HEADER VIRAL PROTEIN/IMMUNE SYSTEM 13-MAY-25 9OMG TITLE CRYO-EM STRUCTURE OF RHESUS ANTIBODY V033-A.I1 IN COMPLEX WITH HIV ENV TITLE 2 TRIMER Q23.17 MD39 CAVEAT 9OMG COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV ENV GP120; COMPND 3 CHAIN: A, C, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HIV ENV GP41 ECTODOMAIN; COMPND 7 CHAIN: B, F, G; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: V033-INT1 HEAVY CHAIN; COMPND 11 CHAIN: H; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: V033-INT1 LIGHT CHAIN; COMPND 15 CHAIN: L; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 13 ORGANISM_TAXID: 9544; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 18 ORGANISM_TAXID: 9544; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NEUTRALIZING ANTIBODY, HIV-1 V2 APEX, SHIV-ELICITED, VIRAL PROTEIN, KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.S.ROARK,L.SHAPIRO,P.D.KWONG REVDAT 1 05-NOV-25 9OMG 0 JRNL AUTH R.HABIB,R.S.ROARK,P.D.KWONG,G.M.SHAW JRNL TITL ENV-ANTIBODY COEVOLUTION IDENTIFIES B CELL PRIMING AS THE JRNL TITL 2 PRINCIPAL BOTTLENECK TO HIV-1 V2 APEX BROADLY NEUTRALIZING JRNL TITL 3 ANTIBODY DEVELOPMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.600 REMARK 3 NUMBER OF PARTICLES : 155379 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9OMG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-25. REMARK 100 THE DEPOSITION ID IS D_1000295834. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : V033-INT1 FAB IN COMPLEX WITH REMARK 245 Q23.17 MD39 ENVELOPE TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5800.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, G, H, L, D, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, j, k, l, REMARK 350 AND CHAINS: m, n, o, p, q, r, s, t, u, v, REMARK 350 AND CHAINS: w, x, y 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 VAL A 31 REMARK 465 GLU A 32 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 THR A 147 REMARK 465 THR A 148 REMARK 465 GLY A 149 REMARK 465 GLN A 187A REMARK 465 GLY A 187B REMARK 465 THR A 400 REMARK 465 TRP A 401 REMARK 465 ASN A 402 REMARK 465 ASP A 403 REMARK 465 THR A 404 REMARK 465 ASP A 405 REMARK 465 SER A 406 REMARK 465 THR A 407 REMARK 465 GLN A 408 REMARK 465 GLU A 409 REMARK 465 VAL A 506 REMARK 465 GLU A 507 REMARK 465 ARG A 508 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 VAL B 518 REMARK 465 SER B 519 REMARK 465 SER B 546 REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 ASN B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 PRO B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 ASP B 568 REMARK 465 GLU B 662 REMARK 465 LEU B 663 REMARK 465 ASP B 664 REMARK 465 VAL C 31 REMARK 465 GLU C 32 REMARK 465 LYS C 59 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 GLU C 62 REMARK 465 THR C 63 REMARK 465 GLU C 64 REMARK 465 THR C 147 REMARK 465 THR C 148 REMARK 465 GLY C 149 REMARK 465 GLN C 187A REMARK 465 GLY C 187B REMARK 465 THR C 400 REMARK 465 TRP C 401 REMARK 465 ASN C 402 REMARK 465 ASP C 403 REMARK 465 THR C 404 REMARK 465 ASP C 405 REMARK 465 SER C 406 REMARK 465 THR C 407 REMARK 465 GLN C 408 REMARK 465 GLU C 409 REMARK 465 VAL C 506 REMARK 465 GLU C 507 REMARK 465 ARG C 508 REMARK 465 VAL E 31 REMARK 465 GLU E 32 REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 THR E 147 REMARK 465 THR E 148 REMARK 465 GLY E 149 REMARK 465 GLN E 187A REMARK 465 GLY E 187B REMARK 465 THR E 400 REMARK 465 TRP E 401 REMARK 465 ASN E 402 REMARK 465 ASP E 403 REMARK 465 THR E 404 REMARK 465 ASP E 405 REMARK 465 SER E 406 REMARK 465 THR E 407 REMARK 465 GLN E 408 REMARK 465 GLU E 409 REMARK 465 VAL E 506 REMARK 465 GLU E 507 REMARK 465 ARG E 508 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 SER F 519 REMARK 465 SER F 546 REMARK 465 GLY F 547 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 ASN F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 PRO F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 ASP F 568 REMARK 465 GLU F 662 REMARK 465 LEU F 663 REMARK 465 ASP F 664 REMARK 465 ALA G 512 REMARK 465 VAL G 513 REMARK 465 GLY G 514 REMARK 465 ILE G 515 REMARK 465 GLY G 516 REMARK 465 ALA G 517 REMARK 465 VAL G 518 REMARK 465 SER G 519 REMARK 465 SER G 546 REMARK 465 GLY G 547 REMARK 465 ILE G 548 REMARK 465 VAL G 549 REMARK 465 GLN G 550 REMARK 465 GLN G 551 REMARK 465 GLN G 552 REMARK 465 ASN G 553 REMARK 465 ASN G 554 REMARK 465 LEU G 555 REMARK 465 LEU G 556 REMARK 465 ARG G 557 REMARK 465 ALA G 558 REMARK 465 PRO G 559 REMARK 465 GLU G 560 REMARK 465 PRO G 561 REMARK 465 GLN G 562 REMARK 465 GLN G 563 REMARK 465 HIS G 564 REMARK 465 LEU G 565 REMARK 465 LEU G 566 REMARK 465 LYS G 567 REMARK 465 ASP G 568 REMARK 465 GLU G 662 REMARK 465 LEU G 663 REMARK 465 ASP G 664 REMARK 465 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 ARG H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLU H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 SER H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 VAL H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 ARG H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 ILE H 213 REMARK 465 LYS H 214 REMARK 465 THR H 215 REMARK 465 CYS H 216 REMARK 465 GLY H 217 REMARK 465 GLY H 218 REMARK 465 GLY H 219 REMARK 465 LEU H 220 REMARK 465 GLU H 221 REMARK 465 VAL H 222 REMARK 465 LEU H 223 REMARK 465 PHE H 224 REMARK 465 GLN H 225 REMARK 465 ILE L 106 REMARK 465 LYS L 107 REMARK 465 ARG L 108 REMARK 465 THR L 109 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 GLU L 122 REMARK 465 ASP L 123 REMARK 465 GLN L 124 REMARK 465 VAL L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 VAL L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 SER L 145 REMARK 465 VAL L 146 REMARK 465 LYS L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 GLY L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 LYS L 155 REMARK 465 THR L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 ASN L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 SER L 183 REMARK 465 THR L 184 REMARK 465 GLU L 185 REMARK 465 TYR L 186 REMARK 465 GLN L 187 REMARK 465 SER L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP F 632 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA A 55 45.27 -142.57 REMARK 500 THR A 135 -1.18 69.38 REMARK 500 ASN A 195 -13.24 69.44 REMARK 500 GLN A 258 -9.71 67.40 REMARK 500 SER A 364 -171.98 56.68 REMARK 500 ASP A 461 -0.22 67.27 REMARK 500 SER A 473 16.00 57.57 REMARK 500 THR B 536 32.46 -91.65 REMARK 500 ASP C 167 33.23 -96.42 REMARK 500 PHE C 210 34.44 -99.79 REMARK 500 GLN C 258 13.93 50.84 REMARK 500 LYS C 268 -40.94 -135.67 REMARK 500 ASN C 355 46.48 -80.36 REMARK 500 PHE C 361 153.11 64.87 REMARK 500 ASN C 411 49.60 -92.28 REMARK 500 LEU C 483 30.28 -98.55 REMARK 500 ASN E 88 15.93 59.39 REMARK 500 GLN E 258 -10.47 69.56 REMARK 500 SER E 364 -171.82 58.93 REMARK 500 ASN E 377 -32.97 -131.96 REMARK 500 ASN E 463 -156.09 51.41 REMARK 500 SER E 473 -5.99 66.77 REMARK 500 ALA F 525 33.00 -98.49 REMARK 500 SER F 528 -169.54 -79.61 REMARK 500 TYR H 100D -61.43 -93.59 REMARK 500 LEU H 100J -3.82 67.81 REMARK 500 SER L 30 -96.00 56.77 REMARK 500 SER L 31 23.57 -140.35 REMARK 500 ALA L 84 -169.05 -127.52 REMARK 500 PHE L 96 46.65 39.37 REMARK 500 PHE L 98 -168.21 -104.37 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG I 1 REMARK 610 NAG n 1 REMARK 610 NAG y 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-70613 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF RHESUS ANTIBODY V033-INT1 IN COMPLEX WITH HIV REMARK 900 ENV TRIMER Q23.17 MD39 DBREF 9OMG A 31 508 PDB 9OMG 9OMG 31 508 DBREF 9OMG B 512 664 PDB 9OMG 9OMG 512 664 DBREF 9OMG C 31 508 PDB 9OMG 9OMG 31 508 DBREF 9OMG E 31 508 PDB 9OMG 9OMG 31 508 DBREF 9OMG F 512 664 PDB 9OMG 9OMG 512 664 DBREF 9OMG G 512 664 PDB 9OMG 9OMG 512 664 DBREF 9OMG H 1 225 PDB 9OMG 9OMG 1 225 DBREF 9OMG L 1 214 PDB 9OMG 9OMG 1 214 SEQRES 1 A 469 VAL GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 469 VAL TRP ARG ASP ALA ASP THR THR LEU PHE CYS ALA SER SEQRES 3 A 469 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 469 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 469 GLU ILE HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET SEQRES 6 A 469 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 A 469 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 469 LEU THR PRO LEU CYS VAL THR LEU HIS CYS THR ASN VAL SEQRES 9 A 469 THR SER VAL ASN THR THR GLY ASP ARG GLU GLY LEU LYS SEQRES 10 A 469 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 469 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 A 469 VAL PRO ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU SEQRES 13 A 469 ILE ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO SEQRES 14 A 469 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS THR SEQRES 15 A 469 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY SEQRES 16 A 469 PHE ASN GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL SEQRES 17 A 469 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 A 469 LEU LEU LEU ASN GLY SER LEU ALA GLU LYS ASN ILE ILE SEQRES 19 A 469 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE SEQRES 20 A 469 ILE VAL GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE SEQRES 21 A 469 ARG PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY SEQRES 22 A 469 PRO GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY SEQRES 23 A 469 ASP ILE ARG GLN ALA HIS CYS ASN VAL THR ARG SER ARG SEQRES 24 A 469 TRP ASN LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG SEQRES 25 A 469 THR TYR PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SEQRES 26 A 469 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 A 469 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 A 469 PHE ASN SER THR TRP TYR VAL ASN SER THR TRP ASN ASP SEQRES 29 A 469 THR ASP SER THR GLN GLU SER ASN ASP THR ILE THR LEU SEQRES 30 A 469 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 A 469 ALA GLY GLN ALA MET TYR ALA PRO PRO ILE PRO GLY VAL SEQRES 32 A 469 ILE LYS CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR SEQRES 33 A 469 ARG ASP GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE SEQRES 34 A 469 ARG PRO GLY GLY SER ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 A 469 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU SEQRES 36 A 469 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 37 A 469 ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ILE THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN ASN ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN LYS SER LEU ASP GLU ILE TRP ASN ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE ASN ASN TYR THR GLN LEU SEQRES 11 B 153 ILE TYR ARG LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU LYS GLU LEU LEU GLU LEU ASP SEQRES 1 C 469 VAL GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 469 VAL TRP ARG ASP ALA ASP THR THR LEU PHE CYS ALA SER SEQRES 3 C 469 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 469 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 469 GLU ILE HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET SEQRES 6 C 469 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 C 469 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 469 LEU THR PRO LEU CYS VAL THR LEU HIS CYS THR ASN VAL SEQRES 9 C 469 THR SER VAL ASN THR THR GLY ASP ARG GLU GLY LEU LYS SEQRES 10 C 469 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 469 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 C 469 VAL PRO ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU SEQRES 13 C 469 ILE ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO SEQRES 14 C 469 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS THR SEQRES 15 C 469 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY SEQRES 16 C 469 PHE ASN GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL SEQRES 17 C 469 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 C 469 LEU LEU LEU ASN GLY SER LEU ALA GLU LYS ASN ILE ILE SEQRES 19 C 469 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE SEQRES 20 C 469 ILE VAL GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE SEQRES 21 C 469 ARG PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY SEQRES 22 C 469 PRO GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY SEQRES 23 C 469 ASP ILE ARG GLN ALA HIS CYS ASN VAL THR ARG SER ARG SEQRES 24 C 469 TRP ASN LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG SEQRES 25 C 469 THR TYR PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SEQRES 26 C 469 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 C 469 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 C 469 PHE ASN SER THR TRP TYR VAL ASN SER THR TRP ASN ASP SEQRES 29 C 469 THR ASP SER THR GLN GLU SER ASN ASP THR ILE THR LEU SEQRES 30 C 469 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 C 469 ALA GLY GLN ALA MET TYR ALA PRO PRO ILE PRO GLY VAL SEQRES 32 C 469 ILE LYS CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR SEQRES 33 C 469 ARG ASP GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE SEQRES 34 C 469 ARG PRO GLY GLY SER ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 C 469 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU SEQRES 36 C 469 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 37 C 469 ARG SEQRES 1 E 469 VAL GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 469 VAL TRP ARG ASP ALA ASP THR THR LEU PHE CYS ALA SER SEQRES 3 E 469 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 E 469 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 469 GLU ILE HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET SEQRES 6 E 469 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 E 469 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 469 LEU THR PRO LEU CYS VAL THR LEU HIS CYS THR ASN VAL SEQRES 9 E 469 THR SER VAL ASN THR THR GLY ASP ARG GLU GLY LEU LYS SEQRES 10 E 469 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 E 469 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 E 469 VAL PRO ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU SEQRES 13 E 469 ILE ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO SEQRES 14 E 469 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS THR SEQRES 15 E 469 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY SEQRES 16 E 469 PHE ASN GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL SEQRES 17 E 469 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 E 469 LEU LEU LEU ASN GLY SER LEU ALA GLU LYS ASN ILE ILE SEQRES 19 E 469 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE SEQRES 20 E 469 ILE VAL GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE SEQRES 21 E 469 ARG PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY SEQRES 22 E 469 PRO GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY SEQRES 23 E 469 ASP ILE ARG GLN ALA HIS CYS ASN VAL THR ARG SER ARG SEQRES 24 E 469 TRP ASN LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG SEQRES 25 E 469 THR TYR PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SEQRES 26 E 469 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 E 469 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 E 469 PHE ASN SER THR TRP TYR VAL ASN SER THR TRP ASN ASP SEQRES 29 E 469 THR ASP SER THR GLN GLU SER ASN ASP THR ILE THR LEU SEQRES 30 E 469 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 E 469 ALA GLY GLN ALA MET TYR ALA PRO PRO ILE PRO GLY VAL SEQRES 32 E 469 ILE LYS CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR SEQRES 33 E 469 ARG ASP GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE SEQRES 34 E 469 ARG PRO GLY GLY SER ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 E 469 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU SEQRES 36 E 469 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 37 E 469 ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ILE THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN ASN ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN LYS SER LEU ASP GLU ILE TRP ASN ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE ASN ASN TYR THR GLN LEU SEQRES 11 F 153 ILE TYR ARG LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU LYS GLU LEU LEU GLU LEU ASP SEQRES 1 G 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 G 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ILE THR LEU SEQRES 3 G 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 G 153 GLN GLN ASN ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 G 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 G 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 G 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 G 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 G 153 ASN LYS SER LEU ASP GLU ILE TRP ASN ASN MET THR TRP SEQRES 10 G 153 LEU GLN TRP ASP LYS GLU ILE ASN ASN TYR THR GLN LEU SEQRES 11 G 153 ILE TYR ARG LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 G 153 LYS ASN GLU LYS GLU LEU LEU GLU LEU ASP SEQRES 1 H 244 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ALA LYS SEQRES 2 H 244 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 244 PHE THR PHE SER SER TYR TRP MET ASN TRP VAL ARG GLN SEQRES 4 H 244 THR PRO GLY LYS GLY LEU GLU TRP ILE SER ALA ILE ASN SEQRES 5 H 244 SER GLY GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 244 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 244 LEU SER LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 244 ALA VAL TYR TYR CYS ALA LYS VAL ASP GLU ASP ASP TYR SEQRES 9 H 244 GLY TYR TYR TYR THR VAL PRO GLY ASP LEU LYS LYS TYR SEQRES 10 H 244 TYR PHE ASP TYR TRP GLY GLN GLY VAL LEU VAL THR VAL SEQRES 11 H 244 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 H 244 ALA PRO SER SER ARG SER THR SER GLU SER THR ALA ALA SEQRES 13 H 244 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 H 244 THR VAL SER TRP ASN SER GLY SER LEU THR SER GLY VAL SEQRES 15 H 244 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 H 244 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 H 244 GLY THR GLN THR TYR VAL CYS ASN VAL ASN HIS LYS PRO SEQRES 18 H 244 SER ASN THR LYS VAL ASP LYS ARG VAL GLU ILE LYS THR SEQRES 19 H 244 CYS GLY GLY GLY LEU GLU VAL LEU PHE GLN SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP LYS VAL THR ILE THR CYS GLN ALA SER SEQRES 3 L 214 GLN SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS PRO LEU ILE TYR LYS ALA SER SEQRES 5 L 214 SER LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 ASN SER ALA PRO PHE SER PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER GLU ASP GLN VAL LYS SER GLY THR VAL SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA SER VAL LYS TRP LYS VAL ASP GLY ALA LEU LYS THR SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP ASN THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 SER THR GLU TYR GLN SER HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET MAN D 4 11 HET NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET BMA T 3 11 HET NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET NAG d 1 14 HET NAG d 2 14 HET NAG e 1 14 HET NAG e 2 14 HET NAG f 1 14 HET NAG f 2 14 HET BMA f 3 11 HET NAG g 1 14 HET NAG g 2 14 HET NAG h 1 14 HET NAG h 2 14 HET BMA h 3 11 HET NAG i 1 14 HET NAG i 2 14 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET MAN j 4 11 HET MAN j 5 11 HET NAG k 1 14 HET NAG k 2 14 HET BMA k 3 11 HET NAG l 1 14 HET NAG l 2 14 HET NAG m 1 14 HET NAG m 2 14 HET BMA m 3 11 HET NAG n 1 14 HET NAG n 2 14 HET BMA n 3 11 HET NAG o 1 14 HET NAG o 2 14 HET NAG p 1 14 HET NAG p 2 14 HET NAG q 1 14 HET NAG q 2 14 HET NAG r 1 14 HET NAG r 2 14 HET BMA r 3 11 HET NAG s 1 14 HET NAG s 2 14 HET NAG t 1 14 HET NAG t 2 14 HET NAG u 1 14 HET NAG u 2 14 HET BMA u 3 11 HET NAG v 1 14 HET NAG v 2 14 HET NAG w 1 14 HET NAG w 2 14 HET NAG x 1 14 HET NAG x 2 14 HET NAG y 1 14 HET NAG y 2 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG F 701 14 HET NAG F 702 14 HET NAG G 701 14 HET NAG G 702 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 9 NAG 102(C8 H15 N O6) FORMUL 9 BMA 16(C6 H12 O6) FORMUL 9 MAN 4(C6 H12 O6) HELIX 1 AA1 ALA A 70 CYS A 74 5 5 HELIX 2 AA2 TRP A 96 ASN A 98 5 3 HELIX 3 AA3 ASN A 99 LYS A 117 1 19 HELIX 4 AA4 LEU A 122 CYS A 126 5 5 HELIX 5 AA5 THR A 334 ARG A 350 1 17 HELIX 6 AA6 THR A 351 GLY A 354 5 4 HELIX 7 AA7 ASP A 368 THR A 373 1 6 HELIX 8 AA8 ASN A 377 GLU A 381 5 5 HELIX 9 AA9 THR A 387 LEU A 390 5 4 HELIX 10 AB1 MET A 475 SER A 481 1 7 HELIX 11 AB2 GLU A 482 TYR A 486 5 5 HELIX 12 AB3 THR B 529 SER B 534 1 6 HELIX 13 AB4 THR B 536 ARG B 542 1 7 HELIX 14 AB5 ASN B 543 LEU B 545 5 3 HELIX 15 AB6 HIS B 570 TRP B 596 1 27 HELIX 16 AB7 SER B 618 MET B 626 1 9 HELIX 17 AB8 TRP B 628 ASN B 636 1 9 HELIX 18 AB9 TYR B 638 LEU B 661 1 24 HELIX 19 AC1 ALA C 70 CYS C 74 5 5 HELIX 20 AC2 ASN C 98 LYS C 117 1 20 HELIX 21 AC3 LEU C 122 CYS C 126 5 5 HELIX 22 AC4 ASP C 150 GLU C 152 5 3 HELIX 23 AC5 ARG C 335 PHE C 353 1 19 HELIX 24 AC6 ASP C 368 THR C 373 1 6 HELIX 25 AC7 ASP C 474 TRP C 479 1 6 HELIX 26 AC8 ASN E 99 LYS E 117 1 19 HELIX 27 AC9 LEU E 122 CYS E 126 5 5 HELIX 28 AD1 ASP E 150 GLU E 152 5 3 HELIX 29 AD2 ARG E 335 GLY E 354 1 20 HELIX 30 AD3 ASP E 368 THR E 373 1 6 HELIX 31 AD4 ASN E 377 GLU E 381 5 5 HELIX 32 AD5 MET E 475 SER E 481 1 7 HELIX 33 AD6 GLU E 482 TYR E 484 5 3 HELIX 34 AD7 GLY F 531 ILE F 535 5 5 HELIX 35 AD8 THR F 536 ASN F 543 1 8 HELIX 36 AD9 HIS F 570 TRP F 596 1 27 HELIX 37 AE1 SER F 618 ASN F 625 1 8 HELIX 38 AE2 THR F 627 ASN F 636 1 10 HELIX 39 AE3 TYR F 638 LEU F 661 1 24 HELIX 40 AE4 THR G 529 SER G 534 1 6 HELIX 41 AE5 THR G 536 ASN G 543 1 8 HELIX 42 AE6 HIS G 570 ILE G 595 1 26 HELIX 43 AE7 SER G 618 ASN G 625 1 8 HELIX 44 AE8 THR G 627 ILE G 635 1 9 HELIX 45 AE9 THR G 639 LEU G 661 1 23 HELIX 46 AF1 THR H 28 TYR H 32 5 5 HELIX 47 AF2 ARG H 83 THR H 87 5 5 SHEET 1 AA1 3 GLY A 495 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL A 36 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 VAL A 488 ILE A 491 -1 O GLU A 490 N ARG A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 GLU A 83 HIS A 85 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 PHE A 53 CYS A 54 0 SHEET 2 AA3 2 TYR A 217 CYS A 218 -1 O CYS A 218 N PHE A 53 SHEET 1 AA4 2 GLU A 91 ASN A 94 0 SHEET 2 AA4 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA5 6 ILE A 181 PRO A 183 0 SHEET 2 AA5 6 GLU A 190 LEU A 193 -1 O ARG A 192 N VAL A 182 SHEET 3 AA5 6 LEU A 129 THR A 132 -1 N LEU A 129 O TYR A 191 SHEET 4 AA5 6 LEU A 154 THR A 162 -1 O ASN A 156 N THR A 132 SHEET 5 AA5 6 ARG A 169 TYR A 177 -1 O GLN A 170 N MET A 161 SHEET 6 AA5 6 GLY H 100A TYR H 100C-1 O TYR H 100C N ARG A 169 SHEET 1 AA6 3 ILE A 201 GLN A 203 0 SHEET 2 AA6 3 ALA A 433 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA6 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA7 6 LEU A 259 LEU A 261 0 SHEET 2 AA7 6 ILE A 443 ASP A 457 -1 O GLY A 451 N LEU A 260 SHEET 3 AA7 6 ILE A 283 ARG A 298 -1 N LEU A 288 O THR A 450 SHEET 4 AA7 6 HIS A 330 VAL A 333 -1 O ASN A 332 N LYS A 295 SHEET 5 AA7 6 ILE A 414 ILE A 420 -1 O ILE A 414 N VAL A 333 SHEET 6 AA7 6 PHE A 383 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 1 AA8 6 ILE A 271 ARG A 273 0 SHEET 2 AA8 6 ILE A 283 ARG A 298 -1 O ILE A 285 N ARG A 273 SHEET 3 AA8 6 ILE A 443 ASP A 457 -1 O THR A 450 N LEU A 288 SHEET 4 AA8 6 ASN A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AA8 6 THR A 357 PHE A 361 1 N ILE A 359 O GLU A 466 SHEET 6 AA8 6 SER A 393 TRP A 395 -1 O TRP A 395 N ILE A 358 SHEET 1 AA9 2 ASN A 301 ILE A 307 0 SHEET 2 AA9 2 PHE A 317 ILE A 323A-1 O GLY A 321 N THR A 303 SHEET 1 AB1 3 GLY C 495 THR C 499 0 SHEET 2 AB1 3 TRP C 35 TYR C 39 -1 N TRP C 35 O THR C 499 SHEET 3 AB1 3 ILE F 603 PRO F 609 -1 O CYS F 604 N VAL C 38 SHEET 1 AB2 5 TRP C 45 ASP C 47 0 SHEET 2 AB2 5 TYR C 486 ILE C 491 -1 O GLU C 490 N ARG C 46 SHEET 3 AB2 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AB2 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB2 5 ILE C 84 HIS C 85 -1 N ILE C 84 O THR C 244 SHEET 1 AB3 3 VAL C 75 PRO C 76 0 SHEET 2 AB3 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AB3 3 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AB4 2 LYS C 92 PHE C 93 0 SHEET 2 AB4 2 GLY C 237 LEU C 238 -1 O GLY C 237 N PHE C 93 SHEET 1 AB5 5 ARG C 169 TYR C 177 0 SHEET 2 AB5 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AB5 5 LEU C 129 ASN C 133 -1 N THR C 132 O ASN C 156 SHEET 4 AB5 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB5 5 ILE C 181 PRO C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AB6 3 ILE C 201 GLN C 203 0 SHEET 2 AB6 3 ALA C 433 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AB6 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AB7 7 LEU C 260 LEU C 261 0 SHEET 2 AB7 7 LYS C 444 THR C 455 -1 O GLY C 451 N LEU C 260 SHEET 3 AB7 7 ILE C 284 ILE C 297 -1 N ILE C 294 O SER C 447 SHEET 4 AB7 7 HIS C 330 THR C 334 -1 O ASN C 332 N LYS C 295 SHEET 5 AB7 7 THR C 413 LYS C 421 -1 O ILE C 414 N VAL C 333 SHEET 6 AB7 7 PHE C 382 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AB7 7 HIS C 374 SER C 375 -1 N HIS C 374 O CYS C 385 SHEET 1 AB8 4 ILE C 271 ARG C 273 0 SHEET 2 AB8 4 ILE C 284 ILE C 297 -1 O ILE C 285 N ARG C 273 SHEET 3 AB8 4 LYS C 444 THR C 455 -1 O SER C 447 N ILE C 294 SHEET 4 AB8 4 ARG C 469 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AB9 2 VAL C 304 ILE C 307 0 SHEET 2 AB9 2 PHE C 317 THR C 320 -1 O PHE C 317 N ILE C 307 SHEET 1 AC1 2 THR C 357 ILE C 358 0 SHEET 2 AC1 2 ASN C 465 GLU C 466 1 O GLU C 466 N THR C 357 SHEET 1 AC2 3 LEU E 494 THR E 499 0 SHEET 2 AC2 3 TRP E 35 TYR E 40 -1 N TYR E 39 O GLY E 495 SHEET 3 AC2 3 ILE G 603 PRO G 609 -1 O VAL G 608 N VAL E 36 SHEET 1 AC3 5 TRP E 45 ASP E 47 0 SHEET 2 AC3 5 TYR E 486 ILE E 491 -1 O GLU E 490 N ARG E 46 SHEET 3 AC3 5 PHE E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AC3 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC3 5 ILE E 84 HIS E 85 -1 N ILE E 84 O THR E 244 SHEET 1 AC4 2 PHE E 53 ALA E 55 0 SHEET 2 AC4 2 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AC5 2 GLU E 91 ASN E 94 0 SHEET 2 AC5 2 THR E 236 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AC6 5 ARG E 169 TYR E 177 0 SHEET 2 AC6 5 LEU E 154 THR E 162 -1 N MET E 161 O GLN E 170 SHEET 3 AC6 5 LEU E 129 ASN E 133 -1 N HIS E 130 O SER E 158 SHEET 4 AC6 5 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC6 5 ILE E 181 PRO E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC7 7 LEU E 259 LEU E 261 0 SHEET 2 AC7 7 LYS E 444 ARG E 456 -1 O GLY E 451 N LEU E 260 SHEET 3 AC7 7 ILE E 284 ILE E 297 -1 N LEU E 288 O THR E 450 SHEET 4 AC7 7 ALA E 329 THR E 334 -1 O ASN E 332 N LYS E 295 SHEET 5 AC7 7 THR E 413 LYS E 421 -1 O CYS E 418 N ALA E 329 SHEET 6 AC7 7 PHE E 382 CYS E 385 -1 N PHE E 382 O LYS E 421 SHEET 7 AC7 7 HIS E 374 SER E 375 -1 N HIS E 374 O CYS E 385 SHEET 1 AC8 6 ILE E 271 ARG E 273 0 SHEET 2 AC8 6 ILE E 284 ILE E 297 -1 O ILE E 285 N ARG E 273 SHEET 3 AC8 6 LYS E 444 ARG E 456 -1 O THR E 450 N LEU E 288 SHEET 4 AC8 6 ASN E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AC8 6 THR E 357 PHE E 361 1 N ILE E 359 O GLU E 466 SHEET 6 AC8 6 SER E 393 THR E 394 -1 O SER E 393 N PHE E 361 SHEET 1 AC9 2 ASN E 301 ARG E 308 0 SHEET 2 AC9 2 ALA E 316 ILE E 323A-1 O PHE E 317 N ILE E 307 SHEET 1 AD1 2 ILE E 423 ILE E 424 0 SHEET 2 AD1 2 MET E 434 TYR E 435 -1 O MET E 434 N ILE E 424 SHEET 1 AD2 4 GLN H 3 SER H 7 0 SHEET 2 AD2 4 SER H 17 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AD2 4 THR H 77 ASN H 82A-1 O LEU H 78 N CYS H 22 SHEET 4 AD2 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AD3 6 LEU H 11 ALA H 12 0 SHEET 2 AD3 6 VAL H 107 VAL H 111 1 O THR H 110 N ALA H 12 SHEET 3 AD3 6 ALA H 88 VAL H 95 -1 N TYR H 90 O VAL H 107 SHEET 4 AD3 6 MET H 34 GLN H 39 -1 N ASN H 35 O ALA H 93 SHEET 5 AD3 6 LEU H 45 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AD3 6 TYR H 58 TYR H 59 -1 O TYR H 58 N ALA H 50 SHEET 1 AD4 4 LEU H 11 ALA H 12 0 SHEET 2 AD4 4 VAL H 107 VAL H 111 1 O THR H 110 N ALA H 12 SHEET 3 AD4 4 ALA H 88 VAL H 95 -1 N TYR H 90 O VAL H 107 SHEET 4 AD4 4 PHE H 100O TRP H 103 -1 O ASP H 101 N LYS H 94 SHEET 1 AD5 4 MET L 4 SER L 7 0 SHEET 2 AD5 4 VAL L 19 ALA L 25 -1 O GLN L 24 N THR L 5 SHEET 3 AD5 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AD5 4 SER L 65 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AD6 5 SER L 10 SER L 12 0 SHEET 2 AD6 5 THR L 102 GLU L 105 1 O GLU L 105 N LEU L 11 SHEET 3 AD6 5 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD6 5 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AD6 5 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.04 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 11 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 12 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 13 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 14 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 15 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 16 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 17 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 18 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 19 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 20 CYS C 501 CYS F 605 1555 1555 2.03 SSBOND 21 CYS E 54 CYS E 74 1555 1555 2.04 SSBOND 22 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 23 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 24 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 25 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 26 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 27 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 28 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 29 CYS E 385 CYS E 418 1555 1555 2.04 SSBOND 30 CYS E 501 CYS G 605 1555 1555 2.03 SSBOND 31 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 32 CYS G 598 CYS G 604 1555 1555 2.03 SSBOND 33 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 34 CYS L 23 CYS L 88 1555 1555 2.03 LINK ND2 ASN A 133 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A 241 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 465 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN B 625 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN C 133 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG j 1 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN C 241 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG f 1 1555 1555 1.43 LINK ND2 ASN C 339 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 602 1555 1555 1.45 LINK ND2 ASN C 465 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG l 1 1555 1555 1.45 LINK ND2 ASN E 133 C1 NAG t 1 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG k 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG w 1 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG v 1 1555 1555 1.44 LINK ND2 ASN E 241 C1 NAG m 1 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG u 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG o 1 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG s 1 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG r 1 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG q 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG E 602 1555 1555 1.43 LINK ND2 ASN E 392 C1 NAG p 1 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 603 1555 1555 1.45 LINK ND2 ASN E 465 C1 NAG x 1 1555 1555 1.44 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.44 LINK ND2 ASN F 625 C1 NAG F 702 1555 1555 1.44 LINK ND2 ASN G 625 C1 NAG G 702 1555 1555 1.45 LINK ND2 ASN G 637 C1 NAG G 701 1555 1555 1.45 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44 LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.49 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.45 LINK O6 BMA V 3 C1 MAN V 4 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.45 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.44 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.45 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG h 2 C1 BMA h 3 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.44 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.44 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.45 LINK O3 BMA j 3 C1 MAN j 4 1555 1555 1.45 LINK O6 BMA j 3 C1 MAN j 5 1555 1555 1.45 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.44 LINK O4 NAG k 2 C1 BMA k 3 1555 1555 1.45 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.49 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.44 LINK O4 NAG m 2 C1 BMA m 3 1555 1555 1.45 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.44 LINK O4 NAG n 2 C1 BMA n 3 1555 1555 1.45 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.45 LINK O4 NAG p 1 C1 NAG p 2 1555 1555 1.44 LINK O4 NAG q 1 C1 NAG q 2 1555 1555 1.45 LINK O4 NAG r 1 C1 NAG r 2 1555 1555 1.44 LINK O4 NAG r 2 C1 BMA r 3 1555 1555 1.44 LINK O4 NAG s 1 C1 NAG s 2 1555 1555 1.44 LINK O4 NAG t 1 C1 NAG t 2 1555 1555 1.45 LINK O4 NAG u 1 C1 NAG u 2 1555 1555 1.44 LINK O4 NAG u 2 C1 BMA u 3 1555 1555 1.45 LINK O4 NAG v 1 C1 NAG v 2 1555 1555 1.44 LINK O4 NAG w 1 C1 NAG w 2 1555 1555 1.44 LINK O4 NAG x 1 C1 NAG x 2 1555 1555 1.45 LINK O4 NAG y 1 C1 NAG y 2 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 -0.33 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000