HEADER IMMUNE SYSTEM/VIRAL PROTEIN 06-MAY-24 9BP1 TITLE RHESUS MACAQUE ITS110.01 FAB IN COMPLEX WITH SIV ENV MPER PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ITS110.01 HEAVY CHAIN; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ITS110.01 LIGHT CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 11 CHAIN: I, E; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 8 ORGANISM_TAXID: 9544; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: SIMIAN IMMUNODEFICIENCY VIRUS; SOURCE 14 ORGANISM_TAXID: 11723 KEYWDS FAB, MPER, MEMBRANE-PROXIMAL EXTERNAL REGION, HIV-1, GP41, IMMUNE KEYWDS 2 SYSTEM, SIV, ANTIBODY, IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR J.GORMAN,P.D.KWONG REVDAT 1 15-JAN-25 9BP1 0 JRNL AUTH J.GORMAN,M.AHMADI,P.D.KWONG JRNL TITL ISOLATION AND STRUCTURE OF BROAD SIV-NEUTRALIZING ANTIBODIES JRNL TITL 2 REVEAL A PROXIMAL HELICAL MPER EPITOPE RECOGNIZED BY A JRNL TITL 3 RHESUS MULTI-DONOR CLASS JRNL REF CELL REP 2025 JRNL REFN ESSN 2211-1247 REMARK 2 REMARK 2 RESOLUTION. 3.58 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX DEV_5278 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) : 3.58 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.72 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.8 REMARK 3 NUMBER OF REFLECTIONS : 12088 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.223 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 605 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 39.7200 - 5.6700 0.95 3319 175 0.2073 0.2458 REMARK 3 2 5.6700 - 4.5100 0.96 3251 172 0.1997 0.2562 REMARK 3 3 4.5000 - 3.9400 0.94 3142 165 0.2268 0.2460 REMARK 3 4 3.9400 - 3.5800 0.53 1771 93 0.2775 0.3949 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.451 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.801 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 42.46 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.50 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 : 0.002 6980 REMARK 3 ANGLE : 0.441 9512 REMARK 3 CHIRALITY : 0.042 1088 REMARK 3 PLANARITY : 0.004 1207 REMARK 3 DIHEDRAL : 11.969 2464 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): 62.4977 -66.8408 -8.1044 REMARK 3 T TENSOR REMARK 3 T11: 0.2407 T22: 0.7879 REMARK 3 T33: 0.3045 T12: 0.1320 REMARK 3 T13: 0.0592 T23: 0.7040 REMARK 3 L TENSOR REMARK 3 L11: 0.0876 L22: 0.0182 REMARK 3 L33: 0.2110 L12: -0.0376 REMARK 3 L13: -0.0025 L23: -0.0030 REMARK 3 S TENSOR REMARK 3 S11: 0.2866 S12: -0.1038 S13: 0.0269 REMARK 3 S21: -0.0942 S22: 0.2299 S23: 0.1596 REMARK 3 S31: -0.1405 S32: -0.4338 S33: 0.6450 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 110 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 74.8717 -42.2065 -31.2313 REMARK 3 T TENSOR REMARK 3 T11: 0.1540 T22: 0.0357 REMARK 3 T33: 0.0755 T12: 0.1514 REMARK 3 T13: 0.2894 T23: -0.0272 REMARK 3 L TENSOR REMARK 3 L11: 0.2009 L22: 0.0323 REMARK 3 L33: 0.0159 L12: 0.0633 REMARK 3 L13: 0.0604 L23: 0.0180 REMARK 3 S TENSOR REMARK 3 S11: -0.2327 S12: 0.0578 S13: -0.1331 REMARK 3 S21: 0.2182 S22: 0.1914 S23: 0.0978 REMARK 3 S31: -0.0515 S32: -0.0303 S33: -0.0425 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): 83.1776 -72.9859 -12.9293 REMARK 3 T TENSOR REMARK 3 T11: 0.0999 T22: -0.1114 REMARK 3 T33: -0.0701 T12: -0.1472 REMARK 3 T13: 0.0925 T23: 0.2574 REMARK 3 L TENSOR REMARK 3 L11: 0.0924 L22: 0.0632 REMARK 3 L33: 0.0463 L12: -0.0828 REMARK 3 L13: -0.0351 L23: 0.0265 REMARK 3 S TENSOR REMARK 3 S11: 0.1722 S12: 0.0395 S13: 0.1141 REMARK 3 S21: -0.2126 S22: 0.1616 S23: 0.0426 REMARK 3 S31: -0.0543 S32: -0.2209 S33: 0.3150 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 88.7322 -39.2930 -24.0691 REMARK 3 T TENSOR REMARK 3 T11: 0.3549 T22: -0.0424 REMARK 3 T33: -0.2932 T12: 0.1059 REMARK 3 T13: 0.0022 T23: 0.2387 REMARK 3 L TENSOR REMARK 3 L11: 0.0839 L22: 0.1077 REMARK 3 L33: 0.0851 L12: -0.0119 REMARK 3 L13: 0.0543 L23: -0.0781 REMARK 3 S TENSOR REMARK 3 S11: -0.1393 S12: -0.0381 S13: -0.0128 REMARK 3 S21: 0.0917 S22: -0.0118 S23: -0.0303 REMARK 3 S31: -0.2403 S32: 0.0143 S33: -0.4037 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 660 THROUGH 675 ) REMARK 3 ORIGIN FOR THE GROUP (A): 62.3287 -81.7400 2.3873 REMARK 3 T TENSOR REMARK 3 T11: 0.3116 T22: 0.4882 REMARK 3 T33: 0.2912 T12: -0.0301 REMARK 3 T13: 0.0067 T23: 0.3649 REMARK 3 L TENSOR REMARK 3 L11: 0.0067 L22: 0.0220 REMARK 3 L33: 0.0505 L12: 0.0027 REMARK 3 L13: -0.0100 L23: -0.0302 REMARK 3 S TENSOR REMARK 3 S11: -0.0040 S12: 0.0216 S13: 0.0004 REMARK 3 S21: 0.0555 S22: -0.0143 S23: 0.0195 REMARK 3 S31: -0.0598 S32: -0.0585 S33: -0.0485 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 660 THROUGH 675 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.8054 -79.2454 1.2710 REMARK 3 T TENSOR REMARK 3 T11: 0.3089 T22: 0.6872 REMARK 3 T33: 0.5481 T12: 0.0301 REMARK 3 T13: 0.0212 T23: -0.4449 REMARK 3 L TENSOR REMARK 3 L11: 0.0005 L22: 0.0008 REMARK 3 L33: 0.0067 L12: 0.0003 REMARK 3 L13: 0.0006 L23: 0.0020 REMARK 3 S TENSOR REMARK 3 S11: 0.0010 S12: 0.0218 S13: -0.0042 REMARK 3 S21: -0.0218 S22: 0.0006 S23: -0.0106 REMARK 3 S31: -0.0311 S32: -0.0107 S33: -0.0014 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.2046 -64.5282 11.7077 REMARK 3 T TENSOR REMARK 3 T11: -0.1279 T22: 1.0753 REMARK 3 T33: 0.8360 T12: -0.0761 REMARK 3 T13: 0.2605 T23: -0.6392 REMARK 3 L TENSOR REMARK 3 L11: 0.0565 L22: 0.0193 REMARK 3 L33: 0.0138 L12: 0.0109 REMARK 3 L13: -0.0040 L23: -0.0049 REMARK 3 S TENSOR REMARK 3 S11: -0.0108 S12: 0.1854 S13: -0.0427 REMARK 3 S21: 0.0406 S22: -0.1088 S23: 0.0951 REMARK 3 S31: -0.0196 S32: -0.0769 S33: -0.1158 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 110 THROUGH 210 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.6527 -37.8426 34.4426 REMARK 3 T TENSOR REMARK 3 T11: 0.3355 T22: 0.4939 REMARK 3 T33: 0.6404 T12: -0.0073 REMARK 3 T13: 0.6015 T23: -0.3535 REMARK 3 L TENSOR REMARK 3 L11: 0.0189 L22: -0.0029 REMARK 3 L33: 0.0142 L12: 0.0101 REMARK 3 L13: -0.0070 L23: -0.0045 REMARK 3 S TENSOR REMARK 3 S11: -0.0139 S12: -0.0122 S13: 0.0080 REMARK 3 S21: 0.1217 S22: 0.0066 S23: 0.0736 REMARK 3 S31: 0.0162 S32: 0.1054 S33: 0.0133 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.5492 -65.1545 16.6328 REMARK 3 T TENSOR REMARK 3 T11: 0.0329 T22: 0.7197 REMARK 3 T33: 0.7850 T12: -0.1669 REMARK 3 T13: 0.3086 T23: -0.4002 REMARK 3 L TENSOR REMARK 3 L11: 0.0691 L22: 0.0237 REMARK 3 L33: 0.0306 L12: -0.0078 REMARK 3 L13: 0.0202 L23: 0.0179 REMARK 3 S TENSOR REMARK 3 S11: 0.1031 S12: 0.1554 S13: -0.0014 REMARK 3 S21: 0.0030 S22: 0.1112 S23: 0.0120 REMARK 3 S31: -0.0661 S32: 0.0684 S33: 0.0997 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 111 THROUGH 210 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.0049 -31.2092 27.3549 REMARK 3 T TENSOR REMARK 3 T11: 0.5759 T22: 0.9147 REMARK 3 T33: 1.3741 T12: 0.3003 REMARK 3 T13: 0.4534 T23: -0.2499 REMARK 3 L TENSOR REMARK 3 L11: 0.1434 L22: 0.0262 REMARK 3 L33: 0.0685 L12: -0.0584 REMARK 3 L13: 0.0688 L23: -0.0199 REMARK 3 S TENSOR REMARK 3 S11: -0.0518 S12: 0.0025 S13: 0.1210 REMARK 3 S21: 0.0006 S22: -0.1254 S23: -0.0305 REMARK 3 S31: -0.0175 S32: 0.0149 S33: -0.1650 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 9BP1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000282973. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-AUG-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13619 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.580 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6 REMARK 200 DATA REDUNDANCY : 2.900 REMARK 200 R MERGE (I) : 0.14000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.58 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.66 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.7 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.96900 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 (%): 57.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG8000 .1M TRIS PH8.5, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z REMARK 290 5555 Y,-X+Y,Z+2/3 REMARK 290 6555 X-Y,X,Z+1/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.78333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 15.39167 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 30.78333 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 15.39167 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5030 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, E, H, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 215 REMARK 465 CYS A 216 REMARK 465 ASP A 217 REMARK 465 LYS A 218 REMARK 465 GLY A 219 REMARK 465 LEU A 220 REMARK 465 GLU A 221 REMARK 465 VAL A 222 REMARK 465 GLU B 213 REMARK 465 CYS B 214 REMARK 465 ALA I 676 REMARK 465 SER I 677 REMARK 465 TRP I 678 REMARK 465 ILE I 679 REMARK 465 LYS I 680 REMARK 465 TYR I 681 REMARK 465 ILE I 682 REMARK 465 GLN I 683 REMARK 465 ARG I 684 REMARK 465 ARG I 685 REMARK 465 ARG I 686 REMARK 465 ALA E 676 REMARK 465 SER E 677 REMARK 465 TRP E 678 REMARK 465 ILE E 679 REMARK 465 LYS E 680 REMARK 465 TYR E 681 REMARK 465 ILE E 682 REMARK 465 GLN E 683 REMARK 465 ARG E 684 REMARK 465 ARG E 685 REMARK 465 ARG E 686 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 PRO H 213 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 GLY H 219 REMARK 465 LEU H 220 REMARK 465 GLU H 221 REMARK 465 VAL H 222 REMARK 465 ARG D 211 REMARK 465 GLY D 212 REMARK 465 GLU D 213 REMARK 465 CYS D 214 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O TYR D 186 OH TYR D 192 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OG SER B 67 O SER B 208 2545 2.02 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 SER A 15 -14.31 78.09 REMARK 500 ILE A 48 -71.79 -81.39 REMARK 500 TYR A 100C -109.17 -116.69 REMARK 500 SER A 130 49.03 -102.39 REMARK 500 ASP A 144 77.16 53.63 REMARK 500 ILE B 29 28.91 -143.99 REMARK 500 THR B 30 -136.91 48.44 REMARK 500 THR B 51 -63.28 71.45 REMARK 500 ASP B 70 97.85 -168.11 REMARK 500 ASP B 92 -46.04 -134.07 REMARK 500 PRO B 95 30.45 -93.49 REMARK 500 ASN B 138 93.08 39.19 REMARK 500 PRO B 141 -169.49 -76.02 REMARK 500 LYS E 662 -111.10 47.16 REMARK 500 LEU E 663 99.79 50.89 REMARK 500 SER H 15 -23.55 79.57 REMARK 500 ILE H 48 -60.58 -91.00 REMARK 500 TYR H 100C -116.48 -99.11 REMARK 500 THR H 135 175.70 72.89 REMARK 500 ALA H 136 119.06 -170.12 REMARK 500 ASP H 144 76.22 58.09 REMARK 500 ILE D 29 27.04 -140.68 REMARK 500 THR D 30 -127.46 52.41 REMARK 500 THR D 51 -32.85 59.69 REMARK 500 SER D 52 16.57 -161.39 REMARK 500 SER D 67 146.78 -174.85 REMARK 500 ALA D 84 -178.70 175.92 REMARK 500 ASP D 92 -41.06 -132.87 REMARK 500 VAL D 110 99.93 -63.93 REMARK 500 ASN D 138 93.34 52.63 REMARK 500 SER D 156 125.76 -170.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9BNS RELATED DB: PDB REMARK 900 RELATED ID: 9BLX RELATED DB: PDB DBREF 9BP1 A 1 222 PDB 9BP1 9BP1 1 222 DBREF 9BP1 B 1 214 PDB 9BP1 9BP1 1 214 DBREF1 9BP1 I 660 686 UNP A0A4Y5TJX4_SIV DBREF2 9BP1 I A0A4Y5TJX4 669 695 DBREF1 9BP1 E 660 686 UNP A0A4Y5TJX4_SIV DBREF2 9BP1 E A0A4Y5TJX4 669 695 DBREF 9BP1 H 1 222 PDB 9BP1 9BP1 1 222 DBREF 9BP1 D 1 214 PDB 9BP1 9BP1 1 214 SEQADV 9BP1 ARG I 684 UNP A0A4Y5TJX TYR 693 CONFLICT SEQADV 9BP1 ARG I 686 UNP A0A4Y5TJX VAL 695 CONFLICT SEQADV 9BP1 ARG E 684 UNP A0A4Y5TJX TYR 693 CONFLICT SEQADV 9BP1 ARG E 686 UNP A0A4Y5TJX VAL 695 CONFLICT SEQRES 1 A 232 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 A 232 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 A 232 ASP SER ILE SER SER GLY ASN TRP TRP THR TRP ILE ARG SEQRES 4 A 232 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY ASN ILE SEQRES 5 A 232 GLY GLY ASN SER GLY THR THR PHE TYR ASN PRO SER LEU SEQRES 6 A 232 LYS SER ARG VAL THR ILE SER ARG ASP THR SER LYS ASN SEQRES 7 A 232 GLN PHE SER LEU LYS VAL ASN SER VAL THR VAL ALA ASP SEQRES 8 A 232 THR ALA VAL TYR PHE CYS ALA ARG HIS SER SER GLY TRP SEQRES 9 A 232 PHE SER LEU TYR GLY LEU ASP SER TRP GLY GLN GLY VAL SEQRES 10 A 232 VAL VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 A 232 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 A 232 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 A 232 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 A 232 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 A 232 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 A 232 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 A 232 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 A 232 GLU PRO LYS SER CYS ASP LYS GLY LEU GLU VAL SEQRES 1 B 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 214 GLN ASP ILE THR SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY ARG ALA PRO LYS LEU LEU ILE TYR LYS THR SER SEQRES 5 B 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN ARG HIS SEQRES 8 B 214 ASP THR THR PRO LEU THR PHE GLY GLY GLY THR THR VAL SEQRES 9 B 214 GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 I 27 LEU GLN LYS LEU ASN SER TRP ASP VAL PHE GLY ASN TRP SEQRES 2 I 27 PHE ASP LEU ALA SER TRP ILE LYS TYR ILE GLN ARG ARG SEQRES 3 I 27 ARG SEQRES 1 E 27 LEU GLN LYS LEU ASN SER TRP ASP VAL PHE GLY ASN TRP SEQRES 2 E 27 PHE ASP LEU ALA SER TRP ILE LYS TYR ILE GLN ARG ARG SEQRES 3 E 27 ARG SEQRES 1 H 232 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 232 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 232 ASP SER ILE SER SER GLY ASN TRP TRP THR TRP ILE ARG SEQRES 4 H 232 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY ASN ILE SEQRES 5 H 232 GLY GLY ASN SER GLY THR THR PHE TYR ASN PRO SER LEU SEQRES 6 H 232 LYS SER ARG VAL THR ILE SER ARG ASP THR SER LYS ASN SEQRES 7 H 232 GLN PHE SER LEU LYS VAL ASN SER VAL THR VAL ALA ASP SEQRES 8 H 232 THR ALA VAL TYR PHE CYS ALA ARG HIS SER SER GLY TRP SEQRES 9 H 232 PHE SER LEU TYR GLY LEU ASP SER TRP GLY GLN GLY VAL SEQRES 10 H 232 VAL VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 232 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 232 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 232 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 232 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 232 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 232 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 232 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 H 232 GLU PRO LYS SER CYS ASP LYS GLY LEU GLU VAL SEQRES 1 D 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 D 214 GLN ASP ILE THR SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 D 214 PRO GLY ARG ALA PRO LYS LEU LEU ILE TYR LYS THR SER SEQRES 5 D 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN ARG HIS SEQRES 8 D 214 ASP THR THR PRO LEU THR PHE GLY GLY GLY THR THR VAL SEQRES 9 D 214 GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG GLY GLU CYS HELIX 1 AA1 THR A 83 THR A 87 5 5 HELIX 2 AA2 SER A 187 GLN A 192 1 6 HELIX 3 AA3 LYS A 201 ASN A 204 5 4 HELIX 4 AA4 GLN B 79 PHE B 83 5 5 HELIX 5 AA5 SER B 121 SER B 127 1 7 HELIX 6 AA6 LYS B 183 LYS B 188 1 6 HELIX 7 AA7 ASN I 664 ASN I 671 1 8 HELIX 8 AA8 ASN E 664 TRP E 672 1 9 HELIX 9 AA9 THR H 83 THR H 87 5 5 HELIX 10 AB1 SER H 127 THR H 131 5 5 HELIX 11 AB2 PRO H 185 GLY H 190 5 6 HELIX 12 AB3 LYS H 201 ASN H 204 5 4 HELIX 13 AB4 GLN D 79 PHE D 83 5 5 HELIX 14 AB5 SER D 121 SER D 127 1 7 HELIX 15 AB6 LYS D 183 HIS D 189 1 7 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O THR A 21 N SER A 7 SHEET 3 AA1 4 GLN A 77 VAL A 82 -1 O VAL A 82 N LEU A 18 SHEET 4 AA1 4 VAL A 67 ILE A 69 -1 N THR A 68 O LYS A 81 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 VAL A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA2 6 ALA A 88 SER A 97 -1 N TYR A 90 O VAL A 107 SHEET 4 AA2 6 TRP A 34 GLN A 39 -1 N ILE A 37 O PHE A 91 SHEET 5 AA2 6 GLU A 46 GLY A 52 -1 O GLY A 49 N TRP A 36 SHEET 6 AA2 6 THR A 57 TYR A 59 -1 O PHE A 58 N ASN A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 VAL A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA3 4 ALA A 88 SER A 97 -1 N TYR A 90 O VAL A 107 SHEET 4 AA3 4 LEU A 100B TRP A 103 -1 O SER A 102 N ARG A 94 SHEET 1 AA4 4 SER A 120 LEU A 124 0 SHEET 2 AA4 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA4 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AA5 4 THR A 131 SER A 132 0 SHEET 2 AA5 4 THR A 135 TYR A 145 -1 O THR A 135 N SER A 132 SHEET 3 AA5 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AA5 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AA6 3 THR A 151 TRP A 154 0 SHEET 2 AA6 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AA6 3 THR A 205 ARG A 210 -1 O THR A 205 N HIS A 200 SHEET 1 AA7 4 THR B 5 SER B 7 0 SHEET 2 AA7 4 VAL B 19 ARG B 24 -1 O ARG B 24 N THR B 5 SHEET 3 AA7 4 PHE B 71 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA7 4 PHE B 62 GLY B 66 -1 N SER B 63 O THR B 74 SHEET 1 AA8 6 SER B 10 ALA B 13 0 SHEET 2 AA8 6 THR B 102 LEU B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AA8 6 THR B 85 ARG B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA8 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AA8 6 LYS B 45 TYR B 49 -1 O LYS B 45 N GLN B 37 SHEET 6 AA8 6 THR B 53 LEU B 54 -1 O THR B 53 N TYR B 49 SHEET 1 AA9 4 SER B 114 PHE B 118 0 SHEET 2 AA9 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AA9 4 TYR B 173 SER B 182 -1 O LEU B 179 N VAL B 132 SHEET 4 AA9 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AB1 4 ALA B 153 LEU B 154 0 SHEET 2 AB1 4 ALA B 144 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB1 4 VAL B 191 HIS B 198 -1 O GLU B 195 N GLN B 147 SHEET 4 AB1 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SHEET 1 AB2 4 GLN H 3 SER H 7 0 SHEET 2 AB2 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AB2 4 GLN H 77 VAL H 82 -1 O VAL H 82 N LEU H 18 SHEET 4 AB2 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AB3 6 LEU H 11 VAL H 12 0 SHEET 2 AB3 6 VAL H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB3 6 ALA H 88 SER H 97 -1 N TYR H 90 O VAL H 107 SHEET 4 AB3 6 TRP H 34 GLN H 39 -1 N ILE H 37 O PHE H 91 SHEET 5 AB3 6 GLU H 46 GLY H 52 -1 O GLY H 49 N TRP H 36 SHEET 6 AB3 6 THR H 57 TYR H 59 -1 O PHE H 58 N ASN H 50 SHEET 1 AB4 4 LEU H 11 VAL H 12 0 SHEET 2 AB4 4 VAL H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB4 4 ALA H 88 SER H 97 -1 N TYR H 90 O VAL H 107 SHEET 4 AB4 4 LEU H 100B TRP H 103 -1 O SER H 102 N ARG H 94 SHEET 1 AB5 4 SER H 120 LEU H 124 0 SHEET 2 AB5 4 ALA H 136 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AB5 4 TYR H 176 VAL H 184 -1 O LEU H 178 N VAL H 142 SHEET 4 AB5 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB6 4 SER H 120 LEU H 124 0 SHEET 2 AB6 4 ALA H 136 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AB6 4 TYR H 176 VAL H 184 -1 O LEU H 178 N VAL H 142 SHEET 4 AB6 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB7 3 THR H 151 TRP H 154 0 SHEET 2 AB7 3 CYS H 196 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB7 3 THR H 205 ASP H 208 -1 O VAL H 207 N VAL H 198 SHEET 1 AB8 4 THR D 5 SER D 7 0 SHEET 2 AB8 4 VAL D 19 ARG D 24 -1 O ARG D 24 N THR D 5 SHEET 3 AB8 4 ASP D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 4 AB8 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AB9 6 SER D 10 SER D 12 0 SHEET 2 AB9 6 THR D 102 GLU D 105 1 O GLU D 105 N LEU D 11 SHEET 3 AB9 6 THR D 85 ARG D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AB9 6 LEU D 33 GLN D 38 -1 N ALA D 34 O GLN D 89 SHEET 5 AB9 6 LYS D 45 TYR D 49 -1 O LYS D 45 N GLN D 37 SHEET 6 AB9 6 THR D 53 LEU D 54 -1 O THR D 53 N TYR D 49 SHEET 1 AC1 4 SER D 114 PHE D 118 0 SHEET 2 AC1 4 THR D 129 PHE D 139 -1 O VAL D 133 N PHE D 118 SHEET 3 AC1 4 TYR D 173 SER D 182 -1 O LEU D 181 N ALA D 130 SHEET 4 AC1 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AC2 3 LYS D 145 VAL D 150 0 SHEET 2 AC2 3 TYR D 192 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 3 AC2 3 VAL D 205 PHE D 209 -1 O VAL D 205 N VAL D 196 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.03 SSBOND 2 CYS A 140 CYS A 196 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 6 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.03 SSBOND 8 CYS D 134 CYS D 194 1555 1555 2.03 CISPEP 1 PHE A 146 PRO A 147 0 -4.42 CISPEP 2 GLU A 148 PRO A 149 0 -4.71 CISPEP 3 SER B 7 PRO B 8 0 -2.17 CISPEP 4 THR B 94 PRO B 95 0 -0.52 CISPEP 5 TYR B 140 PRO B 141 0 5.49 CISPEP 6 PHE H 146 PRO H 147 0 -7.94 CISPEP 7 GLU H 148 PRO H 149 0 -2.30 CISPEP 8 SER D 7 PRO D 8 0 -1.55 CISPEP 9 THR D 94 PRO D 95 0 -0.80 CISPEP 10 TYR D 140 PRO D 141 0 1.03 CRYST1 210.174 210.174 46.175 90.00 90.00 120.00 P 62 12 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 0.004758 0.002747 0.000000 0.00000 SCALE2 0.000000 0.005494 0.000000 0.00000 SCALE3 0.000000 0.000000 0.021657 0.00000