HEADER IMMUNE SYSTEM 21-APR-25 9OAS TITLE CRYSTAL STRUCTURE OF ANTIBODY FAB G001-14 FROM IAVI G001 HUMAN TRIAL TITLE 2 IN COMPLEX WITH A GERMLINE-TARGETING GP120 ENGINEERED OUTER DOMAIN TITLE 3 EOD-GT8-MINGLY-N276 COMPND MOL_ID: 1; COMPND 2 MOLECULE: G001-14 FAB LIGHT CHAIN; COMPND 3 CHAIN: K, L, R, F; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GERMLINE-TARGETING HIV-1 GP120 ENGINEERED OUTER DOMAIN EOD- COMPND 7 GT8-MINGLY-N276; COMPND 8 CHAIN: M, C, D, P; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: G001-14 FAB HEAVY CHAIN; COMPND 12 CHAIN: J, H, Q, E; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; 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: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; 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 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1 ENVELOPE ANTIBODY, HIV CD4 BINDING SITE ANTIBODY, IAVI G001 KEYWDS 2 CLINICAL TRIAL, GERMLINE-TARGETING IMMUNOGEN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR X.LIN,I.A.WILSON REVDAT 1 25-JUN-25 9OAS 0 JRNL AUTH X.LIN,C.A.COTTRELL,O.KALYUZHNIY,R.TINGLE,M.KUBITZ,D.LU, JRNL AUTH 2 M.YUAN,W.R.SCHIEF,I.A.WILSON JRNL TITL STRUCTURAL INSIGHTS INTO VRC01-CLASS BNAB PRECURSORS WITH JRNL TITL 2 DIVERSE LIGHT CHAINS ELICITED IN THE IAVI G001 HUMAN VACCINE JRNL TITL 3 TRIAL. JRNL REF BIORXIV 2025 JRNL REFN ISSN 2692-8205 JRNL PMID 40501797 JRNL DOI 10.1101/2025.05.22.655646 REMARK 2 REMARK 2 RESOLUTION. 2.79 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.08 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 74974 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.216 REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.255 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 3808 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 26.0800 - 8.2900 1.00 2835 140 0.1875 0.1849 REMARK 3 2 8.2900 - 6.6200 0.96 2643 141 0.2107 0.2538 REMARK 3 3 6.6200 - 5.7900 0.97 2652 149 0.2115 0.2452 REMARK 3 4 5.7900 - 5.2700 0.99 2695 157 0.1918 0.1951 REMARK 3 5 5.2700 - 4.8900 0.99 2710 136 0.1780 0.2326 REMARK 3 6 4.8900 - 4.6000 1.00 2686 159 0.1595 0.2088 REMARK 3 7 4.6000 - 4.3700 1.00 2675 142 0.1642 0.2162 REMARK 3 8 4.3700 - 4.1800 1.00 2682 152 0.1714 0.2151 REMARK 3 9 4.1800 - 4.0200 0.99 2692 148 0.1897 0.2439 REMARK 3 10 4.0200 - 3.8900 0.99 2675 159 0.1931 0.2272 REMARK 3 11 3.8900 - 3.7600 1.00 2659 139 0.2152 0.2372 REMARK 3 12 3.7600 - 3.6600 0.98 2655 141 0.2194 0.2956 REMARK 3 13 3.6600 - 3.5600 0.94 2549 144 0.2271 0.2662 REMARK 3 14 3.5600 - 3.4700 0.96 2569 139 0.2347 0.2859 REMARK 3 15 3.4700 - 3.4000 0.98 2617 134 0.2396 0.3045 REMARK 3 16 3.4000 - 3.3200 0.98 2625 129 0.2489 0.2675 REMARK 3 17 3.3200 - 3.2600 0.97 2648 127 0.2626 0.3373 REMARK 3 18 3.2600 - 3.2000 0.98 2637 146 0.2655 0.3409 REMARK 3 19 3.2000 - 3.1400 0.99 2623 137 0.2721 0.3432 REMARK 3 20 3.1400 - 3.0900 0.99 2672 129 0.2689 0.3548 REMARK 3 21 3.0900 - 3.0400 0.99 2604 156 0.2747 0.3301 REMARK 3 22 3.0400 - 2.9900 0.99 2696 133 0.2844 0.3240 REMARK 3 23 2.9900 - 2.9500 0.99 2650 152 0.2951 0.3267 REMARK 3 24 2.9500 - 2.9000 0.98 2577 154 0.3030 0.3898 REMARK 3 25 2.9000 - 2.8700 0.99 2712 129 0.3177 0.3497 REMARK 3 26 2.8700 - 2.8300 0.99 2613 122 0.3194 0.4258 REMARK 3 27 2.8300 - 2.7900 0.79 2115 114 0.3331 0.3910 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) : 0.408 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.759 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 61.05 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.58 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 : 0.004 18772 REMARK 3 ANGLE : 0.710 25528 REMARK 3 CHIRALITY : 0.049 2872 REMARK 3 PLANARITY : 0.005 3264 REMARK 3 DIHEDRAL : 13.964 6848 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 "C" 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 "M" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "P" 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 "E" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "H" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "J" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "Q" 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 "F" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "K" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "L" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "R" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9OAS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-25. REMARK 100 THE DEPOSITION ID IS D_1000295186. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-JAN-22 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 : SSRL REMARK 200 BEAMLINE : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 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 : 75138 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.790 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.86 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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 (%): 57.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (W/V) PEG 8000, 0.2 M ZINC REMARK 280 ACETATE, AND 0.1 M MES PH 6.0, VAPOR DIFFUSION, SITTING DROP, REMARK 280 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 130.52800 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.75900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 130.52800 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.75900 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 APPLY THE FOLLOWING TO CHAINS: K, M, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, R, Q 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 APPLY THE FOLLOWING TO CHAINS: P, F, E 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH C 305 LIES ON A SPECIAL POSITION. REMARK 375 HOH D 311 LIES ON A SPECIAL POSITION. 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 ASP K 1 REMARK 465 CYS K 214 REMARK 465 GLU M -2 REMARK 465 THR M -1 REMARK 465 GLY M 0 REMARK 465 ALA M 170 REMARK 465 SER M 171 REMARK 465 THR M 172 REMARK 465 GLY M 173 REMARK 465 THR M 174 REMARK 465 LYS M 175 REMARK 465 HIS M 176 REMARK 465 HIS M 177 REMARK 465 HIS M 178 REMARK 465 HIS M 179 REMARK 465 HIS M 180 REMARK 465 HIS M 181 REMARK 465 LYS J 129 REMARK 465 SER J 130 REMARK 465 THR J 131 REMARK 465 SER J 215 REMARK 465 CYS J 216 REMARK 465 ASP L 1 REMARK 465 CYS L 214 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 GLU C -2 REMARK 465 THR C -1 REMARK 465 GLY C 0 REMARK 465 ALA C 170 REMARK 465 SER C 171 REMARK 465 THR C 172 REMARK 465 GLY C 173 REMARK 465 THR C 174 REMARK 465 LYS C 175 REMARK 465 HIS C 176 REMARK 465 HIS C 177 REMARK 465 HIS C 178 REMARK 465 HIS C 179 REMARK 465 HIS C 180 REMARK 465 HIS C 181 REMARK 465 GLU D -2 REMARK 465 THR D -1 REMARK 465 GLY D 0 REMARK 465 ALA D 170 REMARK 465 SER D 171 REMARK 465 THR D 172 REMARK 465 GLY D 173 REMARK 465 THR D 174 REMARK 465 LYS D 175 REMARK 465 HIS D 176 REMARK 465 HIS D 177 REMARK 465 HIS D 178 REMARK 465 HIS D 179 REMARK 465 HIS D 180 REMARK 465 HIS D 181 REMARK 465 ASP R 1 REMARK 465 CYS R 214 REMARK 465 LYS Q 129 REMARK 465 SER Q 130 REMARK 465 THR Q 131 REMARK 465 SER Q 215 REMARK 465 CYS Q 216 REMARK 465 GLU P -2 REMARK 465 THR P -1 REMARK 465 GLY P 0 REMARK 465 ALA P 170 REMARK 465 SER P 171 REMARK 465 THR P 172 REMARK 465 GLY P 173 REMARK 465 THR P 174 REMARK 465 LYS P 175 REMARK 465 HIS P 176 REMARK 465 HIS P 177 REMARK 465 HIS P 178 REMARK 465 HIS P 179 REMARK 465 HIS P 180 REMARK 465 HIS P 181 REMARK 465 ASP F 1 REMARK 465 CYS F 214 REMARK 465 LYS E 129 REMARK 465 SER E 130 REMARK 465 THR E 131 REMARK 465 SER E 215 REMARK 465 CYS E 216 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 K 30 -144.24 61.94 REMARK 500 ALA K 51 -47.49 63.23 REMARK 500 ALA K 84 -177.96 -172.03 REMARK 500 TYR K 91 -133.81 63.03 REMARK 500 ASN K 138 82.74 51.86 REMARK 500 GLU K 143 108.65 -59.88 REMARK 500 LYS K 169 -64.95 -93.65 REMARK 500 LYS K 188 -81.48 -68.23 REMARK 500 PRO M 9 -169.67 -77.27 REMARK 500 ALA M 33 -134.98 60.46 REMARK 500 ASN M 34 54.31 -114.07 REMARK 500 ASP M 44 -152.60 -103.15 REMARK 500 GLN M 61 -61.11 61.98 REMARK 500 ALA M 129 87.10 -69.47 REMARK 500 ALA M 165 44.49 -160.95 REMARK 500 ASP J 144 77.62 61.16 REMARK 500 ASN L 30 -146.03 61.61 REMARK 500 ALA L 51 -47.42 63.26 REMARK 500 ALA L 84 -179.19 -172.75 REMARK 500 TYR L 91 -133.90 59.95 REMARK 500 ASN L 138 83.11 50.90 REMARK 500 LYS L 169 -64.35 -93.53 REMARK 500 HIS L 189 127.82 66.94 REMARK 500 ASP H 144 78.92 60.21 REMARK 500 ASN C 32 10.35 56.45 REMARK 500 ASN C 34 59.64 -96.18 REMARK 500 ASP C 44 -151.16 -118.56 REMARK 500 GLN C 61 -56.53 65.13 REMARK 500 GLU C 71 -67.98 -129.01 REMARK 500 ALA C 129 82.66 -65.40 REMARK 500 ALA C 165 60.42 -161.26 REMARK 500 ASN D 32 11.16 56.87 REMARK 500 ASN D 34 55.32 -94.07 REMARK 500 ASP D 44 -150.42 -118.70 REMARK 500 GLN D 61 -57.74 63.22 REMARK 500 GLU D 71 -70.38 -128.87 REMARK 500 ALA D 129 79.83 -68.13 REMARK 500 ALA D 165 60.81 -161.68 REMARK 500 ASN R 30 -146.35 61.11 REMARK 500 ALA R 51 -47.70 62.12 REMARK 500 ALA R 84 -179.41 -173.38 REMARK 500 TYR R 91 -132.88 61.75 REMARK 500 ASN R 138 82.29 52.03 REMARK 500 LYS R 169 -65.46 -92.52 REMARK 500 ASP Q 144 79.10 59.48 REMARK 500 ASN P 32 10.79 57.74 REMARK 500 ASN P 34 56.01 -93.41 REMARK 500 ASP P 44 -150.78 -118.32 REMARK 500 GLN P 61 -56.96 63.39 REMARK 500 GLU P 71 -73.05 -127.02 REMARK 500 REMARK 500 THIS ENTRY HAS 60 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 K 308 DISTANCE = 8.14 ANGSTROMS DBREF 9OAS K 1 214 PDB 9OAS 9OAS 1 214 DBREF 9OAS M -2 181 PDB 9OAS 9OAS -2 181 DBREF 9OAS J 1 216 PDB 9OAS 9OAS 1 216 DBREF 9OAS L 1 214 PDB 9OAS 9OAS 1 214 DBREF 9OAS H 1 216 PDB 9OAS 9OAS 1 216 DBREF 9OAS C -2 181 PDB 9OAS 9OAS -2 181 DBREF 9OAS D -2 181 PDB 9OAS 9OAS -2 181 DBREF 9OAS R 1 214 PDB 9OAS 9OAS 1 214 DBREF 9OAS Q 1 216 PDB 9OAS 9OAS 1 216 DBREF 9OAS P -2 181 PDB 9OAS 9OAS -2 181 DBREF 9OAS F 1 214 PDB 9OAS 9OAS 1 214 DBREF 9OAS E 1 216 PDB 9OAS 9OAS 1 216 SEQRES 1 K 210 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 K 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 K 210 GLN ASP ILE ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 K 210 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 K 210 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 K 210 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU SEQRES 7 K 210 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 K 210 GLU PHE PHE GLY GLY GLY THR LYS VAL GLU ILE LYS ARG SEQRES 9 K 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 K 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 K 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 K 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 K 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 K 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 K 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 K 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 K 210 GLU CYS SEQRES 1 M 184 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 M 184 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 M 184 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 M 184 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 M 184 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 M 184 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 M 184 ARG SER GLU ASN TRP THR ASP ASN ALA LYS SER ILE CYS SEQRES 8 M 184 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 M 184 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 M 184 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 M 184 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 M 184 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 M 184 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 M 184 THR TRP PHE ALA SER THR GLY THR LYS HIS HIS HIS HIS SEQRES 15 M 184 HIS HIS SEQRES 1 J 224 GLN VAL GLN SER VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 J 224 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 J 224 TYR THR PHE THR GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 J 224 ALA PRO GLY GLN GLY LEU GLU TRP VAL GLY TRP ILE ASN SEQRES 5 J 224 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 J 224 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 J 224 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 J 224 ALA VAL TYR TYR CYS ALA ARG VAL SER GLN TYR SER SER SEQRES 9 J 224 GLY TRP TYR PHE GLY TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 J 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 J 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 J 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 J 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 J 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 J 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 J 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 J 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 J 224 LYS SER CYS SEQRES 1 L 210 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 L 210 GLN ASP ILE ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 210 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 210 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 210 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU SEQRES 7 L 210 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 210 GLU PHE PHE GLY GLY GLY THR LYS VAL GLU ILE LYS ARG SEQRES 9 L 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 L 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 L 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 L 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 L 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 L 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 L 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 L 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 L 210 GLU CYS SEQRES 1 H 224 GLN VAL GLN SER VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 224 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 224 TYR THR PHE THR GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 224 ALA PRO GLY GLN GLY LEU GLU TRP VAL GLY TRP ILE ASN SEQRES 5 H 224 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 224 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 224 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 H 224 ALA VAL TYR TYR CYS ALA ARG VAL SER GLN TYR SER SER SEQRES 9 H 224 GLY TRP TYR PHE GLY TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 H 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 H 224 LYS SER CYS SEQRES 1 C 184 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 C 184 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 C 184 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 C 184 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 C 184 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 C 184 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 C 184 ARG SER GLU ASN TRP THR ASP ASN ALA LYS SER ILE CYS SEQRES 8 C 184 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 C 184 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 C 184 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 C 184 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 C 184 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 C 184 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 C 184 THR TRP PHE ALA SER THR GLY THR LYS HIS HIS HIS HIS SEQRES 15 C 184 HIS HIS SEQRES 1 D 184 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 D 184 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 D 184 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 D 184 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 D 184 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 D 184 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 D 184 ARG SER GLU ASN TRP THR ASP ASN ALA LYS SER ILE CYS SEQRES 8 D 184 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 D 184 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 D 184 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 D 184 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 D 184 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 D 184 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 D 184 THR TRP PHE ALA SER THR GLY THR LYS HIS HIS HIS HIS SEQRES 15 D 184 HIS HIS SEQRES 1 R 210 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 R 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 R 210 GLN ASP ILE ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 R 210 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 R 210 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 R 210 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU SEQRES 7 R 210 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 R 210 GLU PHE PHE GLY GLY GLY THR LYS VAL GLU ILE LYS ARG SEQRES 9 R 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 R 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 R 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 R 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 R 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 R 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 R 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 R 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 R 210 GLU CYS SEQRES 1 Q 224 GLN VAL GLN SER VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 Q 224 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 Q 224 TYR THR PHE THR GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 Q 224 ALA PRO GLY GLN GLY LEU GLU TRP VAL GLY TRP ILE ASN SEQRES 5 Q 224 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 Q 224 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 Q 224 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 Q 224 ALA VAL TYR TYR CYS ALA ARG VAL SER GLN TYR SER SER SEQRES 9 Q 224 GLY TRP TYR PHE GLY TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 Q 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 Q 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 Q 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 Q 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 Q 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 Q 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 Q 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 Q 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 Q 224 LYS SER CYS SEQRES 1 P 184 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 P 184 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 P 184 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 P 184 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 P 184 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 P 184 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 P 184 ARG SER GLU ASN TRP THR ASP ASN ALA LYS SER ILE CYS SEQRES 8 P 184 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 P 184 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 P 184 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 P 184 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 P 184 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 P 184 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 P 184 THR TRP PHE ALA SER THR GLY THR LYS HIS HIS HIS HIS SEQRES 15 P 184 HIS HIS SEQRES 1 F 210 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 F 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 F 210 GLN ASP ILE ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 F 210 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 F 210 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 F 210 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU SEQRES 7 F 210 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 F 210 GLU PHE PHE GLY GLY GLY THR LYS VAL GLU ILE LYS ARG SEQRES 9 F 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 F 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 F 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 F 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 F 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 F 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 F 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 F 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 F 210 GLU CYS SEQRES 1 E 224 GLN VAL GLN SER VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 E 224 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 E 224 TYR THR PHE THR GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 E 224 ALA PRO GLY GLN GLY LEU GLU TRP VAL GLY TRP ILE ASN SEQRES 5 E 224 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 E 224 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 E 224 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 E 224 ALA VAL TYR TYR CYS ALA ARG VAL SER GLN TYR SER SER SEQRES 9 E 224 GLY TRP TYR PHE GLY TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 E 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 E 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 E 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 E 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 E 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 E 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 E 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 E 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 E 224 LYS SER CYS HET NAG M 201 14 HET NAG M 202 14 HET NAG M 203 14 HET NAG C 201 14 HET NAG C 202 14 HET NAG C 203 14 HET NAG D 201 14 HET NAG D 202 14 HET NAG D 203 14 HET NAG P 201 14 HET NAG P 202 14 HET NAG P 203 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 13 NAG 12(C8 H15 N O6) FORMUL 25 HOH *134(H2 O) HELIX 1 AA1 SER K 121 LYS K 126 1 6 HELIX 2 AA2 LYS K 183 GLU K 187 1 5 HELIX 3 AA3 PRO M 12 SER M 16 5 5 HELIX 4 AA4 ASP M 44 GLN M 52 1 9 HELIX 5 AA5 ARG M 109 GLY M 128 1 20 HELIX 6 AA6 ASP M 141 ASN M 146 1 6 HELIX 7 AA7 SER M 160 PHE M 164 5 5 HELIX 8 AA8 GLN J 61 GLN J 64 5 4 HELIX 9 AA9 ARG J 83 THR J 87 5 5 HELIX 10 AB1 SER J 187 LEU J 189 5 3 HELIX 11 AB2 SER L 121 LYS L 126 1 6 HELIX 12 AB3 LYS L 183 LYS L 188 1 6 HELIX 13 AB4 GLN H 61 GLN H 64 5 4 HELIX 14 AB5 ARG H 83 THR H 87 5 5 HELIX 15 AB6 SER H 187 LEU H 189 5 3 HELIX 16 AB7 LYS H 201 ASN H 204 5 4 HELIX 17 AB8 PRO C 12 SER C 16 5 5 HELIX 18 AB9 ASP C 44 ARG C 50 1 7 HELIX 19 AC1 ARG C 109 GLY C 128 1 20 HELIX 20 AC2 ASP C 141 ASN C 146 1 6 HELIX 21 AC3 SER C 160 PHE C 164 5 5 HELIX 22 AC4 PRO D 12 SER D 16 5 5 HELIX 23 AC5 ASP D 44 ARG D 50 1 7 HELIX 24 AC6 ARG D 109 GLY D 128 1 20 HELIX 25 AC7 ASP D 141 ASN D 146 1 6 HELIX 26 AC8 SER D 160 PHE D 164 5 5 HELIX 27 AC9 SER R 121 LYS R 126 1 6 HELIX 28 AD1 LYS R 183 GLU R 187 1 5 HELIX 29 AD2 GLN Q 61 GLN Q 64 5 4 HELIX 30 AD3 ARG Q 83 THR Q 87 5 5 HELIX 31 AD4 SER Q 156 ALA Q 158 5 3 HELIX 32 AD5 SER Q 187 LEU Q 189 5 3 HELIX 33 AD6 PRO P 12 SER P 16 5 5 HELIX 34 AD7 ASP P 44 ARG P 50 1 7 HELIX 35 AD8 ARG P 109 GLY P 128 1 20 HELIX 36 AD9 ASP P 141 ASN P 146 1 6 HELIX 37 AE1 SER P 160 PHE P 164 5 5 HELIX 38 AE2 SER F 121 LYS F 126 1 6 HELIX 39 AE3 LYS F 183 LYS F 188 1 6 HELIX 40 AE4 GLN E 61 GLN E 64 5 4 HELIX 41 AE5 ARG E 83 THR E 87 5 5 HELIX 42 AE6 SER E 187 LEU E 189 5 3 SHEET 1 AA1 4 MET K 4 SER K 7 0 SHEET 2 AA1 4 VAL K 19 ALA K 25 -1 O GLN K 24 N THR K 5 SHEET 3 AA1 4 ASP K 70 ILE K 75 -1 O PHE K 73 N ILE K 21 SHEET 4 AA1 4 PHE K 62 SER K 67 -1 N SER K 63 O THR K 74 SHEET 1 AA2 6 SER K 10 ALA K 13 0 SHEET 2 AA2 6 THR K 102 ILE K 106 1 O GLU K 105 N LEU K 11 SHEET 3 AA2 6 THR K 85 GLN K 90 -1 N TYR K 86 O THR K 102 SHEET 4 AA2 6 ASN K 34 GLN K 38 -1 N TYR K 36 O TYR K 87 SHEET 5 AA2 6 LYS K 45 TYR K 49 -1 O ILE K 48 N TRP K 35 SHEET 6 AA2 6 ASN K 53 LEU K 54 -1 O ASN K 53 N TYR K 49 SHEET 1 AA3 4 SER K 10 ALA K 13 0 SHEET 2 AA3 4 THR K 102 ILE K 106 1 O GLU K 105 N LEU K 11 SHEET 3 AA3 4 THR K 85 GLN K 90 -1 N TYR K 86 O THR K 102 SHEET 4 AA3 4 PHE K 97 PHE K 98 -1 O PHE K 97 N GLN K 90 SHEET 1 AA4 4 SER K 114 PHE K 118 0 SHEET 2 AA4 4 THR K 129 PHE K 139 -1 O ASN K 137 N SER K 114 SHEET 3 AA4 4 TYR K 173 SER K 182 -1 O LEU K 179 N VAL K 132 SHEET 4 AA4 4 SER K 159 VAL K 163 -1 N GLN K 160 O THR K 178 SHEET 1 AA5 4 ALA K 153 LEU K 154 0 SHEET 2 AA5 4 LYS K 145 VAL K 150 -1 N VAL K 150 O ALA K 153 SHEET 3 AA5 4 VAL K 191 THR K 197 -1 O ALA K 193 N LYS K 149 SHEET 4 AA5 4 VAL K 205 ASN K 210 -1 O VAL K 205 N VAL K 196 SHEET 1 AA6 7 LEU M 62 LEU M 64 0 SHEET 2 AA6 7 SER M 17 ARG M 26 -1 N GLY M 21 O PHE M 63 SHEET 3 AA6 7 ILE M 87 CYS M 99 -1 O VAL M 95 N ILE M 19 SHEET 4 AA6 7 HIS M 104 SER M 108 -1 O ALA M 106 N ALA M 98 SHEET 5 AA6 7 THR M 2 ARG M 8 -1 N ILE M 3 O ILE M 107 SHEET 6 AA6 7 PHE M 155 CYS M 158 -1 O TYR M 157 N ARG M 8 SHEET 7 AA6 7 HIS M 147 ASN M 150 -1 N HIS M 147 O CYS M 158 SHEET 1 AA7 6 VAL M 74 ARG M 76 0 SHEET 2 AA7 6 ILE M 87 CYS M 99 -1 O CYS M 88 N ARG M 76 SHEET 3 AA7 6 SER M 17 ARG M 26 -1 N ILE M 19 O VAL M 95 SHEET 4 AA7 6 THR M 35 PRO M 40 -1 O ARG M 39 N THR M 25 SHEET 5 AA7 6 THR M 131 PHE M 134 1 O THR M 131 N VAL M 36 SHEET 6 AA7 6 THR M 167 TRP M 168 -1 O TRP M 168 N ILE M 132 SHEET 1 AA8 4 GLN J 3 GLN J 6 0 SHEET 2 AA8 4 VAL J 18 SER J 25 -1 O LYS J 23 N VAL J 5 SHEET 3 AA8 4 THR J 77 LEU J 82 -1 O MET J 80 N VAL J 20 SHEET 4 AA8 4 VAL J 67 ASP J 72 -1 N THR J 70 O TYR J 79 SHEET 1 AA9 6 GLU J 10 LYS J 12 0 SHEET 2 AA9 6 THR J 107 VAL J 111 1 O THR J 110 N LYS J 12 SHEET 3 AA9 6 ALA J 88 SER J 96 -1 N TYR J 90 O THR J 107 SHEET 4 AA9 6 TYR J 32 GLN J 39 -1 N TYR J 33 O VAL J 95 SHEET 5 AA9 6 LEU J 45 ILE J 51 -1 O VAL J 48 N TRP J 36 SHEET 6 AA9 6 THR J 57 TYR J 59 -1 O ASN J 58 N TRP J 50 SHEET 1 AB1 4 SER J 120 LEU J 124 0 SHEET 2 AB1 4 THR J 135 TYR J 145 -1 O LEU J 141 N PHE J 122 SHEET 3 AB1 4 TYR J 176 PRO J 185 -1 O VAL J 184 N ALA J 136 SHEET 4 AB1 4 VAL J 163 THR J 165 -1 N HIS J 164 O VAL J 181 SHEET 1 AB2 4 SER J 120 LEU J 124 0 SHEET 2 AB2 4 THR J 135 TYR J 145 -1 O LEU J 141 N PHE J 122 SHEET 3 AB2 4 TYR J 176 PRO J 185 -1 O VAL J 184 N ALA J 136 SHEET 4 AB2 4 VAL J 169 LEU J 170 -1 N VAL J 169 O SER J 177 SHEET 1 AB3 3 THR J 151 TRP J 154 0 SHEET 2 AB3 3 ILE J 195 HIS J 200 -1 O ASN J 197 N SER J 153 SHEET 3 AB3 3 THR J 205 LYS J 210 -1 O VAL J 207 N VAL J 198 SHEET 1 AB4 4 MET L 4 SER L 7 0 SHEET 2 AB4 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AB4 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AB4 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB512 ASN L 53 LEU L 54 0 SHEET 2 AB512 LYS L 45 TYR L 49 -1 N TYR L 49 O ASN L 53 SHEET 3 AB512 ASN L 34 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AB512 ALA L 84 GLN L 90 -1 O TYR L 87 N TYR L 36 SHEET 5 AB512 THR L 102 ILE L 106 -1 O VAL L 104 N ALA L 84 SHEET 6 AB512 SER L 10 ALA L 13 1 N LEU L 11 O GLU L 105 SHEET 7 AB512 SER F 10 ALA F 13 -1 O SER F 12 N SER L 10 SHEET 8 AB512 THR F 102 ILE F 106 1 O GLU F 105 N LEU F 11 SHEET 9 AB512 THR F 85 GLN F 90 -1 N TYR F 86 O THR F 102 SHEET 10 AB512 ASN F 34 GLN F 38 -1 N TYR F 36 O TYR F 87 SHEET 11 AB512 LYS F 45 TYR F 49 -1 O LYS F 45 N GLN F 37 SHEET 12 AB512 ASN F 53 LEU F 54 -1 O ASN F 53 N TYR F 49 SHEET 1 AB6 8 PHE L 97 PHE L 98 0 SHEET 2 AB6 8 ALA L 84 GLN L 90 -1 N GLN L 90 O PHE L 97 SHEET 3 AB6 8 THR L 102 ILE L 106 -1 O VAL L 104 N ALA L 84 SHEET 4 AB6 8 SER L 10 ALA L 13 1 N LEU L 11 O GLU L 105 SHEET 5 AB6 8 SER F 10 ALA F 13 -1 O SER F 12 N SER L 10 SHEET 6 AB6 8 THR F 102 ILE F 106 1 O GLU F 105 N LEU F 11 SHEET 7 AB6 8 THR F 85 GLN F 90 -1 N TYR F 86 O THR F 102 SHEET 8 AB6 8 PHE F 97 PHE F 98 -1 O PHE F 97 N GLN F 90 SHEET 1 AB7 4 SER L 114 PHE L 118 0 SHEET 2 AB7 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AB7 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB7 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB8 4 ALA L 153 LEU L 154 0 SHEET 2 AB8 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB8 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB8 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB9 4 GLN H 3 GLN H 6 0 SHEET 2 AB9 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AB9 4 THR H 77 LEU H 82 -1 O MET H 80 N VAL H 20 SHEET 4 AB9 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AC1 6 GLU H 10 LYS H 12 0 SHEET 2 AC1 6 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 AC1 6 ALA H 88 SER H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AC1 6 TYR H 32 GLN H 39 -1 N TYR H 33 O VAL H 95 SHEET 5 AC1 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AC1 6 THR H 57 TYR H 59 -1 O ASN H 58 N TRP H 50 SHEET 1 AC2 4 SER H 120 LEU H 124 0 SHEET 2 AC2 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AC2 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AC2 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AC3 4 SER H 120 LEU H 124 0 SHEET 2 AC3 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AC3 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AC3 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AC4 3 THR H 151 TRP H 154 0 SHEET 2 AC4 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AC4 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AC5 7 LEU C 62 LEU C 64 0 SHEET 2 AC5 7 SER C 17 ARG C 26 -1 N GLY C 21 O PHE C 63 SHEET 3 AC5 7 ILE C 87 CYS C 99 -1 O VAL C 95 N ILE C 19 SHEET 4 AC5 7 HIS C 104 SER C 108 -1 O ALA C 106 N ALA C 98 SHEET 5 AC5 7 THR C 2 ARG C 8 -1 N ILE C 3 O ILE C 107 SHEET 6 AC5 7 PHE C 155 CYS C 158 -1 O TYR C 157 N ARG C 8 SHEET 7 AC5 7 HIS C 147 ASN C 150 -1 N HIS C 147 O CYS C 158 SHEET 1 AC6 6 VAL C 74 SER C 77 0 SHEET 2 AC6 6 ILE C 87 CYS C 99 -1 O CYS C 88 N ARG C 76 SHEET 3 AC6 6 SER C 17 ARG C 26 -1 N ILE C 19 O VAL C 95 SHEET 4 AC6 6 THR C 35 PRO C 40 -1 O ARG C 39 N THR C 25 SHEET 5 AC6 6 THR C 131 PHE C 134 1 O THR C 131 N VAL C 36 SHEET 6 AC6 6 SER C 166 TRP C 168 -1 O TRP C 168 N ILE C 132 SHEET 1 AC7 7 LEU D 62 LEU D 64 0 SHEET 2 AC7 7 SER D 17 ARG D 26 -1 N GLY D 21 O PHE D 63 SHEET 3 AC7 7 ILE D 87 CYS D 99 -1 O VAL D 95 N ILE D 19 SHEET 4 AC7 7 HIS D 104 SER D 108 -1 O ALA D 106 N ALA D 98 SHEET 5 AC7 7 THR D 2 ARG D 8 -1 N ILE D 3 O ILE D 107 SHEET 6 AC7 7 PHE D 155 CYS D 158 -1 O TYR D 157 N ARG D 8 SHEET 7 AC7 7 HIS D 147 ASN D 150 -1 N HIS D 147 O CYS D 158 SHEET 1 AC8 6 VAL D 74 SER D 77 0 SHEET 2 AC8 6 ILE D 87 CYS D 99 -1 O CYS D 88 N ARG D 76 SHEET 3 AC8 6 SER D 17 ARG D 26 -1 N ILE D 19 O VAL D 95 SHEET 4 AC8 6 THR D 35 PRO D 40 -1 O ARG D 39 N THR D 25 SHEET 5 AC8 6 THR D 131 PHE D 134 1 O THR D 131 N VAL D 36 SHEET 6 AC8 6 SER D 166 TRP D 168 -1 O SER D 166 N PHE D 134 SHEET 1 AC9 4 MET R 4 SER R 7 0 SHEET 2 AC9 4 VAL R 19 ALA R 25 -1 O THR R 22 N SER R 7 SHEET 3 AC9 4 ASP R 70 ILE R 75 -1 O PHE R 73 N ILE R 21 SHEET 4 AC9 4 PHE R 62 SER R 67 -1 N SER R 63 O THR R 74 SHEET 1 AD1 6 SER R 10 ALA R 13 0 SHEET 2 AD1 6 THR R 102 ILE R 106 1 O GLU R 105 N LEU R 11 SHEET 3 AD1 6 ALA R 84 GLN R 90 -1 N ALA R 84 O VAL R 104 SHEET 4 AD1 6 ASN R 34 GLN R 38 -1 N TYR R 36 O TYR R 87 SHEET 5 AD1 6 LYS R 45 TYR R 49 -1 O ILE R 48 N TRP R 35 SHEET 6 AD1 6 ASN R 53 LEU R 54 -1 O ASN R 53 N TYR R 49 SHEET 1 AD2 4 SER R 10 ALA R 13 0 SHEET 2 AD2 4 THR R 102 ILE R 106 1 O GLU R 105 N LEU R 11 SHEET 3 AD2 4 ALA R 84 GLN R 90 -1 N ALA R 84 O VAL R 104 SHEET 4 AD2 4 PHE R 97 PHE R 98 -1 O PHE R 97 N GLN R 90 SHEET 1 AD3 4 SER R 114 PHE R 118 0 SHEET 2 AD3 4 THR R 129 PHE R 139 -1 O LEU R 135 N PHE R 116 SHEET 3 AD3 4 TYR R 173 SER R 182 -1 O LEU R 181 N ALA R 130 SHEET 4 AD3 4 SER R 159 VAL R 163 -1 N GLN R 160 O THR R 178 SHEET 1 AD4 4 ALA R 153 GLN R 155 0 SHEET 2 AD4 4 LYS R 145 VAL R 150 -1 N TRP R 148 O GLN R 155 SHEET 3 AD4 4 VAL R 191 THR R 197 -1 O GLU R 195 N GLN R 147 SHEET 4 AD4 4 VAL R 205 ASN R 210 -1 O VAL R 205 N VAL R 196 SHEET 1 AD5 4 GLN Q 3 GLN Q 6 0 SHEET 2 AD5 4 VAL Q 18 SER Q 25 -1 O LYS Q 23 N VAL Q 5 SHEET 3 AD5 4 THR Q 77 LEU Q 82 -1 O MET Q 80 N VAL Q 20 SHEET 4 AD5 4 VAL Q 67 ASP Q 72 -1 N THR Q 68 O GLU Q 81 SHEET 1 AD6 6 GLU Q 10 LYS Q 12 0 SHEET 2 AD6 6 THR Q 107 VAL Q 111 1 O THR Q 110 N LYS Q 12 SHEET 3 AD6 6 ALA Q 88 SER Q 96 -1 N TYR Q 90 O THR Q 107 SHEET 4 AD6 6 TYR Q 32 GLN Q 39 -1 N VAL Q 37 O TYR Q 91 SHEET 5 AD6 6 LEU Q 45 ILE Q 51 -1 O VAL Q 48 N TRP Q 36 SHEET 6 AD6 6 THR Q 57 TYR Q 59 -1 O ASN Q 58 N TRP Q 50 SHEET 1 AD7 4 SER Q 120 LEU Q 124 0 SHEET 2 AD7 4 THR Q 135 TYR Q 145 -1 O LEU Q 141 N PHE Q 122 SHEET 3 AD7 4 TYR Q 176 PRO Q 185 -1 O VAL Q 184 N ALA Q 136 SHEET 4 AD7 4 VAL Q 163 THR Q 165 -1 N HIS Q 164 O VAL Q 181 SHEET 1 AD8 4 SER Q 120 LEU Q 124 0 SHEET 2 AD8 4 THR Q 135 TYR Q 145 -1 O LEU Q 141 N PHE Q 122 SHEET 3 AD8 4 TYR Q 176 PRO Q 185 -1 O VAL Q 184 N ALA Q 136 SHEET 4 AD8 4 VAL Q 169 LEU Q 170 -1 N VAL Q 169 O SER Q 177 SHEET 1 AD9 3 THR Q 151 TRP Q 154 0 SHEET 2 AD9 3 ILE Q 195 HIS Q 200 -1 O ASN Q 197 N SER Q 153 SHEET 3 AD9 3 THR Q 205 LYS Q 210 -1 O VAL Q 207 N VAL Q 198 SHEET 1 AE1 7 LEU P 62 LEU P 64 0 SHEET 2 AE1 7 SER P 17 ARG P 26 -1 N GLY P 21 O PHE P 63 SHEET 3 AE1 7 ILE P 87 CYS P 99 -1 O VAL P 95 N ILE P 19 SHEET 4 AE1 7 HIS P 104 SER P 108 -1 O ALA P 106 N ALA P 98 SHEET 5 AE1 7 THR P 2 ARG P 8 -1 N ILE P 3 O ILE P 107 SHEET 6 AE1 7 PHE P 155 CYS P 158 -1 O TYR P 157 N ARG P 8 SHEET 7 AE1 7 HIS P 147 ASN P 150 -1 N HIS P 147 O CYS P 158 SHEET 1 AE2 6 VAL P 74 SER P 77 0 SHEET 2 AE2 6 ILE P 87 CYS P 99 -1 O GLN P 90 N VAL P 74 SHEET 3 AE2 6 SER P 17 ARG P 26 -1 N ILE P 19 O VAL P 95 SHEET 4 AE2 6 THR P 35 PRO P 40 -1 O ARG P 39 N THR P 25 SHEET 5 AE2 6 THR P 131 PHE P 134 1 O THR P 131 N VAL P 36 SHEET 6 AE2 6 SER P 166 TRP P 168 -1 O SER P 166 N PHE P 134 SHEET 1 AE3 4 THR F 5 SER F 7 0 SHEET 2 AE3 4 VAL F 19 GLN F 24 -1 O GLN F 24 N THR F 5 SHEET 3 AE3 4 ASP F 70 ILE F 75 -1 O PHE F 73 N ILE F 21 SHEET 4 AE3 4 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74 SHEET 1 AE4 4 SER F 114 PHE F 118 0 SHEET 2 AE4 4 THR F 129 PHE F 139 -1 O ASN F 137 N SER F 114 SHEET 3 AE4 4 TYR F 173 SER F 182 -1 O LEU F 179 N VAL F 132 SHEET 4 AE4 4 SER F 159 VAL F 163 -1 N GLN F 160 O THR F 178 SHEET 1 AE5 4 ALA F 153 LEU F 154 0 SHEET 2 AE5 4 LYS F 145 VAL F 150 -1 N VAL F 150 O ALA F 153 SHEET 3 AE5 4 VAL F 191 THR F 197 -1 O GLU F 195 N GLN F 147 SHEET 4 AE5 4 VAL F 205 ASN F 210 -1 O VAL F 205 N VAL F 196 SHEET 1 AE6 4 GLN E 3 GLN E 6 0 SHEET 2 AE6 4 VAL E 18 SER E 25 -1 O LYS E 23 N VAL E 5 SHEET 3 AE6 4 THR E 77 LEU E 82 -1 O MET E 80 N VAL E 20 SHEET 4 AE6 4 VAL E 67 ASP E 72 -1 N THR E 70 O TYR E 79 SHEET 1 AE7 6 GLU E 10 LYS E 12 0 SHEET 2 AE7 6 THR E 107 VAL E 111 1 O THR E 110 N LYS E 12 SHEET 3 AE7 6 ALA E 88 SER E 96 -1 N TYR E 90 O THR E 107 SHEET 4 AE7 6 TYR E 32 GLN E 39 -1 N VAL E 37 O TYR E 91 SHEET 5 AE7 6 LEU E 45 ILE E 51 -1 O VAL E 48 N TRP E 36 SHEET 6 AE7 6 THR E 57 TYR E 59 -1 O ASN E 58 N TRP E 50 SHEET 1 AE8 4 SER E 120 LEU E 124 0 SHEET 2 AE8 4 THR E 135 TYR E 145 -1 O LEU E 141 N PHE E 122 SHEET 3 AE8 4 TYR E 176 PRO E 185 -1 O TYR E 176 N TYR E 145 SHEET 4 AE8 4 VAL E 163 THR E 165 -1 N HIS E 164 O VAL E 181 SHEET 1 AE9 4 SER E 120 LEU E 124 0 SHEET 2 AE9 4 THR E 135 TYR E 145 -1 O LEU E 141 N PHE E 122 SHEET 3 AE9 4 TYR E 176 PRO E 185 -1 O TYR E 176 N TYR E 145 SHEET 4 AE9 4 VAL E 169 LEU E 170 -1 N VAL E 169 O SER E 177 SHEET 1 AF1 3 THR E 151 TRP E 154 0 SHEET 2 AF1 3 TYR E 194 HIS E 200 -1 O ASN E 197 N SER E 153 SHEET 3 AF1 3 THR E 205 VAL E 211 -1 O VAL E 211 N TYR E 194 SSBOND 1 CYS K 23 CYS K 88 1555 1555 2.04 SSBOND 2 CYS K 134 CYS K 194 1555 1555 2.04 SSBOND 3 CYS M 7 CYS M 158 1555 1555 2.03 SSBOND 4 CYS M 15 CYS M 151 1555 1555 2.03 SSBOND 5 CYS M 51 CYS M 88 1555 1555 2.03 SSBOND 6 CYS M 99 CYS M 105 1555 1555 2.04 SSBOND 7 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 8 CYS J 140 CYS J 196 1555 1555 2.03 SSBOND 9 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 10 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 11 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 12 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 13 CYS C 7 CYS C 158 1555 1555 2.03 SSBOND 14 CYS C 15 CYS C 151 1555 1555 2.04 SSBOND 15 CYS C 51 CYS C 88 1555 1555 2.03 SSBOND 16 CYS C 99 CYS C 105 1555 1555 2.04 SSBOND 17 CYS D 7 CYS D 158 1555 1555 2.03 SSBOND 18 CYS D 15 CYS D 151 1555 1555 2.04 SSBOND 19 CYS D 51 CYS D 88 1555 1555 2.03 SSBOND 20 CYS D 99 CYS D 105 1555 1555 2.04 SSBOND 21 CYS R 23 CYS R 88 1555 1555 2.04 SSBOND 22 CYS R 134 CYS R 194 1555 1555 2.03 SSBOND 23 CYS Q 22 CYS Q 92 1555 1555 2.03 SSBOND 24 CYS Q 140 CYS Q 196 1555 1555 2.04 SSBOND 25 CYS P 7 CYS P 158 1555 1555 2.03 SSBOND 26 CYS P 15 CYS P 151 1555 1555 2.03 SSBOND 27 CYS P 51 CYS P 88 1555 1555 2.03 SSBOND 28 CYS P 99 CYS P 105 1555 1555 2.04 SSBOND 29 CYS F 23 CYS F 88 1555 1555 2.04 SSBOND 30 CYS F 134 CYS F 194 1555 1555 2.04 SSBOND 31 CYS E 22 CYS E 92 1555 1555 2.03 SSBOND 32 CYS E 140 CYS E 196 1555 1555 2.03 LINK ND2 ASN M 18 C1 NAG M 201 1555 1555 1.44 LINK ND2 ASN M 65 C1 NAG M 202 1555 1555 1.44 LINK ND2 ASN M 79 C1 NAG M 203 1555 1555 1.44 LINK ND2 ASN C 18 C1 NAG C 201 1555 1555 1.44 LINK ND2 ASN C 65 C1 NAG C 202 1555 1555 1.44 LINK ND2 ASN C 79 C1 NAG C 203 1555 1555 1.44 LINK ND2 ASN D 18 C1 NAG D 201 1555 1555 1.44 LINK ND2 ASN D 65 C1 NAG D 202 1555 1555 1.44 LINK ND2 ASN D 79 C1 NAG D 203 1555 1555 1.44 LINK ND2 ASN P 18 C1 NAG P 201 1555 1555 1.44 LINK ND2 ASN P 65 C1 NAG P 202 1555 1555 1.44 LINK ND2 ASN P 79 C1 NAG P 203 1555 1555 1.44 CISPEP 1 SER K 7 PRO K 8 0 0.48 CISPEP 2 TYR K 140 PRO K 141 0 2.01 CISPEP 3 ARG M 8 PRO M 9 0 -1.11 CISPEP 4 PHE J 146 PRO J 147 0 -4.36 CISPEP 5 GLU J 148 PRO J 149 0 -1.85 CISPEP 6 SER L 7 PRO L 8 0 -1.67 CISPEP 7 TYR L 140 PRO L 141 0 3.16 CISPEP 8 PHE H 146 PRO H 147 0 -3.18 CISPEP 9 GLU H 148 PRO H 149 0 -0.23 CISPEP 10 ARG C 8 PRO C 9 0 -4.93 CISPEP 11 ARG D 8 PRO D 9 0 -2.82 CISPEP 12 SER R 7 PRO R 8 0 0.27 CISPEP 13 TYR R 140 PRO R 141 0 2.30 CISPEP 14 PHE Q 146 PRO Q 147 0 -3.57 CISPEP 15 GLU Q 148 PRO Q 149 0 -1.14 CISPEP 16 ARG P 8 PRO P 9 0 -4.03 CISPEP 17 SER F 7 PRO F 8 0 -0.69 CISPEP 18 TYR F 140 PRO F 141 0 3.85 CISPEP 19 PHE E 146 PRO E 147 0 -3.66 CISPEP 20 GLU E 148 PRO E 149 0 -1.47 CRYST1 261.056 75.518 158.146 90.00 92.36 90.00 C 1 2 1 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 0.003831 0.000000 0.000158 0.00000 SCALE2 0.000000 0.013242 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006329 0.00000 MTRIX1 1 -0.871612 0.148719 0.467092 -6.70490 1 MTRIX2 1 0.099290 0.986678 -0.128873 13.46275 1 MTRIX3 1 -0.480035 -0.065950 -0.874767 80.50827 1 MTRIX1 2 0.823100 0.497590 0.273699 -21.37801 1 MTRIX2 2 0.502113 -0.862814 0.058598 -21.20429 1 MTRIX3 2 0.265309 0.089196 -0.960029 41.75185 1 MTRIX1 3 0.521111 0.483297 0.703468 -45.41368 1 MTRIX2 3 0.487736 -0.845013 0.219240 -15.25770 1 MTRIX3 3 0.700398 0.228858 -0.676067 108.12204 1 MTRIX1 4 0.576192 0.423810 0.698848 -44.49879 1 MTRIX2 4 0.437370 -0.882209 0.174401 -13.50289 1 MTRIX3 4 0.690442 0.205166 -0.693683 108.97357 1 MTRIX1 5 0.708259 0.215665 0.672203 -50.17715 1 MTRIX2 5 -0.123585 0.975367 -0.182716 -2.25151 1 MTRIX3 5 -0.695051 0.046336 0.717466 -65.40507 1 MTRIX1 6 -0.025925 -0.452644 -0.891314 80.92185 1 MTRIX2 6 0.402313 -0.820946 0.405206 -23.06897 1 MTRIX3 6 -0.915135 -0.348082 0.203387 11.32054 1 MTRIX1 7 0.633260 0.324522 0.702614 -48.32499 1 MTRIX2 7 -0.356287 0.928163 -0.107579 -15.34692 1 MTRIX3 7 -0.687053 -0.182206 0.703392 -69.67193 1 MTRIX1 8 0.572429 0.420552 0.703890 -45.21327 1 MTRIX2 8 0.416145 -0.888681 0.192534 -14.97243 1 MTRIX3 8 0.706504 0.182708 -0.683718 108.38190 1 MTRIX1 9 -0.008656 -0.445586 -0.895197 81.61468 1 MTRIX2 9 0.417229 -0.815190 0.401727 -22.00408 1 MTRIX3 9 -0.908760 -0.370025 0.192968 11.36578 1