX 1.21.2_5419 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.99 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M KCL, 0.1 M BIS-TRIS, 20% REMARK 280 PEG3350, 10% GLYCEROL, PH 5.82, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 65.03100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.25550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.29700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.25550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 65.03100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.29700 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5940 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26890 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, W, I 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5970 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, X, J 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, Y, K 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6000 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27020 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, Z, L 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 PHE A 27D REMARK 465 ASP A 27E REMARK 465 GLY A 27F REMARK 465 CYS A 214 REMARK 465 ARG B 213 REMARK 465 ASP B 214 REMARK 465 CYS B 215 REMARK 465 GLY B 216 REMARK 465 ASP C 27C REMARK 465 PHE C 27D REMARK 465 ASP C 27E REMARK 465 GLY C 27F REMARK 465 CYS C 214 REMARK 465 ASP D 214 REMARK 465 CYS D 215 REMARK 465 GLY D 216 REMARK 465 CYS E 214 REMARK 465 LYS F 64 REMARK 465 ASP F 214 REMARK 465 CYS F 215 REMARK 465 GLY F 216 REMARK 465 PHE G 27D REMARK 465 ASP G 27E REMARK 465 ASN G 212 REMARK 465 GLU G 213 REMARK 465 CYS G 214 REMARK 465 ASP H 214 REMARK 465 CYS H 215 REMARK 465 GLY H 216 REMARK 465 ARG W 1 REMARK 465 THR W 2 REMARK 465 GLU W 3 REMARK 465 GLY W 175 REMARK 465 ARG X 1 REMARK 465 THR X 2 REMARK 465 GLU X 3 REMARK 465 ASP X 4 REMARK 465 TYR X 33 REMARK 465 SER X 34 REMARK 465 PRO X 35 REMARK 465 GLU X 36 REMARK 465 ASP X 37 REMARK 465 GLY X 175 REMARK 465 ARG Y 1 REMARK 465 THR Y 2 REMARK 465 GLU Y 3 REMARK 465 ASP Y 4 REMARK 465 LEU Y 5 REMARK 465 GLY Y 31 REMARK 465 ALA Y 32 REMARK 465 TYR Y 33 REMARK 465 SER Y 34 REMARK 465 PRO Y 35 REMARK 465 GLU Y 36 REMARK 465 ASP Y 37 REMARK 465 SER Y 51 REMARK 465 GLN Y 74 REMARK 465 GLY Y 175 REMARK 465 ARG Z 1 REMARK 465 THR Z 2 REMARK 465 GLU Z 3 REMARK 465 ASP Z 4 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 SER A 7 OG REMARK 470 GLN A 27 CG CD OE1 NE2 REMARK 470 VAL A 27B CG1 CG2 REMARK 470 ASP A 27C CG OD1 OD2 REMARK 470 GLU A 105 CG CD OE1 OE2 REMARK 470 LYS A 142 CG CD CE NZ REMARK 470 ASN A 145 CG OD1 ND2 REMARK 470 LYS A 147 CG CD CE NZ REMARK 470 SER A 153 OG REMARK 470 GLN A 156 CG CD OE1 NE2 REMARK 470 ASN A 157 CG OD1 ND2 REMARK 470 LYS A 183 CG CD CE NZ REMARK 470 SER A 201 OG REMARK 470 SER A 203 OG REMARK 470 SER A 208 OG REMARK 470 ASN A 210 CG OD1 ND2 REMARK 470 ASN A 212 CG OD1 ND2 REMARK 470 GLU A 213 CG CD OE1 OE2 REMARK 470 GLN B 1 CG CD OE1 NE2 REMARK 470 GLN B 13 OE1 NE2 REMARK 470 ARG B 30 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 43 NZ REMARK 470 LYS B 64 CG CD CE NZ REMARK 470 SER B 74 OG REMARK 470 LYS B 81 CE NZ REMARK 470 ILE B 82 CD1 REMARK 470 SER B 82B OG REMARK 470 LYS B 115 CG CD CE NZ REMARK 470 VAL B 136 CG1 CG2 REMARK 470 LYS B 143 NZ REMARK 470 SER B 161 OG REMARK 470 GLU B 191 CG CD OE1 OE2 REMARK 470 VAL B 197 CG1 CG2 REMARK 470 SER B 203 OG REMARK 470 LYS B 205 CG CD CE NZ REMARK 470 LYS B 208 CG CD CE NZ REMARK 470 LYS B 209 CG CD CE NZ REMARK 470 ILE B 210 CG2 REMARK 470 SER C 27A OG REMARK 470 VAL C 27B CG1 CG2 REMARK 470 ASP C 30 N CB CG OD1 OD2 REMARK 470 LYS C 45 NZ REMARK 470 SER C 153 OG REMARK 470 GLN C 156 OE1 NE2 REMARK 470 LYS C 169 NZ REMARK 470 LYS D 5 CE NZ REMARK 470 SER D 23 OG REMARK 470 ARG D 30 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 43 CE NZ REMARK 470 LEU D 63 CG CD1 CD2 REMARK 470 LYS D 64 CG CD CE NZ REMARK 470 LYS D 81 CD CE NZ REMARK 470 LYS D 115 CG CD CE NZ REMARK 470 VAL D 150 CG1 REMARK 470 LYS D 205 CG CD CE NZ REMARK 470 LYS D 208 NZ REMARK 470 LYS E 24 CG CD CE NZ REMARK 470 GLN E 27 CG CD OE1 NE2 REMARK 470 SER E 27A OG REMARK 470 VAL E 27B CG1 CG2 REMARK 470 ASP E 27C CG OD1 OD2 REMARK 470 PHE E 27D CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP E 30 CG OD1 OD2 REMARK 470 SER E 127 OG REMARK 470 ASP E 143 OD1 OD2 REMARK 470 ASN E 145 CG OD1 ND2 REMARK 470 LYS E 147 CG CD CE NZ REMARK 470 SER E 153 OG REMARK 470 GLN E 156 CG CD OE1 NE2 REMARK 470 ASN E 157 CG OD1 ND2 REMARK 470 ARG E 188 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 195 CG CD OE1 OE2 REMARK 470 SER E 203 OG REMARK 470 GLN F 1 CG CD OE1 NE2 REMARK 470 SER F 7 OG REMARK 470 SER F 25 OG REMARK 470 SER F 28 OG REMARK 470 ARG F 30 CG CD NE CZ NH1 NH2 REMARK 470 LYS F 71 CE NZ REMARK 470 SER F 74 OG REMARK 470 LYS F 115 CG CD CE NZ REMARK 470 LEU F 124 CD2 REMARK 470 SER F 128 OG REMARK 470 GLN F 131 CG CD OE1 NE2 REMARK 470 ASN F 133 CG OD1 ND2 REMARK 470 SER F 134 OG REMARK 470 VAL F 136 CG1 CG2 REMARK 470 SER F 186 OG REMARK 470 LYS F 205 CG CD CE NZ REMARK 470 LYS F 208 CG CD CE NZ REMARK 470 LYS F 209 CE NZ REMARK 470 ARG F 213 CG CD NE CZ NH1 NH2 REMARK 470 VAL G 27B CG1 CG2 REMARK 470 ASP G 27C CG OD1 OD2 REMARK 470 HIS G 76 CG ND1 CD2 CE1 NE2 REMARK 470 LYS G 103 CG CD CE NZ REMARK 470 SER G 122 OG REMARK 470 GLU G 123 CG CD OE1 OE2 REMARK 470 VAL G 132 CG1 CG2 REMARK 470 LYS G 142 CG CD CE NZ REMARK 470 LYS G 147 CG CD CE NZ REMARK 470 LYS G 149 CG CD CE NZ REMARK 470 SER G 153 OG REMARK 470 GLU G 154 CG CD OE1 OE2 REMARK 470 GLN G 156 CG CD OE1 NE2 REMARK 470 ASN G 157 CG OD1 ND2 REMARK 470 VAL G 159 CG1 CG2 REMARK 470 LYS G 169 CE NZ REMARK 470 LEU G 181 CG CD1 CD2 REMARK 470 LYS G 183 NZ REMARK 470 GLU G 185 CG CD OE1 OE2 REMARK 470 ARG G 188 CG CD NE CZ NH1 NH2 REMARK 470 SER G 203 OG REMARK 470 LYS H 5 CG CD CE NZ REMARK 470 LYS H 64 CE NZ REMARK 470 LYS H 81 CE NZ REMARK 470 GLN H 105 CG CD OE1 NE2 REMARK 470 LYS H 115 CG CD CE NZ REMARK 470 LEU H 159 CG CD1 CD2 REMARK 470 SER H 178 OG REMARK 470 SER H 203 OG REMARK 470 LYS H 205 CG CD CE NZ REMARK 470 LYS H 209 NZ REMARK 470 ARG H 213 CG CD NE CZ NH1 NH2 REMARK 470 LEU W 5 CD2 REMARK 470 ILE W 88 CD1 REMARK 470 ARG W 97 CZ NH1 NH2 REMARK 470 TRP W 98 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP W 98 CZ3 CH2 REMARK 470 VAL W 99 CG1 CG2 REMARK 470 LYS W 101 CG CD CE NZ REMARK 470 LYS W 120 CG CD CE NZ REMARK 470 LYS W 128 CG CD CE NZ REMARK 470 ILE W 141 CD1 REMARK 470 LYS W 143 CD CE NZ REMARK 470 LYS W 147 CG CD CE NZ REMARK 470 SER W 151 OG REMARK 470 LEU X 5 CG CD1 CD2 REMARK 470 LYS X 7 CG CD CE NZ REMARK 470 VAL X 9 CG1 CG2 REMARK 470 GLN X 30 OE1 NE2 REMARK 470 GLN X 38 CG CD OE1 NE2 REMARK 470 SER X 39 OG REMARK 470 GLN X 41 CG CD OE1 NE2 REMARK 470 PHE X 43 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU X 46 CG CD OE1 OE2 REMARK 470 SER X 47 OG REMARK 470 LEU X 48 CG CD1 CD2 REMARK 470 ILE X 49 CG1 CG2 CD1 REMARK 470 SER X 50 OG REMARK 470 SER X 51 OG REMARK 470 GLN X 52 CG CD OE1 NE2 REMARK 470 ARG X 70 CG CD NE CZ NH1 NH2 REMARK 470 GLN X 72 CG CD OE1 NE2 REMARK 470 LEU X 75 CG CD1 CD2 REMARK 470 LEU X 78 CG CD1 CD2 REMARK 470 TRP X 98 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP X 98 CZ3 CH2 REMARK 470 VAL X 99 CG1 CG2 REMARK 470 PHE X 100 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS X 101 CG CD CE NZ REMARK 470 GLU X 103 CG CD OE1 OE2 REMARK 470 ILE X 106 CD1 REMARK 470 LYS X 120 CE NZ REMARK 470 LYS X 128 CG CD CE NZ REMARK 470 HIS X 134 CG ND1 CD2 CE1 NE2 REMARK 470 LYS X 147 CG CD CE NZ REMARK 470 SER X 149 OG REMARK 470 LYS Y 7 CG CD CE NZ REMARK 470 GLN Y 38 CG CD OE1 NE2 REMARK 470 SER Y 39 OG REMARK 470 GLN Y 41 CG CD OE1 NE2 REMARK 470 PHE Y 43 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU Y 46 CG CD OE1 OE2 REMARK 470 SER Y 47 OG REMARK 470 LEU Y 48 CG CD1 CD2 REMARK 470 GLN Y 52 CG CD OE1 NE2 REMARK 470 ARG Y 70 CG CD NE CZ NH1 NH2 REMARK 470 GLN Y 72 CG CD OE1 NE2 REMARK 470 LEU Y 75 CG CD1 CD2 REMARK 470 SER Y 79 OG REMARK 470 GLN Y 83 CG CD OE1 NE2 REMARK 470 LYS Y 120 CE NZ REMARK 470 LYS Y 128 CG CD CE NZ REMARK 470 LYS Y 131 CE NZ REMARK 470 HIS Y 135 CG ND1 CD2 CE1 NE2 REMARK 470 LYS Y 147 CG CD CE NZ REMARK 470 LEU Z 5 CG CD1 CD2 REMARK 470 SER Z 34 OG REMARK 470 GLU Z 36 CG CD OE1 OE2 REMARK 470 ASP Z 37 CG OD1 OD2 REMARK 470 GLN Z 38 CG CD OE1 NE2 REMARK 470 GLN Z 52 CG CD OE1 NE2 REMARK 470 GLU Z 68 CG CD OE1 OE2 REMARK 470 GLN Z 74 CG CD OE1 NE2 REMARK 470 VAL Z 99 CG1 CG2 REMARK 470 LYS Z 101 NZ REMARK 470 HIS Z 119 CG ND1 CD2 CE1 NE2 REMARK 470 LYS Z 120 CE NZ REMARK 470 LYS Z 128 CG CD CE NZ REMARK 470 LYS Z 147 CG CD CE NZ 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 GLN F 105 CD GLN F 105 OE1 -0.140 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 CYS B 140 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 CYS D 140 CA - CB - SG ANGL. DEV. = 11.0 DEGREES REMARK 500 CYS F 140 CA - CB - SG ANGL. DEV. = 7.1 DEGREES 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 THR A 51 -48.63 75.02 REMARK 500 HIS A 76 118.20 -163.08 REMARK 500 LEU B 63 42.13 -82.47 REMARK 500 LYS B 64 -121.60 45.32 REMARK 500 ALA B 88 167.70 179.72 REMARK 500 THR C 51 -48.88 80.99 REMARK 500 SER C 67 -111.20 -121.96 REMARK 500 HIS C 76 115.72 -163.97 REMARK 500 ALA C 84 170.25 174.12 REMARK 500 SER D 15 -11.68 74.63 REMARK 500 SER D 160 -36.00 -134.47 REMARK 500 PHE E 27D 148.21 -170.15 REMARK 500 THR E 51 -42.98 76.39 REMARK 500 HIS E 76 113.74 -161.54 REMARK 500 ALA E 84 169.48 176.34 REMARK 500 ASN E 138 61.18 60.92 REMARK 500 SER F 15 -8.36 80.50 REMARK 500 SER F 160 -36.14 -133.07 REMARK 500 SER F 185 0.01 -66.93 REMARK 500 THR G 51 -41.97 73.56 REMARK 500 SER G 67 25.71 -161.46 REMARK 500 THR G 69 5.48 54.32 REMARK 500 HIS G 76 114.85 -162.61 REMARK 500 ALA G 84 174.32 176.38 REMARK 500 ASN G 138 53.39 70.53 REMARK 500 SER H 15 -9.30 76.54 REMARK 500 LYS H 64 56.58 39.67 REMARK 500 SER H 172 62.72 33.47 REMARK 500 LYS H 205 85.80 -151.25 REMARK 500 LYS W 22 -4.10 76.90 REMARK 500 GLN W 52 -55.18 -132.04 REMARK 500 LEU W 78 117.20 -33.81 REMARK 500 GLU W 103 -4.78 67.87 REMARK 500 THR W 173 -152.71 -105.38 REMARK 500 LYS X 22 -2.37 73.85 REMARK 500 THR X 40 -165.67 -110.74 REMARK 500 ILE X 49 -53.90 -121.63 REMARK 500 SER X 50 -164.31 -122.06 REMARK 500 SER X 51 -60.74 -125.24 REMARK 500 THR X 73 -157.22 -130.68 REMARK 500 GLU X 103 -8.17 63.67 REMARK 500 ILE Y 49 -45.95 -131.97 REMARK 500 ALA Y 60 84.43 -151.15 REMARK 500 SER Y 66 -166.05 -76.98 REMARK 500 THR Y 77 -92.80 -112.80 REMARK 500 GLU Y 103 -7.64 78.97 REMARK 500 LYS Z 22 -5.89 77.15 REMARK 500 GLU Z 36 -24.14 75.92 REMARK 500 ILE Z 49 -58.01 -140.89 REMARK 500 GLN Z 52 -54.71 -140.32 REMARK 500 REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 355 DISTANCE = 6.77 ANGSTROMS REMARK 525 HOH B 356 DISTANCE = 8.42 ANGSTROMS REMARK 525 HOH D 438 DISTANCE = 5.91 ANGSTROMS REMARK 525 HOH D 439 DISTANCE = 6.17 ANGSTROMS REMARK 525 HOH D 440 DISTANCE = 7.01 ANGSTROMS REMARK 525 HOH D 441 DISTANCE = 7.27 ANGSTROMS REMARK 525 HOH E 540 DISTANCE = 5.86 ANGSTROMS REMARK 525 HOH F 414 DISTANCE = 7.85 ANGSTROMS REMARK 525 HOH Y 354 DISTANCE = 7.11 ANGSTROMS REMARK 525 HOH Z 417 DISTANCE = 6.55 ANGSTROMS REMARK 525 HOH Z 418 DISTANCE = 7.12 ANGSTROMS REMARK 525 HOH Z 419 DISTANCE = 7.84 ANGSTROMS DBREF 9PRU A 1 214 PDB 9PRU 9PRU 1 214 DBREF 9PRU B 1 216 PDB 9PRU 9PRU 1 216 DBREF 9PRU C 1 214 PDB 9PRU 9PRU 1 214 DBREF 9PRU D 1 216 PDB 9PRU 9PRU 1 216 DBREF 9PRU E 1 214 PDB 9PRU 9PRU 1 214 DBREF 9PRU F 1 216 PDB 9PRU 9PRU 1 216 DBREF 9PRU G 1 214 PDB 9PRU 9PRU 1 214 DBREF 9PRU H 1 216 PDB 9PRU 9PRU 1 216 DBREF 9PRU W 1 175 UNP P08637 FCG3A_HUMAN 19 193 DBREF 9PRU X 1 175 UNP P08637 FCG3A_HUMAN 19 193 DBREF 9PRU Y 1 175 UNP P08637 FCG3A_HUMAN 19 193 DBREF 9PRU Z 1 175 UNP P08637 FCG3A_HUMAN 19 193 SEQADV 9PRU GLN W 38 UNP P08637 ASN 56 ENGINEERED MUTATION SEQADV 9PRU GLN W 74 UNP P08637 ASN 92 ENGINEERED MUTATION SEQADV 9PRU GLN W 169 UNP P08637 ASN 187 ENGINEERED MUTATION SEQADV 9PRU GLN X 38 UNP P08637 ASN 56 ENGINEERED MUTATION SEQADV 9PRU GLN X 74 UNP P08637 ASN 92 ENGINEERED MUTATION SEQADV 9PRU GLN X 169 UNP P08637 ASN 187 ENGINEERED MUTATION SEQADV 9PRU GLN Y 38 UNP P08637 ASN 56 ENGINEERED MUTATION SEQADV 9PRU GLN Y 74 UNP P08637 ASN 92 ENGINEERED MUTATION SEQADV 9PRU GLN Y 169 UNP P08637 ASN 187 ENGINEERED MUTATION SEQADV 9PRU GLN Z 38 UNP P08637 ASN 56 ENGINEERED MUTATION SEQADV 9PRU GLN Z 74 UNP P08637 ASN 92 ENGINEERED MUTATION SEQADV 9PRU GLN Z 169 UNP P08637 ASN 187 ENGINEERED MUTATION SEQRES 1 A 218 ALA ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 A 218 SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS ALA SER SEQRES 3 A 218 GLN SER VAL ASP PHE ASP GLY ASP SER PHE MET ASN TRP SEQRES 4 A 218 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 A 218 TYR THR THR SER ASN LEU GLU SER GLY ILE PRO ALA ARG SEQRES 6 A 218 PHE SER ALA SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 A 218 ILE HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR SEQRES 8 A 218 CYS GLN GLN SER ASN GLU ASP PRO TYR THR PHE GLY GLY SEQRES 9 A 218 GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA PRO SEQRES 10 A 218 THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SEQRES 11 A 218 SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE SEQRES 12 A 218 TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SEQRES 13 A 218 SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP SEQRES 14 A 218 GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR SEQRES 15 A 218 LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER SEQRES 16 A 218 TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO SEQRES 17 A 218 ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 B 221 GLN VAL THR LEU LYS GLU SER GLY PRO GLY ILE LEU GLN SEQRES 2 B 221 PRO SER GLN THR LEU SER LEU THR CYS SER PHE SER GLY SEQRES 3 B 221 PHE SER LEU ARG THR SER GLY MET GLY VAL GLY TRP ILE SEQRES 4 B 221 ARG GLN PRO SER GLY LYS GLY LEU GLU TRP LEU ALA HIS SEQRES 5 B 221 ILE TRP TRP ASP ASP ASP LYS ARG TYR ASN PRO ALA LEU SEQRES 6 B 221 LYS SER ARG LEU THR ILE SER LYS ASP THR SER SER ASN SEQRES 7 B 221 GLN VAL PHE LEU LYS ILE ALA SER VAL ASP THR ALA ASP SEQRES 8 B 221 THR ALA THR TYR TYR CYS ALA GLN ILE ASN PRO ALA TRP SEQRES 9 B 221 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 B 221 ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 B 221 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 B 221 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 B 221 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 B 221 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 B 221 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 B 221 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 B 221 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY SEQRES 1 C 218 ALA ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 C 218 SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS ALA SER SEQRES 3 C 218 GLN SER VAL ASP PHE ASP GLY ASP SER PHE MET ASN TRP SEQRES 4 C 218 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 C 218 TYR THR THR SER ASN LEU GLU SER GLY ILE PRO ALA ARG SEQRES 6 C 218 PHE SER ALA SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 C 218 ILE HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR SEQRES 8 C 218 CYS GLN GLN SER ASN GLU ASP PRO TYR THR PHE GLY GLY SEQRES 9 C 218 GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA PRO SEQRES 10 C 218 THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SEQRES 11 C 218 SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE SEQRES 12 C 218 TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SEQRES 13 C 218 SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP SEQRES 14 C 218 GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR SEQRES 15 C 218 LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER SEQRES 16 C 218 TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO SEQRES 17 C 218 ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 D 221 GLN VAL THR LEU LYS GLU SER GLY PRO GLY ILE LEU GLN SEQRES 2 D 221 PRO SER GLN THR LEU SER LEU THR CYS SER PHE SER GLY SEQRES 3 D 221 PHE SER LEU ARG THR SER GLY MET GLY VAL GLY TRP ILE SEQRES 4 D 221 ARG GLN PRO SER GLY LYS GLY LEU GLU TRP LEU ALA HIS SEQRES 5 D 221 ILE TRP TRP ASP ASP ASP LYS ARG TYR ASN PRO ALA LEU SEQRES 6 D 221 LYS SER ARG LEU THR ILE SER LYS ASP THR SER SER ASN SEQRES 7 D 221 GLN VAL PHE LEU LYS ILE ALA SER VAL ASP THR ALA ASP SEQRES 8 D 221 THR ALA THR TYR TYR CYS ALA GLN ILE ASN PRO ALA TRP SEQRES 9 D 221 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 D 221 ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 D 221 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 D 221 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 D 221 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 D 221 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 D 221 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 D 221 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 D 221 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY SEQRES 1 E 218 ALA ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 E 218 SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS ALA SER SEQRES 3 E 218 GLN SER VAL ASP PHE ASP GLY ASP SER PHE MET ASN TRP SEQRES 4 E 218 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 E 218 TYR THR THR SER ASN LEU GLU SER GLY ILE PRO ALA ARG SEQRES 6 E 218 PHE SER ALA SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 E 218 ILE HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR SEQRES 8 E 218 CYS GLN GLN SER ASN GLU ASP PRO TYR THR PHE GLY GLY SEQRES 9 E 218 GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA PRO SEQRES 10 E 218 THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SEQRES 11 E 218 SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE SEQRES 12 E 218 TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SEQRES 13 E 218 SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP SEQRES 14 E 218 GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR SEQRES 15 E 218 LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER SEQRES 16 E 218 TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO SEQRES 17 E 218 ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 F 221 GLN VAL THR LEU LYS GLU SER GLY PRO GLY ILE LEU GLN SEQRES 2 F 221 PRO SER GLN THR LEU SER LEU THR CYS SER PHE SER GLY SEQRES 3 F 221 PHE SER LEU ARG THR SER GLY MET GLY VAL GLY TRP ILE SEQRES 4 F 221 ARG GLN PRO SER GLY LYS GLY LEU GLU TRP LEU ALA HIS SEQRES 5 F 221 ILE TRP TRP ASP ASP ASP LYS ARG TYR ASN PRO ALA LEU SEQRES 6 F 221 LYS SER ARG LEU THR ILE SER LYS ASP THR SER SER ASN SEQRES 7 F 221 GLN VAL PHE LEU LYS ILE ALA SER VAL ASP THR ALA ASP SEQRES 8 F 221 THR ALA THR TYR TYR CYS ALA GLN ILE ASN PRO ALA TRP SEQRES 9 F 221 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 F 221 ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 F 221 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 F 221 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 F 221 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 F 221 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 F 221 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 F 221 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 F 221 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY SEQRES 1 G 218 ALA ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 G 218 SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS ALA SER SEQRES 3 G 218 GLN SER VAL ASP PHE ASP GLY ASP SER PHE MET ASN TRP SEQRES 4 G 218 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 G 218 TYR THR THR SER ASN LEU GLU SER GLY ILE PRO ALA ARG SEQRES 6 G 218 PHE SER ALA SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 G 218 ILE HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR SEQRES 8 G 218 CYS GLN GLN SER ASN GLU ASP PRO TYR THR PHE GLY GLY SEQRES 9 G 218 GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA PRO SEQRES 10 G 218 THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SEQRES 11 G 218 SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE SEQRES 12 G 218 TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SEQRES 13 G 218 SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP SEQRES 14 G 218 GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR SEQRES 15 G 218 LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER SEQRES 16 G 218 TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO SEQRES 17 G 218 ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 H 221 GLN VAL THR LEU LYS GLU SER GLY PRO GLY ILE LEU GLN SEQRES 2 H 221 PRO SER GLN THR LEU SER LEU THR CYS SER PHE SER GLY SEQRES 3 H 221 PHE SER LEU ARG THR SER GLY MET GLY VAL GLY TRP ILE SEQRES 4 H 221 ARG GLN PRO SER GLY LYS GLY LEU GLU TRP LEU ALA HIS SEQRES 5 H 221 ILE TRP TRP ASP ASP ASP LYS ARG TYR ASN PRO ALA LEU SEQRES 6 H 221 LYS SER ARG LEU THR ILE SER LYS ASP THR SER SER ASN SEQRES 7 H 221 GLN VAL PHE LEU LYS ILE ALA SER VAL ASP THR ALA ASP SEQRES 8 H 221 THR ALA THR TYR TYR CYS ALA GLN ILE ASN PRO ALA TRP SEQRES 9 H 221 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 H 221 ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 H 221 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 H 221 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 221 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 H 221 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 H 221 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 H 221 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 H 221 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY SEQRES 1 W 175 ARG THR GLU ASP LEU PRO LYS ALA VAL VAL PHE LEU GLU SEQRES 2 W 175 PRO GLN TRP TYR ARG VAL LEU GLU LYS ASP SER VAL THR SEQRES 3 W 175 LEU LYS CYS GLN GLY ALA TYR SER PRO GLU ASP GLN SER SEQRES 4 W 175 THR GLN TRP PHE HIS ASN GLU SER LEU ILE SER SER GLN SEQRES 5 W 175 ALA SER SER TYR PHE ILE ASP ALA ALA THR VAL ASP ASP SEQRES 6 W 175 SER GLY GLU TYR ARG CYS GLN THR GLN LEU SER THR LEU SEQRES 7 W 175 SER ASP PRO VAL GLN LEU GLU VAL HIS ILE GLY TRP LEU SEQRES 8 W 175 LEU LEU GLN ALA PRO ARG TRP VAL PHE LYS GLU GLU ASP SEQRES 9 W 175 PRO ILE HIS LEU ARG CYS HIS SER TRP LYS ASN THR ALA SEQRES 10 W 175 LEU HIS LYS VAL THR TYR LEU GLN ASN GLY LYS GLY ARG SEQRES 11 W 175 LYS TYR PHE HIS HIS ASN SER ASP PHE TYR ILE PRO LYS SEQRES 12 W 175 ALA THR LEU LYS ASP SER GLY SER TYR PHE CYS ARG GLY SEQRES 13 W 175 LEU PHE GLY SER LYS ASN VAL SER SER GLU THR VAL GLN SEQRES 14 W 175 ILE THR ILE THR GLN GLY SEQRES 1 X 175 ARG THR GLU ASP LEU PRO LYS ALA VAL VAL PHE LEU GLU SEQRES 2 X 175 PRO GLN TRP TYR ARG VAL LEU GLU LYS ASP SER VAL THR SEQRES 3 X 175 LEU LYS CYS GLN GLY ALA TYR SER PRO GLU ASP GLN SER SEQRES 4 X 175 THR GLN TRP PHE HIS ASN GLU SER LEU ILE SER SER GLN SEQRES 5 X 175 ALA SER SER TYR PHE ILE ASP ALA ALA THR VAL ASP ASP SEQRES 6 X 175 SER GLY GLU TYR ARG CYS GLN THR GLN LEU SER THR LEU SEQRES 7 X 175 SER ASP PRO VAL GLN LEU GLU VAL HIS ILE GLY TRP LEU SEQRES 8 X 175 LEU LEU GLN ALA PRO ARG TRP VAL PHE LYS GLU GLU ASP SEQRES 9 X 175 PRO ILE HIS LEU ARG CYS HIS SER TRP LYS ASN THR ALA SEQRES 10 X 175 LEU HIS LYS VAL THR TYR LEU GLN ASN GLY LYS GLY ARG SEQRES 11 X 175 LYS TYR PHE HIS HIS ASN SER ASP PHE TYR ILE PRO LYS SEQRES 12 X 175 ALA THR LEU LYS ASP SER GLY SER TYR PHE CYS ARG GLY SEQRES 13 X 175 LEU PHE GLY SER LYS ASN VAL SER SER GLU THR VAL GLN SEQRES 14 X 175 ILE THR ILE THR GLN GLY SEQRES 1 Y 175 ARG THR GLU ASP LEU PRO LYS ALA VAL VAL PHE LEU GLU SEQRES 2 Y 175 PRO GLN TRP TYR ARG VAL LEU GLU LYS ASP SER VAL THR SEQRES 3 Y 175 LEU LYS CYS GLN GLY ALA TYR SER PRO GLU ASP GLN SER SEQRES 4 Y 175 THR GLN TRP PHE HIS ASN GLU SER LEU ILE SER SER GLN SEQRES 5 Y 175 ALA SER SER TYR PHE ILE ASP ALA ALA THR VAL ASP ASP SEQRES 6 Y 175 SER GLY GLU TYR ARG CYS GLN THR GLN LEU SER THR LEU SEQRES 7 Y 175 SER ASP PRO VAL GLN LEU GLU VAL HIS ILE GLY TRP LEU SEQRES 8 Y 175 LEU LEU GLN ALA PRO ARG TRP VAL PHE LYS GLU GLU ASP SEQRES 9 Y 175 PRO ILE HIS LEU ARG CYS HIS SER TRP LYS ASN THR ALA SEQRES 10 Y 175 LEU HIS LYS VAL THR TYR LEU GLN ASN GLY LYS GLY ARG SEQRES 11 Y 175 LYS TYR PHE HIS HIS ASN SER ASP PHE TYR ILE PRO LYS SEQRES 12 Y 175 ALA THR LEU LYS ASP SER GLY SER TYR PHE CYS ARG GLY SEQRES 13 Y 175 LEU PHE GLY SER LYS ASN VAL SER SER GLU THR VAL GLN SEQRES 14 Y 175 ILE THR ILE THR GLN GLY SEQRES 1 Z 175 ARG THR GLU ASP LEU PRO LYS ALA VAL VAL PHE LEU GLU SEQRES 2 Z 175 PRO GLN TRP TYR ARG VAL LEU GLU LYS ASP SER VAL THR SEQRES 3 Z 175 LEU LYS CYS GLN GLY ALA TYR SER PRO GLU ASP GLN SER SEQRES 4 Z 175 THR GLN TRP PHE HIS ASN GLU SER LEU ILE SER SER GLN SEQRES 5 Z 175 ALA SER SER TYR PHE ILE ASP ALA ALA THR VAL ASP ASP SEQRES 6 Z 175 SER GLY GLU TYR ARG CYS GLN THR GLN LEU SER THR LEU SEQRES 7 Z 175 SER ASP PRO VAL GLN LEU GLU VAL HIS ILE GLY TRP LEU SEQRES 8 Z 175 LEU LEU GLN ALA PRO ARG TRP VAL PHE LYS GLU GLU ASP SEQRES 9 Z 175 PRO ILE HIS LEU ARG CYS HIS SER TRP LYS ASN THR ALA SEQRES 10 Z 175 LEU HIS LYS VAL THR TYR LEU GLN ASN GLY LYS GLY ARG SEQRES 11 Z 175 LYS TYR PHE HIS HIS ASN SER ASP PHE TYR ILE PRO LYS SEQRES 12 Z 175 ALA THR LEU LYS ASP SER GLY SER TYR PHE CYS ARG GLY SEQRES 13 Z 175 LEU PHE GLY SER LYS ASN VAL SER SER GLU THR VAL GLN SEQRES 14 Z 175 ILE THR ILE THR GLN GLY HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET NAG K 1 14 HET NAG K 2 14 HET NAG L 1 14 HET NAG L 2 14 HET BMA L 3 11 HET GOL A 301 6 HET GOL C 301 6 HET NA E 301 1 HET GOL E 302 6 HET NA G 301 1 HET CL G 302 1 HET NA H 301 1 HET NAG W 201 14 HET NAG X 201 14 HET NAG Y 201 14 HET NAG Z 201 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM GOL GLYCEROL HETNAM NA SODIUM ION HETNAM CL CHLORIDE ION HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 13 NAG 12(C8 H15 N O6) FORMUL 13 BMA 3(C6 H12 O6) FORMUL 17 GOL 3(C3 H8 O3) FORMUL 19 NA 3(NA 1+) FORMUL 22 CL CL 1- FORMUL 28 HOH *1245(H2 O) HELIX 1 AA1 GLU A 79 THR A 83 5 5 HELIX 2 AA2 SER A 121 GLY A 128 1 8 HELIX 3 AA3 LYS A 183 GLU A 187 1 5 HELIX 4 AA4 ASP B 83 THR B 87 5 5 HELIX 5 AA5 SER B 128 ASN B 133 5 6 HELIX 6 AA6 SER B 156 SER B 158 5 3 HELIX 7 AA7 PRO B 200 SER B 203 5 4 HELIX 8 AA8 GLU C 79 THR C 83 5 5 HELIX 9 AA9 SER C 121 THR C 126 1 6 HELIX 10 AB1 LYS C 183 GLU C 187 1 5 HELIX 11 AB2 PRO D 61 LYS D 64 5 4 HELIX 12 AB3 ASP D 83 THR D 87 5 5 HELIX 13 AB4 SER D 128 ASN D 133 5 6 HELIX 14 AB5 SER D 156 SER D 158 5 3 HELIX 15 AB6 PRO D 200 SER D 203 5 4 HELIX 16 AB7 GLU E 79 THR E 83 5 5 HELIX 17 AB8 SER E 121 THR E 126 1 6 HELIX 18 AB9 LYS E 183 GLU E 187 1 5 HELIX 19 AC1 ASP F 83 THR F 87 5 5 HELIX 20 AC2 SER F 128 ASN F 133 5 6 HELIX 21 AC3 SER F 156 SER F 158 5 3 HELIX 22 AC4 PRO F 200 SER F 203 5 4 HELIX 23 AC5 GLU G 79 THR G 83 5 5 HELIX 24 AC6 SER G 121 SER G 127 1 7 HELIX 25 AC7 LYS G 183 GLU G 187 1 5 HELIX 26 AC8 PRO H 61 LYS H 64 5 4 HELIX 27 AC9 ASP H 83 THR H 87 5 5 HELIX 28 AD1 ALA H 129 ASN H 133 5 5 HELIX 29 AD2 SER H 186 TRP H 188 5 3 HELIX 30 AD3 PRO H 200 SER H 203 5 4 HELIX 31 AD4 THR W 62 SER W 66 5 5 HELIX 32 AD5 LYS W 114 THR W 116 5 3 HELIX 33 AD6 THR W 145 SER W 149 5 5 HELIX 34 AD7 THR X 62 SER X 66 5 5 HELIX 35 AD8 LYS X 114 THR X 116 5 3 HELIX 36 AD9 THR X 145 SER X 149 5 5 HELIX 37 AE1 THR Y 62 SER Y 66 5 5 HELIX 38 AE2 LYS Y 114 THR Y 116 5 3 HELIX 39 AE3 THR Y 145 SER Y 149 5 5 HELIX 40 AE4 THR Z 62 SER Z 66 5 5 HELIX 41 AE5 LYS Z 114 THR Z 116 5 3 HELIX 42 AE6 THR Z 145 SER Z 149 5 5 SHEET 1 AA1 4 LEU A 4 SER A 7 0 SHEET 2 AA1 4 ALA A 19 ALA A 25 -1 O SER A 22 N SER A 7 SHEET 3 AA1 4 ASP A 70 ILE A 75 -1 O LEU A 73 N ILE A 21 SHEET 4 AA1 4 PHE A 62 GLY A 66 -1 N SER A 63 O ASN A 74 SHEET 1 AA2 6 SER A 10 VAL A 13 0 SHEET 2 AA2 6 THR A 102 LEU A 106 1 O GLU A 105 N LEU A 11 SHEET 3 AA2 6 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 104 SHEET 4 AA2 6 MET A 33 GLN A 38 -1 N ASN A 34 O GLN A 89 SHEET 5 AA2 6 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 AA2 6 ASN A 53 LEU A 54 -1 O ASN A 53 N TYR A 49 SHEET 1 AA3 4 SER A 10 VAL A 13 0 SHEET 2 AA3 4 THR A 102 LEU A 106 1 O GLU A 105 N LEU A 11 SHEET 3 AA3 4 ALA A 84 GLN A 90 -1 N ALA A 84 O LEU A 104 SHEET 4 AA3 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AA4 4 THR A 114 PHE A 118 0 SHEET 2 AA4 4 GLY A 129 PHE A 139 -1 O ASN A 137 N THR A 114 SHEET 3 AA4 4 TYR A 173 THR A 182 -1 O TYR A 173 N PHE A 139 SHEET 4 AA4 4 VAL A 159 TRP A 163 -1 N SER A 162 O SER A 176 SHEET 1 AA5 4 SER A 153 GLU A 154 0 SHEET 2 AA5 4 ASN A 145 ILE A 150 -1 N ILE A 150 O SER A 153 SHEET 3 AA5 4 SER A 191 THR A 197 -1 O THR A 197 N ASN A 145 SHEET 4 AA5 4 ILE A 205 ASN A 210 -1 O LYS A 207 N CYS A 194 SHEET 1 AA6 4 THR B 3 SER B 7 0 SHEET 2 AA6 4 LEU B 18 SER B 25 -1 O THR B 21 N SER B 7 SHEET 3 AA6 4 GLN B 77 ILE B 82 -1 O VAL B 78 N CYS B 22 SHEET 4 AA6 4 LEU B 67 ASP B 72 -1 N SER B 70 O PHE B 79 SHEET 1 AA7 6 ILE B 11 LEU B 12 0 SHEET 2 AA7 6 THR B 107 VAL B 111 1 O THR B 110 N LEU B 12 SHEET 3 AA7 6 ALA B 88 ILE B 95 -1 N TYR B 90 O THR B 107 SHEET 4 AA7 6 GLY B 35 GLN B 39 -1 N ILE B 37 O TYR B 91 SHEET 5 AA7 6 GLU B 46 TRP B 52 -1 O LEU B 48 N TRP B 36 SHEET 6 AA7 6 LYS B 57 TYR B 59 -1 O ARG B 58 N HIS B 50 SHEET 1 AA8 4 ILE B 11 LEU B 12 0 SHEET 2 AA8 4 THR B 107 VAL B 111 1 O THR B 110 N LEU B 12 SHEET 3 AA8 4 ALA B 88 ILE B 95 -1 N TYR B 90 O THR B 107 SHEET 4 AA8 4 PHE B 100 TRP B 103 -1 O TYR B 102 N GLN B 94 SHEET 1 AA9 4 SER B 120 LEU B 124 0 SHEET 2 AA9 4 MET B 135 TYR B 145 -1 O LEU B 141 N TYR B 122 SHEET 3 AA9 4 LEU B 174 PRO B 184 -1 O TYR B 175 N TYR B 145 SHEET 4 AA9 4 VAL B 163 THR B 165 -1 N HIS B 164 O SER B 180 SHEET 1 AB1 4 SER B 120 LEU B 124 0 SHEET 2 AB1 4 MET B 135 TYR B 145 -1 O LEU B 141 N TYR B 122 SHEET 3 AB1 4 LEU B 174 PRO B 184 -1 O TYR B 175 N TYR B 145 SHEET 4 AB1 4 VAL B 169 GLN B 171 -1 N GLN B 171 O LEU B 174 SHEET 1 AB2 3 THR B 151 TRP B 154 0 SHEET 2 AB2 3 THR B 194 HIS B 199 -1 O ASN B 196 N THR B 153 SHEET 3 AB2 3 THR B 204 LYS B 209 -1 O THR B 204 N HIS B 199 SHEET 1 AB3 4 LEU C 4 SER C 7 0 SHEET 2 AB3 4 ALA C 19 ALA C 25 -1 O SER C 22 N SER C 7 SHEET 3 AB3 4 ASP C 70 ILE C 75 -1 O LEU C 73 N ILE C 21 SHEET 4 AB3 4 PHE C 62 GLY C 66 -1 N SER C 63 O ASN C 74 SHEET 1 AB4 6 SER C 10 VAL C 13 0 SHEET 2 AB4 6 THR C 102 LEU C 106 1 O GLU C 105 N LEU C 11 SHEET 3 AB4 6 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104 SHEET 4 AB4 6 MET C 33 GLN C 38 -1 N GLN C 38 O THR C 85 SHEET 5 AB4 6 LYS C 45 TYR C 49 -1 O LEU C 47 N TRP C 35 SHEET 6 AB4 6 ASN C 53 LEU C 54 -1 O ASN C 53 N TYR C 49 SHEET 1 AB5 4 SER C 10 VAL C 13 0 SHEET 2 AB5 4 THR C 102 LEU C 106 1 O GLU C 105 N LEU C 11 SHEET 3 AB5 4 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104 SHEET 4 AB5 4 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90 SHEET 1 AB6 4 THR C 114 PHE C 118 0 SHEET 2 AB6 4 GLY C 129 PHE C 139 -1 O PHE C 135 N SER C 116 SHEET 3 AB6 4 TYR C 173 THR C 182 -1 O LEU C 179 N VAL C 132 SHEET 4 AB6 4 VAL C 159 TRP C 163 -1 N SER C 162 O SER C 176 SHEET 1 AB7 4 SER C 153 ARG C 155 0 SHEET 2 AB7 4 ASN C 145 ILE C 150 -1 N ILE C 150 O SER C 153 SHEET 3 AB7 4 SER C 191 THR C 197 -1 O GLU C 195 N LYS C 147 SHEET 4 AB7 4 ILE C 205 ASN C 210 -1 O ILE C 205 N ALA C 196 SHEET 1 AB8 4 THR D 3 SER D 7 0 SHEET 2 AB8 4 LEU D 18 SER D 25 -1 O SER D 23 N LYS D 5 SHEET 3 AB8 4 GLN D 77 ILE D 82 -1 O VAL D 78 N CYS D 22 SHEET 4 AB8 4 LEU D 67 ASP D 72 -1 N ASP D 72 O GLN D 77 SHEET 1 AB9 6 ILE D 11 LEU D 12 0 SHEET 2 AB9 6 THR D 107 VAL D 111 1 O THR D 110 N LEU D 12 SHEET 3 AB9 6 ALA D 88 ILE D 95 -1 N TYR D 90 O THR D 107 SHEET 4 AB9 6 GLY D 35 GLN D 39 -1 N ILE D 37 O TYR D 91 SHEET 5 AB9 6 GLU D 46 TRP D 52 -1 O LEU D 48 N TRP D 36 SHEET 6 AB9 6 LYS D 57 TYR D 59 -1 O ARG D 58 N HIS D 50 SHEET 1 AC1 4 ILE D 11 LEU D 12 0 SHEET 2 AC1 4 THR D 107 VAL D 111 1 O THR D 110 N LEU D 12 SHEET 3 AC1 4 ALA D 88 ILE D 95 -1 N TYR D 90 O THR D 107 SHEET 4 AC1 4 PHE D 100 TRP D 103 -1 O TYR D 102 N GLN D 94 SHEET 1 AC2 4 SER D 120 LEU D 124 0 SHEET 2 AC2 4 MET D 135 TYR D 145 -1 O LEU D 141 N TYR D 122 SHEET 3 AC2 4 LEU D 174 PRO D 184 -1 O LEU D 177 N VAL D 142 SHEET 4 AC2 4 VAL D 163 THR D 165 -1 N HIS D 164 O SER D 180 SHEET 1 AC3 4 SER D 120 LEU D 124 0 SHEET 2 AC3 4 MET D 135 TYR D 145 -1 O LEU D 141 N TYR D 122 SHEET 3 AC3 4 LEU D 174 PRO D 184 -1 O LEU D 177 N VAL D 142 SHEET 4 AC3 4 VAL D 169 GLN D 171 -1 N GLN D 171 O LEU D 174 SHEET 1 AC4 3 THR D 151 TRP D 154 0 SHEET 2 AC4 3 THR D 194 HIS D 199 -1 O ASN D 196 N THR D 153 SHEET 3 AC4 3 THR D 204 LYS D 209 -1 O THR D 204 N HIS D 199 SHEET 1 AC5 4 LEU E 4 SER E 7 0 SHEET 2 AC5 4 ALA E 19 ALA E 25 -1 O SER E 22 N SER E 7 SHEET 3 AC5 4 ASP E 70 ILE E 75 -1 O LEU E 73 N ILE E 21 SHEET 4 AC5 4 PHE E 62 SER E 67 -1 N SER E 63 O ASN E 74 SHEET 1 AC6 6 SER E 10 VAL E 13 0 SHEET 2 AC6 6 THR E 102 LEU E 106 1 O GLU E 105 N LEU E 11 SHEET 3 AC6 6 ALA E 84 GLN E 90 -1 N ALA E 84 O LEU E 104 SHEET 4 AC6 6 MET E 33 GLN E 38 -1 N GLN E 38 O THR E 85 SHEET 5 AC6 6 LYS E 45 TYR E 49 -1 O LEU E 47 N TRP E 35 SHEET 6 AC6 6 ASN E 53 LEU E 54 -1 O ASN E 53 N TYR E 49 SHEET 1 AC7 4 SER E 10 VAL E 13 0 SHEET 2 AC7 4 THR E 102 LEU E 106 1 O GLU E 105 N LEU E 11 SHEET 3 AC7 4 ALA E 84 GLN E 90 -1 N ALA E 84 O LEU E 104 SHEET 4 AC7 4 THR E 97 PHE E 98 -1 O THR E 97 N GLN E 90 SHEET 1 AC8 4 THR E 114 PHE E 118 0 SHEET 2 AC8 4 GLY E 129 PHE E 139 -1 O ASN E 137 N THR E 114 SHEET 3 AC8 4 TYR E 173 THR E 182 -1 O LEU E 181 N ALA E 130 SHEET 4 AC8 4 VAL E 159 TRP E 163 -1 N SER E 162 O SER E 176 SHEET 1 AC9 4 SER E 153 ARG E 155 0 SHEET 2 AC9 4 ASN E 145 ILE E 150 -1 N ILE E 150 O SER E 153 SHEET 3 AC9 4 SER E 191 THR E 197 -1 O THR E 197 N ASN E 145 SHEET 4 AC9 4 ILE E 205 ASN E 210 -1 O LYS E 207 N CYS E 194 SHEET 1 AD1 4 THR F 3 SER F 7 0 SHEET 2 AD1 4 LEU F 18 SER F 25 -1 O SER F 23 N LYS F 5 SHEET 3 AD1 4 GLN F 77 ILE F 82 -1 O VAL F 78 N CYS F 22 SHEET 4 AD1 4 LEU F 67 ASP F 72 -1 N ASP F 72 O GLN F 77 SHEET 1 AD2 6 ILE F 11 LEU F 12 0 SHEET 2 AD2 6 THR F 107 VAL F 111 1 O THR F 110 N LEU F 12 SHEET 3 AD2 6 ALA F 88 ILE F 95 -1 N TYR F 90 O THR F 107 SHEET 4 AD2 6 GLY F 35 GLN F 39 -1 N ILE F 37 O TYR F 91 SHEET 5 AD2 6 GLU F 46 TRP F 52 -1 O LEU F 48 N TRP F 36 SHEET 6 AD2 6 LYS F 57 TYR F 59 -1 O ARG F 58 N HIS F 50 SHEET 1 AD3 4 ILE F 11 LEU F 12 0 SHEET 2 AD3 4 THR F 107 VAL F 111 1 O THR F 110 N LEU F 12 SHEET 3 AD3 4 ALA F 88 ILE F 95 -1 N TYR F 90 O THR F 107 SHEET 4 AD3 4 PHE F 100 TRP F 103 -1 O ALA F 101 N GLN F 94 SHEET 1 AD4 4 SER F 120 LEU F 124 0 SHEET 2 AD4 4 MET F 135 TYR F 145 -1 O GLY F 139 N LEU F 124 SHEET 3 AD4 4 LEU F 174 PRO F 184 -1 O VAL F 181 N LEU F 138 SHEET 4 AD4 4 VAL F 163 THR F 165 -1 N HIS F 164 O SER F 180 SHEET 1 AD5 4 SER F 120 LEU F 124 0 SHEET 2 AD5 4 MET F 135 TYR F 145 -1 O GLY F 139 N LEU F 124 SHEET 3 AD5 4 LEU F 174 PRO F 184 -1 O VAL F 181 N LEU F 138 SHEET 4 AD5 4 VAL F 169 GLN F 171 -1 N GLN F 171 O LEU F 174 SHEET 1 AD6 3 THR F 151 TRP F 154 0 SHEET 2 AD6 3 THR F 194 HIS F 199 -1 O ALA F 198 N THR F 151 SHEET 3 AD6 3 THR F 204 LYS F 209 -1 O VAL F 206 N VAL F 197 SHEET 1 AD7 4 LEU G 4 SER G 7 0 SHEET 2 AD7 4 ALA G 19 ALA G 25 -1 O SER G 22 N SER G 7 SHEET 3 AD7 4 PHE G 71 ILE G 75 -1 O PHE G 71 N CYS G 23 SHEET 4 AD7 4 PHE G 62 GLY G 66 -1 N SER G 63 O ASN G 74 SHEET 1 AD8 6 SER G 10 VAL G 13 0 SHEET 2 AD8 6 THR G 102 LEU G 106 1 O GLU G 105 N LEU G 11 SHEET 3 AD8 6 ALA G 84 GLN G 90 -1 N ALA G 84 O LEU G 104 SHEET 4 AD8 6 MET G 33 GLN G 38 -1 N ASN G 34 O GLN G 89 SHEET 5 AD8 6 PRO G 44 TYR G 49 -1 O LEU G 47 N TRP G 35 SHEET 6 AD8 6 ASN G 53 LEU G 54 -1 O ASN G 53 N TYR G 49 SHEET 1 AD9 4 SER G 10 VAL G 13 0 SHEET 2 AD9 4 THR G 102 LEU G 106 1 O GLU G 105 N LEU G 11 SHEET 3 AD9 4 ALA G 84 GLN G 90 -1 N ALA G 84 O LEU G 104 SHEET 4 AD9 4 THR G 97 PHE G 98 -1 O THR G 97 N GLN G 90 SHEET 1 AE1 4 THR G 114 PHE G 118 0 SHEET 2 AE1 4 GLY G 129 PHE G 139 -1 O PHE G 135 N SER G 116 SHEET 3 AE1 4 TYR G 173 THR G 182 -1 O LEU G 179 N VAL G 132 SHEET 4 AE1 4 VAL G 159 TRP G 163 -1 N LEU G 160 O THR G 178 SHEET 1 AE2 4 GLU G 154 ARG G 155 0 SHEET 2 AE2 4 ASN G 145 ILE G 150 -1 N TRP G 148 O ARG G 155 SHEET 3 AE2 4 SER G 191 THR G 197 -1 O GLU G 195 N LYS G 147 SHEET 4 AE2 4 ILE G 205 ASN G 210 -1 O ILE G 205 N ALA G 196 SHEET 1 AE3 4 THR H 3 SER H 7 0 SHEET 2 AE3 4 LEU H 18 SER H 25 -1 O SER H 23 N LYS H 5 SHEET 3 AE3 4 GLN H 77 ILE H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AE3 4 LEU H 67 ASP H 72 -1 N SER H 70 O PHE H 79 SHEET 1 AE4 6 ILE H 11 LEU H 12 0 SHEET 2 AE4 6 THR H 107 VAL H 111 1 O THR H 110 N LEU H 12 SHEET 3 AE4 6 ALA H 88 ILE H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AE4 6 GLY H 35 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AE4 6 GLU H 46 TRP H 52 -1 O LEU H 48 N TRP H 36 SHEET 6 AE4 6 LYS H 57 TYR H 59 -1 O ARG H 58 N HIS H 50 SHEET 1 AE5 4 ILE H 11 LEU H 12 0 SHEET 2 AE5 4 THR H 107 VAL H 111 1 O THR H 110 N LEU H 12 SHEET 3 AE5 4 ALA H 88 ILE H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AE5 4 PHE H 100 TRP H 103 -1 O TYR H 102 N GLN H 94 SHEET 1 AE6 4 SER H 120 LEU H 124 0 SHEET 2 AE6 4 MET H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AE6 4 LEU H 174 PRO H 184 -1 O TYR H 175 N TYR H 145 SHEET 4 AE6 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 SHEET 1 AE7 4 SER H 120 LEU H 124 0 SHEET 2 AE7 4 MET H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AE7 4 LEU H 174 PRO H 184 -1 O TYR H 175 N TYR H 145 SHEET 4 AE7 4 VAL H 169 GLN H 171 -1 N GLN H 171 O LEU H 174 SHEET 1 AE8 3 THR H 151 TRP H 154 0 SHEET 2 AE8 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 AE8 3 THR H 204 LYS H 209 -1 O THR H 204 N HIS H 199 SHEET 1 AE9 3 VAL W 9 GLU W 13 0 SHEET 2 AE9 3 VAL W 25 GLN W 30 -1 O LYS W 28 N PHE W 11 SHEET 3 AE9 3 TYR W 56 ILE W 58 -1 O ILE W 58 N VAL W 25 SHEET 1 AF1 5 ARG W 18 LEU W 20 0 SHEET 2 AF1 5 VAL W 82 HIS W 87 1 O HIS W 87 N VAL W 19 SHEET 3 AF1 5 GLY W 67 GLN W 72 -1 N GLY W 67 O LEU W 84 SHEET 4 AF1 5 GLN W 41 HIS W 44 -1 N PHE W 43 O ARG W 70 SHEET 5 AF1 5 SER W 47 SER W 50 -1 O ILE W 49 N TRP W 42 SHEET 1 AF2 3 LEU W 91 GLN W 94 0 SHEET 2 AF2 3 ILE W 106 SER W 112 -1 O ARG W 109 N GLN W 94 SHEET 3 AF2 3 PHE W 139 ILE W 141 -1 O PHE W 139 N LEU W 108 SHEET 1 AF3 5 VAL W 99 LYS W 101 0 SHEET 2 AF3 5 VAL W 168 THR W 173 1 O THR W 173 N PHE W 100 SHEET 3 AF3 5 GLY W 150 PHE W 158 -1 N TYR W 152 O VAL W 168 SHEET 4 AF3 5 HIS W 119 GLN W 125 -1 N HIS W 119 O LEU W 157 SHEET 5 AF3 5 LYS W 128 HIS W 135 -1 O ARG W 130 N TYR W 123 SHEET 1 AF4 4 VAL W 99 LYS W 101 0 SHEET 2 AF4 4 VAL W 168 THR W 173 1 O THR W 173 N PHE W 100 SHEET 3 AF4 4 GLY W 150 PHE W 158 -1 N TYR W 152 O VAL W 168 SHEET 4 AF4 4 LYS W 161 SER W 164 -1 O LYS W 161 N PHE W 158 SHEET 1 AF5 3 VAL X 10 GLU X 13 0 SHEET 2 AF5 3 VAL X 25 CYS X 29 -1 O THR X 26 N GLU X 13 SHEET 3 AF5 3 SER X 55 ILE X 58 -1 O ILE X 58 N VAL X 25 SHEET 1 AF6 5 ARG X 18 LEU X 20 0 SHEET 2 AF6 5 VAL X 82 HIS X 87 1 O HIS X 87 N VAL X 19 SHEET 3 AF6 5 GLY X 67 GLN X 72 -1 N GLY X 67 O LEU X 84 SHEET 4 AF6 5 GLN X 41 HIS X 44 -1 N PHE X 43 O ARG X 70 SHEET 5 AF6 5 SER X 47 LEU X 48 -1 O SER X 47 N HIS X 44 SHEET 1 AF7 3 LEU X 91 GLN X 94 0 SHEET 2 AF7 3 ILE X 106 SER X 112 -1 O HIS X 111 N LEU X 92 SHEET 3 AF7 3 PHE X 139 ILE X 141 -1 O ILE X 141 N ILE X 106 SHEET 1 AF8 5 VAL X 99 LYS X 101 0 SHEET 2 AF8 5 VAL X 168 THR X 173 1 O THR X 173 N PHE X 100 SHEET 3 AF8 5 GLY X 150 PHE X 158 -1 N TYR X 152 O VAL X 168 SHEET 4 AF8 5 HIS X 119 GLN X 125 -1 N LEU X 124 O PHE X 153 SHEET 5 AF8 5 LYS X 128 HIS X 135 -1 O ARG X 130 N TYR X 123 SHEET 1 AF9 4 VAL X 99 LYS X 101 0 SHEET 2 AF9 4 VAL X 168 THR X 173 1 O THR X 173 N PHE X 100 SHEET 3 AF9 4 GLY X 150 PHE X 158 -1 N TYR X 152 O VAL X 168 SHEET 4 AF9 4 LYS X 161 SER X 164 -1 O LYS X 161 N PHE X 158 SHEET 1 AG1 3 VAL Y 9 GLU Y 13 0 SHEET 2 AG1 3 VAL Y 25 GLN Y 30 -1 O LYS Y 28 N PHE Y 11 SHEET 3 AG1 3 SER Y 55 ILE Y 58 -1 O ILE Y 58 N VAL Y 25 SHEET 1 AG2 5 ARG Y 18 LEU Y 20 0 SHEET 2 AG2 5 VAL Y 82 HIS Y 87 1 O HIS Y 87 N VAL Y 19 SHEET 3 AG2 5 GLY Y 67 ARG Y 70 -1 N GLY Y 67 O LEU Y 84 SHEET 4 AG2 5 TRP Y 42 HIS Y 44 -1 N PHE Y 43 O ARG Y 70 SHEET 5 AG2 5 LEU Y 48 SER Y 50 -1 O ILE Y 49 N TRP Y 42 SHEET 1 AG3 3 LEU Y 91 GLN Y 94 0 SHEET 2 AG3 3 ILE Y 106 SER Y 112 -1 O ARG Y 109 N GLN Y 94 SHEET 3 AG3 3 PHE Y 139 ILE Y 141 -1 O PHE Y 139 N LEU Y 108 SHEET 1 AG4 5 VAL Y 99 LYS Y 101 0 SHEET 2 AG4 5 VAL Y 168 THR Y 173 1 O THR Y 173 N PHE Y 100 SHEET 3 AG4 5 GLY Y 150 PHE Y 158 -1 N TYR Y 152 O VAL Y 168 SHEET 4 AG4 5 HIS Y 119 GLN Y 125 -1 N HIS Y 119 O LEU Y 157 SHEET 5 AG4 5 LYS Y 128 HIS Y 135 -1 O HIS Y 134 N LYS Y 120 SHEET 1 AG5 4 VAL Y 99 LYS Y 101 0 SHEET 2 AG5 4 VAL Y 168 THR Y 173 1 O THR Y 173 N PHE Y 100 SHEET 3 AG5 4 GLY Y 150 PHE Y 158 -1 N TYR Y 152 O VAL Y 168 SHEET 4 AG5 4 LYS Y 161 SER Y 164 -1 O VAL Y 163 N GLY Y 156 SHEET 1 AG6 3 VAL Z 9 GLU Z 13 0 SHEET 2 AG6 3 VAL Z 25 GLN Z 30 -1 O GLN Z 30 N VAL Z 9 SHEET 3 AG6 3 SER Z 55 ILE Z 58 -1 O ILE Z 58 N VAL Z 25 SHEET 1 AG7 5 ARG Z 18 LEU Z 20 0 SHEET 2 AG7 5 VAL Z 82 HIS Z 87 1 O HIS Z 87 N VAL Z 19 SHEET 3 AG7 5 GLY Z 67 GLN Z 72 -1 N TYR Z 69 O VAL Z 82 SHEET 4 AG7 5 GLN Z 41 HIS Z 44 -1 N PHE Z 43 O ARG Z 70 SHEET 5 AG7 5 SER Z 47 LEU Z 48 -1 O SER Z 47 N HIS Z 44 SHEET 1 AG8 3 LEU Z 91 GLN Z 94 0 SHEET 2 AG8 3 ILE Z 106 SER Z 112 -1 O ARG Z 109 N GLN Z 94 SHEET 3 AG8 3 PHE Z 139 ILE Z 141 -1 O ILE Z 141 N ILE Z 106 SHEET 1 AG9 2 PHE Z 100 LYS Z 101 0 SHEET 2 AG9 2 ILE Z 172 THR Z 173 1 O THR Z 173 N PHE Z 100 SHEET 1 AH1 4 LYS Z 128 HIS Z 135 0 SHEET 2 AH1 4 HIS Z 119 GLN Z 125 -1 N TYR Z 123 O ARG Z 130 SHEET 3 AH1 4 GLY Z 150 PHE Z 158 -1 O LEU Z 157 N HIS Z 119 SHEET 4 AH1 4 LYS Z 161 SER Z 164 -1 O LYS Z 161 N PHE Z 158 SHEET 1 AH2 4 LYS Z 128 HIS Z 135 0 SHEET 2 AH2 4 HIS Z 119 GLN Z 125 -1 N TYR Z 123 O ARG Z 130 SHEET 3 AH2 4 GLY Z 150 PHE Z 158 -1 O LEU Z 157 N HIS Z 119 SHEET 4 AH2 4 VAL Z 168 ILE Z 170 -1 O ILE Z 170 N GLY Z 150 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.05 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.04 SSBOND 3 CYS B 22 CYS B 92 1555 1555 2.06 SSBOND 4 CYS B 140 CYS B 195 1555 1555 2.04 SSBOND 5 CYS C 23 CYS C 88 1555 1555 2.07 SSBOND 6 CYS C 134 CYS C 194 1555 1555 2.04 SSBOND 7 CYS D 22 CYS D 92 1555 1555 2.06 SSBOND 8 CYS D 140 CYS D 195 1555 1555 2.05 SSBOND 9 CYS E 23 CYS E 88 1555 1555 2.06 SSBOND 10 CYS E 134 CYS E 194 1555 1555 2.04 SSBOND 11 CYS F 22 CYS F 92 1555 1555 2.07 SSBOND 12 CYS F 140 CYS F 195 1555 1555 2.04 SSBOND 13 CYS G 23 CYS G 88 1555 1555 2.07 SSBOND 14 CYS G 134 CYS G 194 1555 1555 2.04 SSBOND 15 CYS H 22 CYS H 92 1555 1555 2.06 SSBOND 16 CYS H 140 CYS H 195 1555 1555 2.04 SSBOND 17 CYS W 29 CYS W 71 1555 1555 2.08 SSBOND 18 CYS W 110 CYS W 154 1555 1555 2.07 SSBOND 19 CYS X 29 CYS X 71 1555 1555 2.03 SSBOND 20 CYS X 110 CYS X 154 1555 1555 2.07 SSBOND 21 CYS Y 29 CYS Y 71 1555 1555 2.02 SSBOND 22 CYS Y 110 CYS Y 154 1555 1555 2.06 SSBOND 23 CYS Z 29 CYS Z 71 1555 1555 2.05 SSBOND 24 CYS Z 110 CYS Z 154 1555 1555 2.08 LINK ND2 ASN W 45 C1 NAG I 1 1555 1555 1.43 LINK ND2 ASN W 162 C1 NAG W 201 1555 1555 1.43 LINK ND2 ASN X 45 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN X 162 C1 NAG X 201 1555 1555 1.44 LINK ND2 ASN Y 45 C1 NAG K 1 1555 1555 1.43 LINK ND2 ASN Y 162 C1 NAG Y 201 1555 1555 1.48 LINK ND2 ASN Z 45 C1 NAG L 1 1555 1555 1.44 LINK ND2 ASN Z 162 C1 NAG Z 201 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.46 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.49 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.43 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45 LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.47 LINK O HOH C 551 NA NA E 301 3646 1555 2.88 LINK NA NA G 301 O HOH X 303 1555 1555 2.90 LINK OD1 ASN H 76 NA NA H 301 1555 1555 2.71 CISPEP 1 SER A 7 PRO A 8 0 -4.59 CISPEP 2 HIS A 76 PRO A 77 0 -1.70 CISPEP 3 ASP A 94 PRO A 95 0 -5.07 CISPEP 4 TYR A 140 PRO A 141 0 3.44 CISPEP 5 PHE B 146 PRO B 147 0 -1.08 CISPEP 6 GLU B 148 PRO B 149 0 4.80 CISPEP 7 TRP B 188 PRO B 189 0 16.25 CISPEP 8 SER C 7 PRO C 8 0 -4.59 CISPEP 9 HIS C 76 PRO C 77 0 2.13 CISPEP 10 ASP C 94 PRO C 95 0 -4.06 CISPEP 11 TYR C 140 PRO C 141 0 -1.49 CISPEP 12 PHE D 146 PRO D 147 0 -4.81 CISPEP 13 GLU D 148 PRO D 149 0 1.75 CISPEP 14 TRP D 188 PRO D 189 0 4.56 CISPEP 15 SER E 7 PRO E 8 0 -6.53 CISPEP 16 HIS E 76 PRO E 77 0 3.71 CISPEP 17 ASP E 94 PRO E 95 0 -6.28 CISPEP 18 TYR E 140 PRO E 141 0 5.35 CISPEP 19 PHE F 146 PRO F 147 0 -6.49 CISPEP 20 GLU F 148 PRO F 149 0 -2.86 CISPEP 21 TRP F 188 PRO F 189 0 -1.92 CISPEP 22 SER G 7 PRO G 8 0 -6.42 CISPEP 23 HIS G 76 PRO G 77 0 2.11 CISPEP 24 ASP G 94 PRO G 95 0 -2.28 CISPEP 25 TYR G 140 PRO G 141 0 6.28 CISPEP 26 PHE H 146 PRO H 147 0 -3.61 CISPEP 27 GLU H 148 PRO H 149 0 0.83 CISPEP 28 TRP H 188 PRO H 189 0 4.76 CISPEP 29 GLU W 13 PRO W 14 0 -6.57 CISPEP 30 GLU X 13 PRO X 14 0 -7.27 CISPEP 31 GLU Y 13 PRO Y 14 0 -3.79 CISPEP 32 GLU Z 13 PRO Z 14 0 -5.43 CRYST1 130.062 130.594 170.511 90.00 90.00 90.00 P 21 21 21 16 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 0.007689 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007657 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005865 0.00000