HEADER IMMUNE SYSTEM 21-APR-25 9OAR TITLE CRYSTAL STRUCTURE OF ANTIBODY FAB G001-179 FROM IAVI G001 HUMAN TRIAL TITLE 2 IN COMPLEX WITH A GERMLINE-TARGETING GP120 ENGINEERED OUTER DOMAIN TITLE 3 EOD-GT8-MINGLY COMPND MOL_ID: 1; COMPND 2 MOLECULE: GERMLINE-TARGETING HIV-1 GP120 ENGINEERED OUTER DOMAIN EOD- COMPND 3 GT8-MINGLY; COMPND 4 CHAIN: C, A; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: G001-179 FAB HEAVY CHAIN; COMPND 8 CHAIN: H, B; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: G001-179 FAB LIGHT CHAIN; COMPND 12 CHAIN: L, D; 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 9OAR 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. 1.94 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) : 1.94 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.28 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 86.2 REMARK 3 NUMBER OF REFLECTIONS : 96730 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.258 REMARK 3 R VALUE (WORKING SET) : 0.213 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250 REMARK 3 FREE R VALUE TEST SET COUNT : 5082 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 26.2800 - 5.2600 0.85 4813 209 0.1978 0.2120 REMARK 3 2 5.2600 - 4.1800 0.90 5015 265 0.1730 0.2395 REMARK 3 3 4.1800 - 3.6500 0.88 4902 272 0.1885 0.2396 REMARK 3 4 3.6500 - 3.3200 0.78 4380 191 0.2072 0.2207 REMARK 3 5 3.3200 - 3.0800 0.85 4763 236 0.2274 0.2790 REMARK 3 6 3.0800 - 2.9000 0.87 4863 279 0.2471 0.3221 REMARK 3 7 2.9000 - 2.7600 0.88 4945 258 0.2802 0.3480 REMARK 3 8 2.7600 - 2.6400 0.89 4999 272 0.2945 0.3238 REMARK 3 9 2.6400 - 2.5400 0.89 4995 228 0.3112 0.3716 REMARK 3 10 2.5400 - 2.4500 0.75 4192 255 0.3124 0.3900 REMARK 3 11 2.4500 - 2.3700 0.83 4652 231 0.3194 0.3633 REMARK 3 12 2.3700 - 2.3000 0.85 4738 274 0.3233 0.3613 REMARK 3 13 2.3000 - 2.2400 0.86 4844 252 0.3189 0.3207 REMARK 3 14 2.2400 - 2.1900 0.87 4908 243 0.3261 0.3306 REMARK 3 15 2.1900 - 2.1400 0.87 4825 236 0.3242 0.3266 REMARK 3 16 2.1400 - 2.0900 0.89 5065 189 0.3375 0.4044 REMARK 3 17 2.0900 - 2.0500 0.87 4800 258 0.3354 0.3627 REMARK 3 18 2.0500 - 2.0100 0.87 4937 202 0.3430 0.3185 REMARK 3 19 2.0100 - 1.9800 0.77 4261 187 0.3367 0.3363 REMARK 3 20 1.9800 - 1.9400 0.22 1243 53 0.3478 0.4052 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) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.356 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.21 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: 0.4800 REMARK 3 OPERATOR: -H,K,-L REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 9292 REMARK 3 ANGLE : 0.919 12636 REMARK 3 CHIRALITY : 0.058 1420 REMARK 3 PLANARITY : 0.008 1620 REMARK 3 DIHEDRAL : 14.269 3370 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "A" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "C" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "B" 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 GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "D" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "L" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9OAR 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_1000295197. 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 : 96860 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940 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 (%) : 89.6 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00 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 (%): 58.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3350 AND 0.2 M AMMONIUM REMARK 280 SULFATE AT PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 HIS 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 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP L 1 REMARK 465 ILE L 2 REMARK 465 GLN L 3 REMARK 465 CYS L 214 REMARK 465 GLU A -2 REMARK 465 THR A -1 REMARK 465 GLY A 0 REMARK 465 ALA A 170 REMARK 465 SER A 171 REMARK 465 THR A 172 REMARK 465 GLY A 173 REMARK 465 THR A 174 REMARK 465 HIS A 175 REMARK 465 HIS A 176 REMARK 465 HIS A 177 REMARK 465 HIS A 178 REMARK 465 HIS A 179 REMARK 465 HIS A 180 REMARK 465 SER B 127 REMARK 465 SER B 128 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 SER B 132 REMARK 465 GLY B 133 REMARK 465 SER B 215 REMARK 465 CYS B 216 REMARK 465 ASP D 1 REMARK 465 ILE D 2 REMARK 465 GLN D 3 REMARK 465 CYS D 214 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 C 32 28.27 46.12 REMARK 500 ASN C 34 46.29 -90.17 REMARK 500 ASP C 44 -154.81 -142.98 REMARK 500 GLN C 61 -58.98 66.98 REMARK 500 GLU C 71 -57.31 -125.32 REMARK 500 ALA C 165 67.77 -158.72 REMARK 500 ASN H 99 -40.87 74.20 REMARK 500 ASP H 144 67.50 60.74 REMARK 500 PRO H 147 -153.65 -83.87 REMARK 500 SER L 30 -118.34 60.38 REMARK 500 ALA L 51 -44.76 72.77 REMARK 500 TYR L 91 -130.54 53.94 REMARK 500 ASN L 138 73.27 61.98 REMARK 500 LYS L 169 -68.19 -95.45 REMARK 500 LYS L 190 -61.08 -107.87 REMARK 500 ASN A 34 44.10 -89.44 REMARK 500 ASP A 44 -158.74 -140.06 REMARK 500 GLN A 61 -59.83 66.21 REMARK 500 GLU A 71 -56.25 -125.10 REMARK 500 ALA A 165 68.59 -161.54 REMARK 500 CYS B 98 -86.95 -73.04 REMARK 500 ASN B 99 -31.98 141.36 REMARK 500 PRO B 147 -157.81 -86.12 REMARK 500 SER D 30 -117.14 63.88 REMARK 500 ALA D 51 -42.97 73.67 REMARK 500 TYR D 91 -128.28 52.56 REMARK 500 ASN D 138 70.21 58.39 REMARK 500 LYS D 169 -67.96 -95.94 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 C 515 DISTANCE = 5.91 ANGSTROMS REMARK 525 HOH C 516 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH C 517 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH C 518 DISTANCE = 5.94 ANGSTROMS REMARK 525 HOH C 519 DISTANCE = 5.97 ANGSTROMS REMARK 525 HOH C 520 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH C 521 DISTANCE = 6.46 ANGSTROMS REMARK 525 HOH C 522 DISTANCE = 6.67 ANGSTROMS REMARK 525 HOH C 523 DISTANCE = 6.81 ANGSTROMS REMARK 525 HOH C 524 DISTANCE = 6.85 ANGSTROMS REMARK 525 HOH C 525 DISTANCE = 7.81 ANGSTROMS REMARK 525 HOH C 526 DISTANCE = 8.23 ANGSTROMS REMARK 525 HOH C 527 DISTANCE = 8.83 ANGSTROMS REMARK 525 HOH H 583 DISTANCE = 5.88 ANGSTROMS REMARK 525 HOH H 584 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH H 585 DISTANCE = 5.94 ANGSTROMS REMARK 525 HOH H 586 DISTANCE = 6.11 ANGSTROMS REMARK 525 HOH H 587 DISTANCE = 6.52 ANGSTROMS REMARK 525 HOH H 588 DISTANCE = 7.21 ANGSTROMS REMARK 525 HOH H 589 DISTANCE = 7.22 ANGSTROMS REMARK 525 HOH H 590 DISTANCE = 7.36 ANGSTROMS REMARK 525 HOH H 591 DISTANCE = 7.64 ANGSTROMS REMARK 525 HOH L 581 DISTANCE = 5.96 ANGSTROMS REMARK 525 HOH L 582 DISTANCE = 6.06 ANGSTROMS REMARK 525 HOH L 583 DISTANCE = 6.08 ANGSTROMS REMARK 525 HOH L 584 DISTANCE = 6.65 ANGSTROMS REMARK 525 HOH L 585 DISTANCE = 6.69 ANGSTROMS REMARK 525 HOH L 586 DISTANCE = 8.43 ANGSTROMS REMARK 525 HOH L 587 DISTANCE = 8.51 ANGSTROMS REMARK 525 HOH L 588 DISTANCE = 9.19 ANGSTROMS REMARK 525 HOH A 512 DISTANCE = 6.17 ANGSTROMS REMARK 525 HOH A 513 DISTANCE = 6.56 ANGSTROMS REMARK 525 HOH A 514 DISTANCE = 8.02 ANGSTROMS REMARK 525 HOH A 515 DISTANCE = 8.73 ANGSTROMS REMARK 525 HOH A 516 DISTANCE = 8.90 ANGSTROMS REMARK 525 HOH B 613 DISTANCE = 5.87 ANGSTROMS REMARK 525 HOH B 614 DISTANCE = 5.89 ANGSTROMS REMARK 525 HOH B 615 DISTANCE = 6.01 ANGSTROMS REMARK 525 HOH B 616 DISTANCE = 6.08 ANGSTROMS REMARK 525 HOH B 617 DISTANCE = 6.16 ANGSTROMS REMARK 525 HOH B 618 DISTANCE = 6.33 ANGSTROMS REMARK 525 HOH B 619 DISTANCE = 6.55 ANGSTROMS REMARK 525 HOH B 620 DISTANCE = 6.62 ANGSTROMS REMARK 525 HOH B 621 DISTANCE = 6.78 ANGSTROMS REMARK 525 HOH B 622 DISTANCE = 6.84 ANGSTROMS REMARK 525 HOH B 623 DISTANCE = 7.03 ANGSTROMS REMARK 525 HOH B 624 DISTANCE = 10.10 ANGSTROMS REMARK 525 HOH D 593 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH D 594 DISTANCE = 6.18 ANGSTROMS REMARK 525 HOH D 595 DISTANCE = 6.77 ANGSTROMS REMARK 525 HOH D 596 DISTANCE = 7.14 ANGSTROMS DBREF 9OAR C -2 180 PDB 9OAR 9OAR -2 180 DBREF 9OAR H 1 216 PDB 9OAR 9OAR 1 216 DBREF 9OAR L 1 214 PDB 9OAR 9OAR 1 214 DBREF 9OAR A -2 180 PDB 9OAR 9OAR -2 180 DBREF 9OAR B 1 216 PDB 9OAR 9OAR 1 216 DBREF 9OAR D 1 214 PDB 9OAR 9OAR 1 214 SEQRES 1 C 183 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 C 183 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 C 183 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 C 183 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 C 183 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 C 183 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 C 183 ARG SER GLU ASP TRP ARG ASP ASN ALA LYS SER ILE CYS SEQRES 8 C 183 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 C 183 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 C 183 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 C 183 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 C 183 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 C 183 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 C 183 THR TRP PHE ALA SER THR GLY THR HIS HIS HIS HIS HIS SEQRES 15 C 183 HIS SEQRES 1 H 227 GLN VAL GLN LEU VAL GLN SER GLY ALA ASP VAL LYS LYS SEQRES 2 H 227 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 227 TYR THR PHE THR ASP TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 227 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 227 ASP ARG VAL THR MET THR ARG ASP THR SER VAL SER THR SEQRES 7 H 227 ALA TYR MET GLU VAL SER GLY LEU ARG SER ASP ASP THR SEQRES 8 H 227 ALA VAL TYR TYR CYS ALA ARG ILE LYS LEU CYS ASN GLY SEQRES 9 H 227 GLY SER CYS ASN TRP SER LEU GLY TYR TRP GLY GLN GLY SEQRES 10 H 227 SER LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 227 VAL GLU PRO 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 SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 210 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY 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 PRO GLY THR LYS VAL ASP 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 A 183 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 A 183 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 A 183 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 A 183 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 A 183 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 A 183 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 A 183 ARG SER GLU ASP TRP ARG ASP ASN ALA LYS SER ILE CYS SEQRES 8 A 183 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 A 183 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 A 183 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 A 183 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 A 183 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 A 183 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 A 183 THR TRP PHE ALA SER THR GLY THR HIS HIS HIS HIS HIS SEQRES 15 A 183 HIS SEQRES 1 B 227 GLN VAL GLN LEU VAL GLN SER GLY ALA ASP VAL LYS LYS SEQRES 2 B 227 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 B 227 TYR THR PHE THR ASP TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 B 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 B 227 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 B 227 ASP ARG VAL THR MET THR ARG ASP THR SER VAL SER THR SEQRES 7 B 227 ALA TYR MET GLU VAL SER GLY LEU ARG SER ASP ASP THR SEQRES 8 B 227 ALA VAL TYR TYR CYS ALA ARG ILE LYS LEU CYS ASN GLY SEQRES 9 B 227 GLY SER CYS ASN TRP SER LEU GLY TYR TRP GLY GLN GLY SEQRES 10 B 227 SER LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 B 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 B 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 B 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 B 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 B 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 B 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 B 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 B 227 VAL GLU PRO LYS SER CYS SEQRES 1 D 210 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 210 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 D 210 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 D 210 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 D 210 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 210 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU SEQRES 7 D 210 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 D 210 GLU PHE PHE GLY PRO GLY THR LYS VAL ASP ILE LYS ARG SEQRES 9 D 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 D 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 D 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 D 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 D 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 D 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 D 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 D 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 D 210 GLU CYS HET NAG C 201 14 HET NAG C 202 14 HET NAG A 201 14 HET NAG A 202 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 7 NAG 4(C8 H15 N O6) FORMUL 11 HOH *1642(H2 O) HELIX 1 AA1 PRO C 12 SER C 16 5 5 HELIX 2 AA2 ASP C 44 ARG C 50 1 7 HELIX 3 AA3 ARG C 109 GLY C 128 1 20 HELIX 4 AA4 ASP C 141 ASN C 146 1 6 HELIX 5 AA5 THR H 28 TYR H 32 5 5 HELIX 6 AA6 GLN H 61 GLN H 64 5 4 HELIX 7 AA7 THR H 73 VAL H 75 5 3 HELIX 8 AA8 ARG H 83 THR H 87 5 5 HELIX 9 AA9 SER H 156 ALA H 158 5 3 HELIX 10 AB1 SER H 187 LEU H 189 5 3 HELIX 11 AB2 LYS H 201 ASN H 204 5 4 HELIX 12 AB3 GLN L 79 ILE L 83 5 5 HELIX 13 AB4 SER L 121 LYS L 126 1 6 HELIX 14 AB5 LYS L 183 GLU L 187 1 5 HELIX 15 AB6 PRO A 12 SER A 16 5 5 HELIX 16 AB7 ASP A 44 ARG A 50 1 7 HELIX 17 AB8 ARG A 109 GLY A 128 1 20 HELIX 18 AB9 ASP A 141 ASN A 146 1 6 HELIX 19 AC1 THR B 28 TYR B 32 5 5 HELIX 20 AC2 GLN B 61 GLN B 64 5 4 HELIX 21 AC3 THR B 73 VAL B 75 5 3 HELIX 22 AC4 ARG B 83 THR B 87 5 5 HELIX 23 AC5 SER B 156 ALA B 158 5 3 HELIX 24 AC6 SER B 187 LEU B 189 5 3 HELIX 25 AC7 LYS B 201 ASN B 204 5 4 HELIX 26 AC8 SER D 121 LYS D 126 1 6 HELIX 27 AC9 LYS D 183 LYS D 188 1 6 SHEET 1 AA1 7 LEU C 62 LEU C 64 0 SHEET 2 AA1 7 SER C 17 ARG C 26 -1 N GLY C 21 O PHE C 63 SHEET 3 AA1 7 ILE C 87 CYS C 99 -1 O VAL C 89 N LEU C 22 SHEET 4 AA1 7 HIS C 104 SER C 108 -1 O ALA C 106 N ALA C 98 SHEET 5 AA1 7 THR C 2 ARG C 8 -1 N ILE C 3 O ILE C 107 SHEET 6 AA1 7 GLU C 154 CYS C 158 -1 O TYR C 157 N ARG C 8 SHEET 7 AA1 7 HIS C 147 CYS C 151 -1 N CYS C 151 O GLU C 154 SHEET 1 AA2 6 VAL C 74 ARG C 76 0 SHEET 2 AA2 6 ILE C 87 CYS C 99 -1 O GLN C 90 N VAL C 74 SHEET 3 AA2 6 SER C 17 ARG C 26 -1 N LEU C 22 O VAL C 89 SHEET 4 AA2 6 THR C 35 PRO C 40 -1 O ARG C 39 N THR C 25 SHEET 5 AA2 6 THR C 131 PHE C 134 1 O THR C 131 N VAL C 36 SHEET 6 AA2 6 SER C 166 TRP C 168 -1 O TRP C 168 N ILE C 132 SHEET 1 AA3 4 GLN H 3 GLN H 6 0 SHEET 2 AA3 4 SER H 17 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA3 4 THR H 77 SER H 82A-1 O ALA H 78 N CYS H 22 SHEET 4 AA3 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA4 6 ASP H 10 LYS H 12 0 SHEET 2 AA4 6 SER H 107 VAL H 111 1 O THR H 110 N ASP H 10 SHEET 3 AA4 6 ALA H 88 ILE H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA4 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA4 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA4 6 THR H 57 TYR H 59 -1 O ASN H 58 N TRP H 50 SHEET 1 AA5 4 ASP H 10 LYS H 12 0 SHEET 2 AA5 4 SER H 107 VAL H 111 1 O THR H 110 N ASP H 10 SHEET 3 AA5 4 ALA H 88 ILE H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA5 4 LEU H 100G TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA6 4 SER H 120 LEU H 124 0 SHEET 2 AA6 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA6 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA6 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA7 4 SER H 120 LEU H 124 0 SHEET 2 AA7 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA7 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA7 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA8 3 THR H 151 TRP H 154 0 SHEET 2 AA8 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA8 3 THR H 205 LYS H 210 -1 O LYS H 209 N CYS H 196 SHEET 1 AA9 4 THR L 5 SER L 7 0 SHEET 2 AA9 4 VAL L 19 GLN L 24 -1 O THR L 22 N SER L 7 SHEET 3 AA9 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AA9 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AB1 6 SER L 10 ALA L 13 0 SHEET 2 AB1 6 THR L 98 ILE L 102 1 O ASP L 101 N LEU L 11 SHEET 3 AB1 6 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 98 SHEET 4 AB1 6 ASN L 34 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AB1 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AB1 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AB2 4 SER L 10 ALA L 13 0 SHEET 2 AB2 4 THR L 98 ILE L 102 1 O ASP L 101 N LEU L 11 SHEET 3 AB2 4 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 98 SHEET 4 AB2 4 PHE L 93 PHE L 94 -1 O PHE L 93 N GLN L 90 SHEET 1 AB3 4 SER L 114 PHE L 118 0 SHEET 2 AB3 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB3 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AB3 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB4 4 ALA L 153 GLN L 155 0 SHEET 2 AB4 4 ALA L 144 VAL L 150 -1 N TRP L 148 O GLN L 155 SHEET 3 AB4 4 VAL L 191 HIS L 198 -1 O ALA L 193 N LYS L 149 SHEET 4 AB4 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB5 7 LEU A 62 LEU A 64 0 SHEET 2 AB5 7 SER A 17 ARG A 26 -1 N GLY A 21 O PHE A 63 SHEET 3 AB5 7 ILE A 87 CYS A 99 -1 O VAL A 95 N ILE A 19 SHEET 4 AB5 7 HIS A 104 SER A 108 -1 O ALA A 106 N ALA A 98 SHEET 5 AB5 7 THR A 2 ARG A 8 -1 N ILE A 3 O ILE A 107 SHEET 6 AB5 7 GLU A 154 CYS A 158 -1 O TYR A 157 N ARG A 8 SHEET 7 AB5 7 HIS A 147 CYS A 151 -1 N PHE A 149 O PHE A 156 SHEET 1 AB6 6 VAL A 74 SER A 77 0 SHEET 2 AB6 6 ILE A 87 CYS A 99 -1 O GLN A 90 N VAL A 74 SHEET 3 AB6 6 SER A 17 ARG A 26 -1 N ILE A 19 O VAL A 95 SHEET 4 AB6 6 THR A 35 PRO A 40 -1 O ARG A 39 N THR A 25 SHEET 5 AB6 6 THR A 131 PHE A 134 1 O THR A 131 N VAL A 36 SHEET 6 AB6 6 SER A 166 TRP A 168 -1 O SER A 166 N PHE A 134 SHEET 1 AB7 4 GLN B 3 GLN B 6 0 SHEET 2 AB7 4 SER B 17 SER B 25 -1 O LYS B 23 N VAL B 5 SHEET 3 AB7 4 THR B 77 SER B 82A-1 O VAL B 82 N VAL B 18 SHEET 4 AB7 4 VAL B 67 ASP B 72 -1 N THR B 68 O GLU B 81 SHEET 1 AB8 6 ASP B 10 LYS B 12 0 SHEET 2 AB8 6 SER B 107 VAL B 111 1 O THR B 110 N LYS B 12 SHEET 3 AB8 6 ALA B 88 ARG B 94 -1 N ALA B 88 O VAL B 109 SHEET 4 AB8 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 91 SHEET 5 AB8 6 GLU B 46 ILE B 51 -1 O MET B 48 N TRP B 36 SHEET 6 AB8 6 THR B 57 TYR B 59 -1 O ASN B 58 N TRP B 50 SHEET 1 AB9 4 ASP B 10 LYS B 12 0 SHEET 2 AB9 4 SER B 107 VAL B 111 1 O THR B 110 N LYS B 12 SHEET 3 AB9 4 ALA B 88 ARG B 94 -1 N ALA B 88 O VAL B 109 SHEET 4 AB9 4 TYR B 102 TRP B 103 -1 O TYR B 102 N ARG B 94 SHEET 1 AC1 4 SER B 120 LEU B 124 0 SHEET 2 AC1 4 THR B 135 TYR B 145 -1 O GLY B 139 N LEU B 124 SHEET 3 AC1 4 TYR B 176 PRO B 185 -1 O VAL B 184 N ALA B 136 SHEET 4 AC1 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AC2 4 SER B 120 LEU B 124 0 SHEET 2 AC2 4 THR B 135 TYR B 145 -1 O GLY B 139 N LEU B 124 SHEET 3 AC2 4 TYR B 176 PRO B 185 -1 O VAL B 184 N ALA B 136 SHEET 4 AC2 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AC3 3 THR B 151 TRP B 154 0 SHEET 2 AC3 3 TYR B 194 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AC3 3 THR B 205 VAL B 211 -1 O THR B 205 N HIS B 200 SHEET 1 AC4 4 THR D 5 SER D 7 0 SHEET 2 AC4 4 VAL D 19 GLN D 24 -1 O THR D 22 N SER D 7 SHEET 3 AC4 4 ASP D 70 ILE D 75 -1 O PHE D 73 N ILE D 21 SHEET 4 AC4 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AC5 6 SER D 10 SER D 14 0 SHEET 2 AC5 6 THR D 98 LYS D 103 1 O LYS D 99 N LEU D 11 SHEET 3 AC5 6 ALA D 84 GLN D 90 -1 N ALA D 84 O VAL D 100 SHEET 4 AC5 6 ASN D 34 GLN D 38 -1 N GLN D 38 O THR D 85 SHEET 5 AC5 6 LYS D 45 TYR D 49 -1 O LYS D 45 N GLN D 37 SHEET 6 AC5 6 ASN D 53 LEU D 54 -1 O ASN D 53 N TYR D 49 SHEET 1 AC6 4 SER D 10 SER D 14 0 SHEET 2 AC6 4 THR D 98 LYS D 103 1 O LYS D 99 N LEU D 11 SHEET 3 AC6 4 ALA D 84 GLN D 90 -1 N ALA D 84 O VAL D 100 SHEET 4 AC6 4 PHE D 93 PHE D 94 -1 O PHE D 93 N GLN D 90 SHEET 1 AC7 4 SER D 114 PHE D 118 0 SHEET 2 AC7 4 THR D 129 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AC7 4 TYR D 173 SER D 182 -1 O LEU D 181 N ALA D 130 SHEET 4 AC7 4 SER D 159 VAL D 163 -1 N SER D 162 O SER D 176 SHEET 1 AC8 4 ALA D 153 GLN D 155 0 SHEET 2 AC8 4 LYS D 145 VAL D 150 -1 N TRP D 148 O GLN D 155 SHEET 3 AC8 4 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 4 AC8 4 VAL D 205 ASN D 210 -1 O PHE D 209 N TYR D 192 SSBOND 1 CYS C 7 CYS C 158 1555 1555 2.05 SSBOND 2 CYS C 15 CYS C 151 1555 1555 2.04 SSBOND 3 CYS C 51 CYS C 88 1555 1555 2.04 SSBOND 4 CYS C 99 CYS C 105 1555 1555 2.02 SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 6 CYS H 98 CYS H 100C 1555 1555 2.02 SSBOND 7 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 8 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 9 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 10 CYS A 7 CYS A 158 1555 1555 2.04 SSBOND 11 CYS A 15 CYS A 151 1555 1555 2.05 SSBOND 12 CYS A 51 CYS A 88 1555 1555 2.04 SSBOND 13 CYS A 99 CYS A 105 1555 1555 2.04 SSBOND 14 CYS B 22 CYS B 92 1555 1555 2.04 SSBOND 15 CYS B 98 CYS B 100C 1555 1555 2.02 SSBOND 16 CYS B 140 CYS B 196 1555 1555 2.03 SSBOND 17 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 18 CYS D 134 CYS D 194 1555 1555 2.04 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 A 18 C1 NAG A 201 1555 1555 1.44 LINK ND2 ASN A 65 C1 NAG A 202 1555 1555 1.44 CISPEP 1 ARG C 8 PRO C 9 0 -3.30 CISPEP 2 PHE H 146 PRO H 147 0 -2.87 CISPEP 3 GLU H 148 PRO H 149 0 0.02 CISPEP 4 SER L 7 PRO L 8 0 -1.13 CISPEP 5 TYR L 140 PRO L 141 0 1.81 CISPEP 6 ARG A 8 PRO A 9 0 -4.56 CISPEP 7 PHE B 146 PRO B 147 0 -4.44 CISPEP 8 GLU B 148 PRO B 149 0 1.63 CISPEP 9 SER D 7 PRO D 8 0 -0.97 CISPEP 10 TYR D 140 PRO D 141 0 3.41 CRYST1 49.216 65.929 122.098 89.90 96.93 90.03 P 1 2 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 0.020319 0.000011 0.002470 0.00000 SCALE2 0.000000 0.015168 -0.000025 0.00000 SCALE3 0.000000 0.000000 0.008250 0.00000 MTRIX1 1 -0.999998 -0.001905 0.000205 49.18412 1 MTRIX2 1 -0.001906 0.999997 -0.001177 32.98726 1 MTRIX3 1 -0.000203 -0.001177 -0.999999 0.09404 1 MTRIX1 2 -0.999993 -0.003324 -0.001755 49.28849 1 MTRIX2 2 -0.003322 0.999994 -0.000880 32.94434 1 MTRIX3 2 0.001758 -0.000874 -0.999998 0.04965 1 MTRIX1 3 -0.999996 -0.002648 -0.000426 49.20446 1 MTRIX2 3 -0.002647 0.999996 -0.001096 32.95159 1 MTRIX3 3 0.000429 -0.001095 -0.999999 0.11458 1