HEADER VIRAL PROTEIN/IMMUNE SYSTEM 15-MAY-24 9BTH TITLE RHESUS FAB 42056-A.01 IN COMPLEX WITH CAP256SU.WK34 RNS SOSIP ENV COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 11 CHAIN: G, D, F; COMPND 12 SYNONYM: ENV POLYPROTEIN; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 16 CHAIN: C, E, B; COMPND 17 FRAGMENT: UNP RESIDUES 498-651; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 11676; 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 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 13 ORGANISM_TAXID: 11676; SOURCE 14 GENE: ENV; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 4; SOURCE 18 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 19 ORGANISM_TAXID: 11676; SOURCE 20 GENE: ENV; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, SOSIP, VACCINE, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX, V2-APEX, KEYWDS 2 MULTI-DONOR, SHIV, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR J.GORMAN,P.D.KWONG REVDAT 1 11-JUN-25 9BTH 0 JRNL AUTH J.GORMAN,P.D.KWONG JRNL TITL HIV-1 NEUTRALIZING ANTIBODIES IN SHIV-INFECTEDMACAQUES JRNL TITL 2 RECAPITULATE STRUCTURALLY DIVERGENT MODES OF HUMAN V2-APEX JRNL TITL 3 RECOGNITION WITH A SINGLE D GENE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.20 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 : 6VTT REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT 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) : 4.200 REMARK 3 NUMBER OF PARTICLES : 69264 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9BTH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000283890. 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 : RHESUS FAB 42056-A.01 IN REMARK 245 COMPLEX WITH CAP256SU.WK34 RNS REMARK 245 SOSIP ENV REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 5603.00 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: H, L, G, C, D, E, F, B, A, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V 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 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 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 GLY 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 ALA 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 ILE 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 LYS H 210 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 LEU H 223 REMARK 465 PHE H 224 REMARK 465 GLN H 225 REMARK 465 ILE L 106 REMARK 465 ARG 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 ASP L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 ALA 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 LYS L 145 REMARK 465 VAL L 146 REMARK 465 GLN L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER 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 SER 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 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS 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 465 GLU G 62 REMARK 465 LYS G 63 REMARK 465 ASN G 144 REMARK 465 ALA G 145 REMARK 465 THR G 146 REMARK 465 TYR G 147 REMARK 465 LYS G 148 REMARK 465 GLY G 149 REMARK 465 THR G 150 REMARK 465 ARG G 151 REMARK 465 GLY G 185A REMARK 465 GLU G 185B REMARK 465 GLY G 185C REMARK 465 ASN G 185D REMARK 465 THR G 398A REMARK 465 TYR G 398B REMARK 465 SER G 398C REMARK 465 THR G 398D REMARK 465 GLY G 398E REMARK 465 SER G 398F REMARK 465 ASN G 398G REMARK 465 SER G 398H REMARK 465 GLY G 458 REMARK 465 GLY G 459 REMARK 465 GLY G 460 REMARK 465 ASN G 461 REMARK 465 ASN G 462 REMARK 465 SER G 463 REMARK 465 VAL G 505 REMARK 465 VAL G 506 REMARK 465 GLN G 507 REMARK 465 ARG G 508 REMARK 465 ARG G 509 REMARK 465 ARG G 510 REMARK 465 ARG G 511 REMARK 465 ARG G 512 REMARK 465 ARG G 513 REMARK 465 ALA C 511 REMARK 465 VAL C 512 REMARK 465 ARG C 542 REMARK 465 GLN C 543 REMARK 465 LEU C 544 REMARK 465 LEU C 545 REMARK 465 SER C 546 REMARK 465 GLY C 547 REMARK 465 ILE C 548 REMARK 465 VAL C 549 REMARK 465 GLN C 550 REMARK 465 GLN C 551 REMARK 465 GLN C 552 REMARK 465 SER C 553 REMARK 465 ASN C 554 REMARK 465 LEU C 555 REMARK 465 LEU C 556 REMARK 465 ARG C 557 REMARK 465 ALA C 558 REMARK 465 PRO C 559 REMARK 465 GLU C 560 REMARK 465 ALA C 561 REMARK 465 GLN C 562 REMARK 465 GLN C 563 REMARK 465 HIS C 564 REMARK 465 MET C 565 REMARK 465 LEU C 566 REMARK 465 GLN C 567 REMARK 465 ASP C 664 REMARK 465 LYS D 59 REMARK 465 SER D 60 REMARK 465 TYR D 61 REMARK 465 GLU D 62 REMARK 465 ASN D 144 REMARK 465 ALA D 145 REMARK 465 THR D 146 REMARK 465 TYR D 147 REMARK 465 LYS D 148 REMARK 465 GLY D 149 REMARK 465 THR D 150 REMARK 465 ARG D 151 REMARK 465 GLY D 185A REMARK 465 GLU D 185B REMARK 465 GLY D 185C REMARK 465 ASN D 185D REMARK 465 THR D 398A REMARK 465 TYR D 398B REMARK 465 SER D 398C REMARK 465 THR D 398D REMARK 465 GLY D 398E REMARK 465 SER D 398F REMARK 465 ASN D 398G REMARK 465 SER D 398H REMARK 465 GLY D 458 REMARK 465 GLY D 459 REMARK 465 GLY D 460 REMARK 465 ASN D 461 REMARK 465 ASN D 462 REMARK 465 SER D 463 REMARK 465 VAL D 505 REMARK 465 VAL D 506 REMARK 465 GLN D 507 REMARK 465 ARG D 508 REMARK 465 ARG D 509 REMARK 465 ARG D 510 REMARK 465 ARG D 511 REMARK 465 ARG D 512 REMARK 465 ARG D 513 REMARK 465 ALA E 511 REMARK 465 VAL E 512 REMARK 465 VAL E 513 REMARK 465 GLY E 514 REMARK 465 ALA E 541 REMARK 465 ARG E 542 REMARK 465 GLN E 543 REMARK 465 LEU E 544 REMARK 465 LEU E 545 REMARK 465 SER E 546 REMARK 465 GLY E 547 REMARK 465 ILE E 548 REMARK 465 VAL E 549 REMARK 465 GLN E 550 REMARK 465 GLN E 551 REMARK 465 GLN E 552 REMARK 465 SER E 553 REMARK 465 ASN E 554 REMARK 465 LEU E 555 REMARK 465 LEU E 556 REMARK 465 ARG E 557 REMARK 465 ALA E 558 REMARK 465 PRO E 559 REMARK 465 GLU E 560 REMARK 465 ALA E 561 REMARK 465 GLN E 562 REMARK 465 GLN E 563 REMARK 465 HIS E 564 REMARK 465 MET E 565 REMARK 465 LEU E 566 REMARK 465 GLN E 567 REMARK 465 ASP E 664 REMARK 465 LYS F 59 REMARK 465 SER F 60 REMARK 465 TYR F 61 REMARK 465 GLU F 62 REMARK 465 LYS F 63 REMARK 465 ASN F 144 REMARK 465 ALA F 145 REMARK 465 THR F 146 REMARK 465 TYR F 147 REMARK 465 LYS F 148 REMARK 465 GLY F 149 REMARK 465 THR F 150 REMARK 465 ARG F 151 REMARK 465 GLY F 185A REMARK 465 GLU F 185B REMARK 465 GLY F 185C REMARK 465 ASN F 185D REMARK 465 THR F 398A REMARK 465 TYR F 398B REMARK 465 SER F 398C REMARK 465 THR F 398D REMARK 465 GLY F 398E REMARK 465 SER F 398F REMARK 465 ASN F 398G REMARK 465 SER F 398H REMARK 465 GLY F 458 REMARK 465 GLY F 459 REMARK 465 GLY F 460 REMARK 465 ASN F 461 REMARK 465 ASN F 462 REMARK 465 SER F 463 REMARK 465 VAL F 505 REMARK 465 VAL F 506 REMARK 465 GLN F 507 REMARK 465 ARG F 508 REMARK 465 ARG F 509 REMARK 465 ARG F 510 REMARK 465 ARG F 511 REMARK 465 ARG F 512 REMARK 465 ARG F 513 REMARK 465 ALA B 511 REMARK 465 GLN B 543 REMARK 465 LEU B 544 REMARK 465 LEU B 545 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 SER 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 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 MET B 565 REMARK 465 LEU B 566 REMARK 465 GLN B 567 REMARK 465 ASP B 664 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 VAL G 36 OG1 THR C 606 2.04 REMARK 500 O VAL F 307 OG1 THR F 316 2.08 REMARK 500 OG SER G 264 OE1 GLU G 482 2.10 REMARK 500 O VAL D 36 OG1 THR E 606 2.11 REMARK 500 O LEU D 277 NH1 ARG D 456 2.16 REMARK 500 O ALA B 532 OG1 THR B 536 2.18 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 LEU H 48 -60.61 -100.66 REMARK 500 ASP H 53 51.05 -92.86 REMARK 500 ALA H 54 -97.85 50.92 REMARK 500 ASP H 100B 50.10 -97.38 REMARK 500 TYS H 100C -67.38 65.56 REMARK 500 SER H 100H 145.40 -171.71 REMARK 500 SER L 27A -65.21 67.55 REMARK 500 LEU L 27B 158.12 65.14 REMARK 500 VAL L 27C 54.63 39.48 REMARK 500 ARG L 27E -98.01 56.58 REMARK 500 GLN L 27F 17.01 56.41 REMARK 500 LYS L 30 -178.66 -172.62 REMARK 500 VAL L 51 -46.79 74.21 REMARK 500 TYR G 40 45.85 -93.28 REMARK 500 SER G 60 165.40 64.46 REMARK 500 VAL G 68 -66.57 60.53 REMARK 500 THR G 71 -115.94 60.85 REMARK 500 ALA G 73 172.56 81.11 REMARK 500 CYS G 74 -169.61 -118.37 REMARK 500 THR G 77 -170.46 54.73 REMARK 500 GLN G 82 16.11 -143.06 REMARK 500 ILE G 108 -77.12 65.89 REMARK 500 SER G 189 174.88 64.78 REMARK 500 ASN G 234 44.62 -91.00 REMARK 500 PRO G 253 71.63 -68.74 REMARK 500 GLU G 268 18.33 56.04 REMARK 500 PHE G 392 -159.75 -150.61 REMARK 500 ASN G 393 0.53 83.05 REMARK 500 LEU G 453 59.77 -95.07 REMARK 500 LYS G 485 35.62 -99.35 REMARK 500 ALA C 526 -161.80 60.36 REMARK 500 LEU D 34 163.62 62.88 REMARK 500 GLU D 64 177.09 66.67 REMARK 500 VAL D 65 155.50 62.76 REMARK 500 THR D 71 -169.56 62.83 REMARK 500 HIS D 72 33.13 -96.72 REMARK 500 THR D 77 -112.39 70.68 REMARK 500 ASP D 78 60.08 38.38 REMARK 500 GLN D 82 35.04 -89.23 REMARK 500 ASP D 107 -169.66 -115.82 REMARK 500 ILE D 108 -57.61 69.19 REMARK 500 ASP D 133 169.06 179.73 REMARK 500 THR D 232 38.11 -98.15 REMARK 500 ASN D 262 11.98 59.63 REMARK 500 GLU D 268 -7.72 75.34 REMARK 500 THR D 387 17.81 50.35 REMARK 500 PHE D 392 -74.45 -112.80 REMARK 500 ASN D 393 -13.51 59.14 REMARK 500 LYS D 394 -175.05 -173.56 REMARK 500 GLN D 428 57.37 38.21 REMARK 500 REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44890 RELATED DB: EMDB REMARK 900 RHESUS FAB 42056-A.01 IN COMPLEX WITH CAP256SU.WK34 RNS SOSIP ENV DBREF 9BTH H 1 225 PDB 9BTH 9BTH 1 225 DBREF 9BTH L 1 214 PDB 9BTH 9BTH 1 214 DBREF1 9BTH G 33 511 UNP A0A0N9FF17_9HIV1 DBREF2 9BTH G A0A0N9FF17 29 497 DBREF1 9BTH C 511 664 UNP A0A0N9FF17_9HIV1 DBREF2 9BTH C A0A0N9FF17 498 651 DBREF1 9BTH D 33 511 UNP A0A0N9FF17_9HIV1 DBREF2 9BTH D A0A0N9FF17 29 497 DBREF1 9BTH E 511 664 UNP A0A0N9FF17_9HIV1 DBREF2 9BTH E A0A0N9FF17 498 651 DBREF1 9BTH F 33 511 UNP A0A0N9FF17_9HIV1 DBREF2 9BTH F A0A0N9FF17 29 497 DBREF1 9BTH B 511 664 UNP A0A0N9FF17_9HIV1 DBREF2 9BTH B A0A0N9FF17 498 651 SEQADV 9BTH ILE G 204 UNP A0A0N9FF1 ALA 196 CONFLICT SEQADV 9BTH MET G 302 UNP A0A0N9FF1 ASN 294 CONFLICT SEQADV 9BTH LEU G 320 UNP A0A0N9FF1 THR 310 CONFLICT SEQADV 9BTH PRO G 329 UNP A0A0N9FF1 ALA 320 CONFLICT SEQADV 9BTH PRO G 437 UNP A0A0N9FF1 SER 423 CONFLICT SEQADV 9BTH ASN G 442 UNP A0A0N9FF1 GLU 428 CONFLICT SEQADV 9BTH CYS G 501 UNP A0A0N9FF1 ALA 487 CONFLICT SEQADV 9BTH ASN G 502 UNP A0A0N9FF1 ARG 488 CONFLICT SEQADV 9BTH THR G 504 UNP A0A0N9FF1 ARG 490 CONFLICT SEQADV 9BTH ARG G 508 UNP A0A0N9FF1 LYS 494 CONFLICT SEQADV 9BTH ARG G 509 UNP A0A0N9FF1 GLU 495 CONFLICT SEQADV 9BTH ARG G 510 UNP A0A0N9FF1 LYS 496 CONFLICT SEQADV 9BTH ARG G 512 UNP A0A0N9FF1 EXPRESSION TAG SEQADV 9BTH ARG G 513 UNP A0A0N9FF1 EXPRESSION TAG SEQADV 9BTH ASN C 535 UNP A0A0N9FF1 ILE 522 CONFLICT SEQADV 9BTH PRO C 559 UNP A0A0N9FF1 ILE 546 CONFLICT SEQADV 9BTH GLY C 569 UNP A0A0N9FF1 THR 556 CONFLICT SEQADV 9BTH PHE C 573 UNP A0A0N9FF1 ILE 560 CONFLICT SEQADV 9BTH GLU C 588 UNP A0A0N9FF1 LYS 575 CONFLICT SEQADV 9BTH VAL C 589 UNP A0A0N9FF1 ASP 576 CONFLICT SEQADV 9BTH CYS C 605 UNP A0A0N9FF1 THR 592 CONFLICT SEQADV 9BTH PRO C 609 UNP A0A0N9FF1 TYR 596 CONFLICT SEQADV 9BTH GLY C 636 UNP A0A0N9FF1 ASP 623 CONFLICT SEQADV 9BTH PHE C 651 UNP A0A0N9FF1 LYS 638 CONFLICT SEQADV 9BTH ILE C 655 UNP A0A0N9FF1 SER 642 CONFLICT SEQADV 9BTH ASN C 660 UNP A0A0N9FF1 LEU 647 CONFLICT SEQADV 9BTH THR C 662 UNP A0A0N9FF1 ALA 649 CONFLICT SEQADV 9BTH ILE D 204 UNP A0A0N9FF1 ALA 196 CONFLICT SEQADV 9BTH MET D 302 UNP A0A0N9FF1 ASN 294 CONFLICT SEQADV 9BTH LEU D 320 UNP A0A0N9FF1 THR 310 CONFLICT SEQADV 9BTH PRO D 329 UNP A0A0N9FF1 ALA 320 CONFLICT SEQADV 9BTH PRO D 437 UNP A0A0N9FF1 SER 423 CONFLICT SEQADV 9BTH ASN D 442 UNP A0A0N9FF1 GLU 428 CONFLICT SEQADV 9BTH CYS D 501 UNP A0A0N9FF1 ALA 487 CONFLICT SEQADV 9BTH ASN D 502 UNP A0A0N9FF1 ARG 488 CONFLICT SEQADV 9BTH THR D 504 UNP A0A0N9FF1 ARG 490 CONFLICT SEQADV 9BTH ARG D 508 UNP A0A0N9FF1 LYS 494 CONFLICT SEQADV 9BTH ARG D 509 UNP A0A0N9FF1 GLU 495 CONFLICT SEQADV 9BTH ARG D 510 UNP A0A0N9FF1 LYS 496 CONFLICT SEQADV 9BTH ARG D 512 UNP A0A0N9FF1 EXPRESSION TAG SEQADV 9BTH ARG D 513 UNP A0A0N9FF1 EXPRESSION TAG SEQADV 9BTH ASN E 535 UNP A0A0N9FF1 ILE 522 CONFLICT SEQADV 9BTH PRO E 559 UNP A0A0N9FF1 ILE 546 CONFLICT SEQADV 9BTH GLY E 569 UNP A0A0N9FF1 THR 556 CONFLICT SEQADV 9BTH PHE E 573 UNP A0A0N9FF1 ILE 560 CONFLICT SEQADV 9BTH GLU E 588 UNP A0A0N9FF1 LYS 575 CONFLICT SEQADV 9BTH VAL E 589 UNP A0A0N9FF1 ASP 576 CONFLICT SEQADV 9BTH CYS E 605 UNP A0A0N9FF1 THR 592 CONFLICT SEQADV 9BTH PRO E 609 UNP A0A0N9FF1 TYR 596 CONFLICT SEQADV 9BTH GLY E 636 UNP A0A0N9FF1 ASP 623 CONFLICT SEQADV 9BTH PHE E 651 UNP A0A0N9FF1 LYS 638 CONFLICT SEQADV 9BTH ILE E 655 UNP A0A0N9FF1 SER 642 CONFLICT SEQADV 9BTH ASN E 660 UNP A0A0N9FF1 LEU 647 CONFLICT SEQADV 9BTH THR E 662 UNP A0A0N9FF1 ALA 649 CONFLICT SEQADV 9BTH ILE F 204 UNP A0A0N9FF1 ALA 196 CONFLICT SEQADV 9BTH MET F 302 UNP A0A0N9FF1 ASN 294 CONFLICT SEQADV 9BTH LEU F 320 UNP A0A0N9FF1 THR 310 CONFLICT SEQADV 9BTH PRO F 329 UNP A0A0N9FF1 ALA 320 CONFLICT SEQADV 9BTH PRO F 437 UNP A0A0N9FF1 SER 423 CONFLICT SEQADV 9BTH ASN F 442 UNP A0A0N9FF1 GLU 428 CONFLICT SEQADV 9BTH CYS F 501 UNP A0A0N9FF1 ALA 487 CONFLICT SEQADV 9BTH ASN F 502 UNP A0A0N9FF1 ARG 488 CONFLICT SEQADV 9BTH THR F 504 UNP A0A0N9FF1 ARG 490 CONFLICT SEQADV 9BTH ARG F 508 UNP A0A0N9FF1 LYS 494 CONFLICT SEQADV 9BTH ARG F 509 UNP A0A0N9FF1 GLU 495 CONFLICT SEQADV 9BTH ARG F 510 UNP A0A0N9FF1 LYS 496 CONFLICT SEQADV 9BTH ARG F 512 UNP A0A0N9FF1 EXPRESSION TAG SEQADV 9BTH ARG F 513 UNP A0A0N9FF1 EXPRESSION TAG SEQADV 9BTH ASN B 535 UNP A0A0N9FF1 ILE 522 CONFLICT SEQADV 9BTH PRO B 559 UNP A0A0N9FF1 ILE 546 CONFLICT SEQADV 9BTH GLY B 569 UNP A0A0N9FF1 THR 556 CONFLICT SEQADV 9BTH PHE B 573 UNP A0A0N9FF1 ILE 560 CONFLICT SEQADV 9BTH GLU B 588 UNP A0A0N9FF1 LYS 575 CONFLICT SEQADV 9BTH VAL B 589 UNP A0A0N9FF1 ASP 576 CONFLICT SEQADV 9BTH CYS B 605 UNP A0A0N9FF1 THR 592 CONFLICT SEQADV 9BTH PRO B 609 UNP A0A0N9FF1 TYR 596 CONFLICT SEQADV 9BTH GLY B 636 UNP A0A0N9FF1 ASP 623 CONFLICT SEQADV 9BTH PHE B 651 UNP A0A0N9FF1 LYS 638 CONFLICT SEQADV 9BTH ILE B 655 UNP A0A0N9FF1 SER 642 CONFLICT SEQADV 9BTH ASN B 660 UNP A0A0N9FF1 LEU 647 CONFLICT SEQADV 9BTH THR B 662 UNP A0A0N9FF1 ALA 649 CONFLICT SEQRES 1 H 244 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY MET VAL LYS SEQRES 2 H 244 PRO SER GLU THR LEU THR LEU THR CYS ALA VAL PHE GLY SEQRES 3 H 244 GLY ARG VAL THR SER GLY ASP SER PHE TRP THR TRP ILE SEQRES 4 H 244 ARG GLN SER PRO THR LYS GLY LEU GLU TRP LEU ALA GLY SEQRES 5 H 244 ILE SER GLY ASP ALA ASP ASN PRO THR TYR ASN PRO SER SEQRES 6 H 244 LEU LYS SER ARG LEU THR ILE SER LYS ASP PRO SER LYS SEQRES 7 H 244 ASN GLN VAL SER LEU LYS VAL THR SER VAL THR ALA THR SEQRES 8 H 244 ASP THR ALA VAL TYR TYR CYS ALA ARG GLU LYS GLN TYR SEQRES 9 H 244 TYR PHE ASP ASP TYS TYR SER VAL GLU SER GLY ARG VAL SEQRES 10 H 244 GLY MET ASP SER TRP GLY GLN GLY VAL ALA VAL ILE 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 LYS SER THR SER GLY GLY 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 ALA 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 ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 H 244 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 H 244 CYS ASP LYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 L 220 ASP ILE VAL MET THR GLN THR PRO ILE SER LEU PRO VAL SEQRES 2 L 220 SER LEU GLY GLU SER ALA THR ILE SER CYS ARG SER SER SEQRES 3 L 220 ARG SER LEU VAL ASP ARG GLN ASP GLY LYS THR TYR LEU SEQRES 4 L 220 GLU TRP TYR PHE GLN LYS PRO GLY GLN SER PRO GLN LEU SEQRES 5 L 220 LEU ILE TYR GLU VAL ALA ASN ARG ALA SER GLY VAL PRO SEQRES 6 L 220 ASP ARG PHE ARG GLY SER GLY SER ASP THR ASP PHE THR SEQRES 7 L 220 LEU LYS ILE SER ARG VAL GLU ALA ASP ASP VAL ALA ILE SEQRES 8 L 220 TYR TYR CYS MET GLN SER LEU ASP PRO PRO HIS THR PHE SEQRES 9 L 220 GLY GLN GLY THR LYS VAL GLU ILE ARG ARG THR VAL ALA SEQRES 10 L 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 L 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 L 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 L 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 L 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 L 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 L 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 L 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 471 GLY LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 G 471 ARG GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 G 471 LYS SER TYR GLU LYS GLU VAL HIS ASN VAL TRP ALA THR SEQRES 4 G 471 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU LEU SEQRES 5 G 471 VAL LEU GLU ASN VAL THR GLU ASN PHE ASN MET TRP LYS SEQRES 6 G 471 ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE ILE SER SEQRES 7 G 471 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 G 471 PRO LEU CYS VAL THR LEU ASN CYS SER ASP ALA LYS VAL SEQRES 9 G 471 ASN ALA THR TYR LYS GLY THR ARG GLU GLU ILE LYS ASN SEQRES 10 G 471 CYS SER PHE ASN ALA THR THR GLU LEU ARG ASP LYS LYS SEQRES 11 G 471 ARG ARG GLU TYR ALA LEU PHE TYR ARG LEU ASP ILE VAL SEQRES 12 G 471 PRO LEU SER GLY GLU GLY ASN ASN ASN SER GLU TYR ARG SEQRES 13 G 471 LEU ILE ASN CYS ASN THR SER VAL ILE THR GLN ILE CYS SEQRES 14 G 471 PRO LYS VAL THR PHE ASP PRO ILE PRO ILE HIS TYR CYS SEQRES 15 G 471 ALA PRO ALA GLY TYR ALA ILE LEU LYS CYS ASN ASN LYS SEQRES 16 G 471 THR PHE ASN GLY THR GLY PRO CYS ASN ASN VAL SER THR SEQRES 17 G 471 VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR SEQRES 18 G 471 GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU ILE SEQRES 19 G 471 ILE ILE ARG SER GLU ASN LEU THR ASP ASN VAL LYS THR SEQRES 20 G 471 ILE ILE VAL HIS LEU ASN GLU SER VAL GLU ILE THR CYS SEQRES 21 G 471 THR ARG PRO ASN ASN MET THR ARG LYS SER VAL ARG ILE SEQRES 22 G 471 GLY PRO GLY GLN THR PHE TYR ALA LEU GLY ASP ILE ILE SEQRES 23 G 471 GLY ASP ILE ARG GLN PRO HIS CYS ASN ILE SER GLU ILE SEQRES 24 G 471 LYS TRP GLU LYS THR LEU GLN ARG VAL SER GLU LYS LEU SEQRES 25 G 471 ARG GLU HIS PHE ASN LYS THR ILE ILE PHE ASN GLN SER SEQRES 26 G 471 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 G 471 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER ASP LEU SEQRES 28 G 471 PHE PHE ASN LYS THR PHE ASN GLU THR TYR SER THR GLY SEQRES 29 G 471 SER ASN SER THR ASN SER THR ILE THR LEU PRO CYS ARG SEQRES 30 G 471 ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL GLY ARG SEQRES 31 G 471 ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 G 471 LYS SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 G 471 GLY GLY ASN ASN SER THR LYS GLU THR PHE ARG PRO GLY SEQRES 34 G 471 GLY GLY ASN MET ARG ASP ASN TRP ARG SER GLU LEU TYR SEQRES 35 G 471 LYS TYR LYS VAL VAL GLU VAL LYS PRO LEU GLY ILE ALA SEQRES 36 G 471 PRO THR GLU CYS ASN ARG THR VAL VAL GLN ARG ARG ARG SEQRES 37 G 471 ARG ARG ARG SEQRES 1 C 154 ALA VAL VAL GLY LEU GLY ALA VAL PHE LEU GLY PHE LEU SEQRES 2 C 154 GLY ALA ALA GLY SER THR MET GLY ALA ALA SER ASN THR SEQRES 3 C 154 LEU THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL SEQRES 4 C 154 GLN GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN SEQRES 5 C 154 GLN HIS MET LEU GLN LEU GLY VAL TRP GLY PHE LYS GLN SEQRES 6 C 154 LEU GLN ALA ARG VAL LEU ALA ILE GLU ARG TYR LEU GLU SEQRES 7 C 154 VAL GLN GLN LEU LEU GLY MET TRP GLY CYS SER GLY LYS SEQRES 8 C 154 LEU ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SEQRES 9 C 154 SER ASN LYS THR TYR ASN GLU ILE TRP ASP ASN MET THR SEQRES 10 C 154 TRP MET GLN TRP ASP ARG GLU ILE GLY ASN TYR THR ASP SEQRES 11 C 154 THR ILE TYR LYS LEU LEU GLU VAL SER GLN PHE GLN GLN SEQRES 12 C 154 GLU ILE ASN GLU LYS ASP ASN LEU THR LEU ASP SEQRES 1 D 471 GLY LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 D 471 ARG GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 D 471 LYS SER TYR GLU LYS GLU VAL HIS ASN VAL TRP ALA THR SEQRES 4 D 471 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU LEU SEQRES 5 D 471 VAL LEU GLU ASN VAL THR GLU ASN PHE ASN MET TRP LYS SEQRES 6 D 471 ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE ILE SER SEQRES 7 D 471 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 D 471 PRO LEU CYS VAL THR LEU ASN CYS SER ASP ALA LYS VAL SEQRES 9 D 471 ASN ALA THR TYR LYS GLY THR ARG GLU GLU ILE LYS ASN SEQRES 10 D 471 CYS SER PHE ASN ALA THR THR GLU LEU ARG ASP LYS LYS SEQRES 11 D 471 ARG ARG GLU TYR ALA LEU PHE TYR ARG LEU ASP ILE VAL SEQRES 12 D 471 PRO LEU SER GLY GLU GLY ASN ASN ASN SER GLU TYR ARG SEQRES 13 D 471 LEU ILE ASN CYS ASN THR SER VAL ILE THR GLN ILE CYS SEQRES 14 D 471 PRO LYS VAL THR PHE ASP PRO ILE PRO ILE HIS TYR CYS SEQRES 15 D 471 ALA PRO ALA GLY TYR ALA ILE LEU LYS CYS ASN ASN LYS SEQRES 16 D 471 THR PHE ASN GLY THR GLY PRO CYS ASN ASN VAL SER THR SEQRES 17 D 471 VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR SEQRES 18 D 471 GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU ILE SEQRES 19 D 471 ILE ILE ARG SER GLU ASN LEU THR ASP ASN VAL LYS THR SEQRES 20 D 471 ILE ILE VAL HIS LEU ASN GLU SER VAL GLU ILE THR CYS SEQRES 21 D 471 THR ARG PRO ASN ASN MET THR ARG LYS SER VAL ARG ILE SEQRES 22 D 471 GLY PRO GLY GLN THR PHE TYR ALA LEU GLY ASP ILE ILE SEQRES 23 D 471 GLY ASP ILE ARG GLN PRO HIS CYS ASN ILE SER GLU ILE SEQRES 24 D 471 LYS TRP GLU LYS THR LEU GLN ARG VAL SER GLU LYS LEU SEQRES 25 D 471 ARG GLU HIS PHE ASN LYS THR ILE ILE PHE ASN GLN SER SEQRES 26 D 471 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 D 471 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER ASP LEU SEQRES 28 D 471 PHE PHE ASN LYS THR PHE ASN GLU THR TYR SER THR GLY SEQRES 29 D 471 SER ASN SER THR ASN SER THR ILE THR LEU PRO CYS ARG SEQRES 30 D 471 ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL GLY ARG SEQRES 31 D 471 ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 D 471 LYS SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 D 471 GLY GLY ASN ASN SER THR LYS GLU THR PHE ARG PRO GLY SEQRES 34 D 471 GLY GLY ASN MET ARG ASP ASN TRP ARG SER GLU LEU TYR SEQRES 35 D 471 LYS TYR LYS VAL VAL GLU VAL LYS PRO LEU GLY ILE ALA SEQRES 36 D 471 PRO THR GLU CYS ASN ARG THR VAL VAL GLN ARG ARG ARG SEQRES 37 D 471 ARG ARG ARG SEQRES 1 E 154 ALA VAL VAL GLY LEU GLY ALA VAL PHE LEU GLY PHE LEU SEQRES 2 E 154 GLY ALA ALA GLY SER THR MET GLY ALA ALA SER ASN THR SEQRES 3 E 154 LEU THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL SEQRES 4 E 154 GLN GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN SEQRES 5 E 154 GLN HIS MET LEU GLN LEU GLY VAL TRP GLY PHE LYS GLN SEQRES 6 E 154 LEU GLN ALA ARG VAL LEU ALA ILE GLU ARG TYR LEU GLU SEQRES 7 E 154 VAL GLN GLN LEU LEU GLY MET TRP GLY CYS SER GLY LYS SEQRES 8 E 154 LEU ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SEQRES 9 E 154 SER ASN LYS THR TYR ASN GLU ILE TRP ASP ASN MET THR SEQRES 10 E 154 TRP MET GLN TRP ASP ARG GLU ILE GLY ASN TYR THR ASP SEQRES 11 E 154 THR ILE TYR LYS LEU LEU GLU VAL SER GLN PHE GLN GLN SEQRES 12 E 154 GLU ILE ASN GLU LYS ASP ASN LEU THR LEU ASP SEQRES 1 F 471 GLY LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 F 471 ARG GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 F 471 LYS SER TYR GLU LYS GLU VAL HIS ASN VAL TRP ALA THR SEQRES 4 F 471 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU LEU SEQRES 5 F 471 VAL LEU GLU ASN VAL THR GLU ASN PHE ASN MET TRP LYS SEQRES 6 F 471 ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE ILE SER SEQRES 7 F 471 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 F 471 PRO LEU CYS VAL THR LEU ASN CYS SER ASP ALA LYS VAL SEQRES 9 F 471 ASN ALA THR TYR LYS GLY THR ARG GLU GLU ILE LYS ASN SEQRES 10 F 471 CYS SER PHE ASN ALA THR THR GLU LEU ARG ASP LYS LYS SEQRES 11 F 471 ARG ARG GLU TYR ALA LEU PHE TYR ARG LEU ASP ILE VAL SEQRES 12 F 471 PRO LEU SER GLY GLU GLY ASN ASN ASN SER GLU TYR ARG SEQRES 13 F 471 LEU ILE ASN CYS ASN THR SER VAL ILE THR GLN ILE CYS SEQRES 14 F 471 PRO LYS VAL THR PHE ASP PRO ILE PRO ILE HIS TYR CYS SEQRES 15 F 471 ALA PRO ALA GLY TYR ALA ILE LEU LYS CYS ASN ASN LYS SEQRES 16 F 471 THR PHE ASN GLY THR GLY PRO CYS ASN ASN VAL SER THR SEQRES 17 F 471 VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR SEQRES 18 F 471 GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU ILE SEQRES 19 F 471 ILE ILE ARG SER GLU ASN LEU THR ASP ASN VAL LYS THR SEQRES 20 F 471 ILE ILE VAL HIS LEU ASN GLU SER VAL GLU ILE THR CYS SEQRES 21 F 471 THR ARG PRO ASN ASN MET THR ARG LYS SER VAL ARG ILE SEQRES 22 F 471 GLY PRO GLY GLN THR PHE TYR ALA LEU GLY ASP ILE ILE SEQRES 23 F 471 GLY ASP ILE ARG GLN PRO HIS CYS ASN ILE SER GLU ILE SEQRES 24 F 471 LYS TRP GLU LYS THR LEU GLN ARG VAL SER GLU LYS LEU SEQRES 25 F 471 ARG GLU HIS PHE ASN LYS THR ILE ILE PHE ASN GLN SER SEQRES 26 F 471 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 F 471 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER ASP LEU SEQRES 28 F 471 PHE PHE ASN LYS THR PHE ASN GLU THR TYR SER THR GLY SEQRES 29 F 471 SER ASN SER THR ASN SER THR ILE THR LEU PRO CYS ARG SEQRES 30 F 471 ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL GLY ARG SEQRES 31 F 471 ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 F 471 LYS SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 F 471 GLY GLY ASN ASN SER THR LYS GLU THR PHE ARG PRO GLY SEQRES 34 F 471 GLY GLY ASN MET ARG ASP ASN TRP ARG SER GLU LEU TYR SEQRES 35 F 471 LYS TYR LYS VAL VAL GLU VAL LYS PRO LEU GLY ILE ALA SEQRES 36 F 471 PRO THR GLU CYS ASN ARG THR VAL VAL GLN ARG ARG ARG SEQRES 37 F 471 ARG ARG ARG SEQRES 1 B 154 ALA VAL VAL GLY LEU GLY ALA VAL PHE LEU GLY PHE LEU SEQRES 2 B 154 GLY ALA ALA GLY SER THR MET GLY ALA ALA SER ASN THR SEQRES 3 B 154 LEU THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL SEQRES 4 B 154 GLN GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN SEQRES 5 B 154 GLN HIS MET LEU GLN LEU GLY VAL TRP GLY PHE LYS GLN SEQRES 6 B 154 LEU GLN ALA ARG VAL LEU ALA ILE GLU ARG TYR LEU GLU SEQRES 7 B 154 VAL GLN GLN LEU LEU GLY MET TRP GLY CYS SER GLY LYS SEQRES 8 B 154 LEU ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SEQRES 9 B 154 SER ASN LYS THR TYR ASN GLU ILE TRP ASP ASN MET THR SEQRES 10 B 154 TRP MET GLN TRP ASP ARG GLU ILE GLY ASN TYR THR ASP SEQRES 11 B 154 THR ILE TYR LYS LEU LEU GLU VAL SER GLN PHE GLN GLN SEQRES 12 B 154 GLU ILE ASN GLU LYS ASP ASN LEU THR LEU ASP HET TYS H 100C 16 HET NAG A 1 14 HET NAG A 2 14 HET BMA A 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 MAN K 4 11 HET MAN K 5 11 HET MAN K 6 11 HET NAG M 1 14 HET NAG M 2 14 HET BMA M 3 11 HET MAN M 4 11 HET MAN M 5 11 HET MAN M 6 11 HET MAN M 7 11 HET MAN M 8 11 HET MAN M 9 11 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 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 MAN Q 4 11 HET MAN Q 5 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 MAN T 4 11 HET MAN T 5 11 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 11 HET MAN U 5 11 HET MAN U 6 11 HET MAN U 7 11 HET NAG V 1 14 HET NAG V 2 14 HET NAG G 601 14 HET NAG G 602 14 HET NAG G 603 14 HET NAG G 604 14 HET NAG G 605 14 HET NAG G 606 14 HET NAG G 607 14 HET NAG G 608 14 HET NAG G 609 14 HET NAG G 610 14 HET NAG G 611 14 HET NAG G 612 14 HET NAG G 613 14 HET NAG G 614 14 HET NAG G 615 14 HET NAG G 616 14 HET NAG C 701 14 HET NAG C 702 14 HET NAG D 601 14 HET NAG D 602 14 HET NAG D 603 14 HET NAG D 604 14 HET NAG D 605 14 HET NAG D 606 14 HET NAG D 607 14 HET NAG D 608 14 HET NAG D 609 14 HET NAG D 610 14 HET NAG D 611 14 HET NAG D 612 14 HET NAG D 613 14 HET NAG D 614 14 HET NAG D 615 14 HET NAG E 701 14 HET NAG E 702 14 HET NAG E 703 14 HET NAG E 704 14 HET NAG F 601 14 HET NAG F 602 14 HET NAG F 603 14 HET NAG F 604 14 HET NAG F 605 14 HET NAG F 606 14 HET NAG F 607 14 HET NAG F 608 14 HET NAG F 609 14 HET NAG F 610 14 HET NAG F 611 14 HET NAG F 612 14 HET NAG F 613 14 HET NAG F 614 14 HET NAG F 615 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG B 704 14 HETNAM TYS O-SULFO-L-TYROSINE 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 1 TYS C9 H11 N O6 S FORMUL 9 NAG 84(C8 H15 N O6) FORMUL 9 BMA 8(C6 H12 O6) FORMUL 11 MAN 19(C6 H12 O6) HELIX 1 AA1 PRO H 61 SER H 65 5 5 HELIX 2 AA2 THR H 83 THR H 87 5 5 HELIX 3 AA3 GLU L 79 VAL L 83 5 5 HELIX 4 AA4 ASN G 98 ASP G 107 1 10 HELIX 5 AA5 ILE G 108 LYS G 117 1 10 HELIX 6 AA6 LEU G 122 CYS G 126 5 5 HELIX 7 AA7 ASN G 195 THR G 198 5 4 HELIX 8 AA8 GLU G 335 GLU G 351 1 17 HELIX 9 AA9 MET G 475 SER G 481 1 7 HELIX 10 AB1 LEU C 515 LEU C 520 1 6 HELIX 11 AB2 GLY C 521 GLY C 524 5 4 HELIX 12 AB3 THR C 529 SER C 534 1 6 HELIX 13 AB4 LEU C 537 ALA C 541 5 5 HELIX 14 AB5 VAL C 570 TRP C 596 1 27 HELIX 15 AB6 THR C 618 TRP C 623 1 6 HELIX 16 AB7 THR C 627 GLY C 636 1 10 HELIX 17 AB8 TYR C 638 THR C 662 1 25 HELIX 18 AB9 MET D 100 ASP D 107 1 8 HELIX 19 AC1 ILE D 108 LYS D 117 1 10 HELIX 20 AC2 LEU D 122 CYS D 126 5 5 HELIX 21 AC3 ASN D 195 ASN D 197 5 3 HELIX 22 AC4 SER D 334 ASN D 356 1 21 HELIX 23 AC5 ASN D 425 GLU D 429 5 5 HELIX 24 AC6 ASN D 474 ASN D 478 5 5 HELIX 25 AC7 TRP D 479 TYR D 484 1 6 HELIX 26 AC8 VAL E 518 GLY E 524 1 7 HELIX 27 AC9 ALA E 532 GLN E 540 1 9 HELIX 28 AD1 GLY E 569 TRP E 596 1 28 HELIX 29 AD2 THR E 618 TRP E 623 1 6 HELIX 30 AD3 THR E 627 GLY E 636 1 10 HELIX 31 AD4 TYR E 638 LEU E 663 1 26 HELIX 32 AD5 ASP F 99 LEU F 116 1 18 HELIX 33 AD6 LEU F 122 CYS F 126 5 5 HELIX 34 AD7 SER F 334 LEU F 349 1 16 HELIX 35 AD8 ARG F 350 PHE F 353 5 4 HELIX 36 AD9 MET F 475 LEU F 483 1 9 HELIX 37 AE1 TYR F 484 TYR F 486 5 3 HELIX 38 AE2 GLY B 516 GLY B 524 1 9 HELIX 39 AE3 THR B 529 LEU B 537 1 9 HELIX 40 AE4 THR B 538 ALA B 541 5 4 HELIX 41 AE5 GLY B 569 GLY B 597 1 29 HELIX 42 AE6 ASN B 611 SER B 615 5 5 HELIX 43 AE7 THR B 618 TRP B 623 1 6 HELIX 44 AE8 THR B 627 GLY B 636 1 10 HELIX 45 AE9 TYR B 638 THR B 662 1 25 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 PHE H 25 -1 O THR H 21 N SER H 7 SHEET 3 AA1 4 GLN H 77 VAL H 82 -1 O VAL H 82 N LEU H 18 SHEET 4 AA1 4 LEU H 67 LYS H 71 -1 N THR H 68 O LYS H 81 SHEET 1 AA2 6 MET H 11 VAL H 12 0 SHEET 2 AA2 6 VAL H 107 VAL H 111 1 O ILE H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 ASP H 100A-1 N TYR H 90 O VAL H 107 SHEET 4 AA2 6 SER H 34 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O LEU H 48 N TRP H 36 SHEET 6 AA2 6 THR H 58 TYR H 59 -1 O THR H 58 N GLY H 50 SHEET 1 AA3 4 MET H 11 VAL H 12 0 SHEET 2 AA3 4 VAL H 107 VAL H 111 1 O ILE H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 ASP H 100A-1 N TYR H 90 O VAL H 107 SHEET 4 AA3 4 VAL H 100F TRP H 103 -1 O VAL H 100K N LYS H 96 SHEET 1 AA4 4 THR L 5 THR L 7 0 SHEET 2 AA4 4 ALA L 19 ARG L 24 -1 O SER L 22 N THR L 7 SHEET 3 AA4 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA4 4 PHE L 62 GLY L 66 -1 N SER L 65 O THR L 72 SHEET 1 AA5 6 SER L 10 PRO L 12 0 SHEET 2 AA5 6 LYS L 103 GLU L 105 1 O LYS L 103 N LEU L 11 SHEET 3 AA5 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA5 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA5 6 GLN L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA5 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA6 4 SER L 10 PRO L 12 0 SHEET 2 AA6 4 LYS L 103 GLU L 105 1 O LYS L 103 N LEU L 11 SHEET 3 AA6 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA6 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AA7 3 GLY G 495 THR G 499 0 SHEET 2 AA7 3 TRP G 35 TYR G 39 -1 N THR G 37 O ALA G 497 SHEET 3 AA7 3 ILE C 603 PRO C 609 -1 O VAL C 608 N VAL G 36 SHEET 1 AA8 4 TRP G 45 GLU G 47 0 SHEET 2 AA8 4 VAL G 488 VAL G 491 -1 O GLU G 490 N ARG G 46 SHEET 3 AA8 4 TYR G 223 CYS G 228 -1 N ALA G 224 O VAL G 489 SHEET 4 AA8 4 VAL G 242 VAL G 245 -1 O SER G 243 N LYS G 227 SHEET 1 AA9 3 VAL G 75 PRO G 76 0 SHEET 2 AA9 3 PHE G 53 SER G 56 1 N SER G 56 O VAL G 75 SHEET 3 AA9 3 HIS G 216 CYS G 218 -1 O HIS G 216 N ALA G 55 SHEET 1 AB1 2 GLU G 91 ASN G 94 0 SHEET 2 AB1 2 THR G 236 CYS G 239 -1 O CYS G 239 N GLU G 91 SHEET 1 AB2 3 ASN G 130 SER G 132 0 SHEET 2 AB2 3 ILE G 154 PHE G 159 -1 O SER G 158 N ASN G 130 SHEET 3 AB2 3 GLU G 172 TYR G 177 -1 O ALA G 174 N CYS G 157 SHEET 1 AB3 2 ILE G 181 VAL G 182 0 SHEET 2 AB3 2 ARG G 192 LEU G 193 -1 O ARG G 192 N VAL G 182 SHEET 1 AB4 3 VAL G 200 GLN G 203 0 SHEET 2 AB4 3 ARG G 432 TYR G 435 1 O TYR G 435 N THR G 202 SHEET 3 AB4 3 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AB5 4 LEU G 259 LEU G 261 0 SHEET 2 AB5 4 ILE G 443 LEU G 452 -1 O THR G 450 N LEU G 260 SHEET 3 AB5 4 ILE G 284 ARG G 298 -1 N VAL G 292 O ILE G 449 SHEET 4 AB5 4 ILE G 272 SER G 274 -1 N ARG G 273 O ILE G 285 SHEET 1 AB6 5 LEU G 259 LEU G 261 0 SHEET 2 AB6 5 ILE G 443 LEU G 452 -1 O THR G 450 N LEU G 260 SHEET 3 AB6 5 ILE G 284 ARG G 298 -1 N VAL G 292 O ILE G 449 SHEET 4 AB6 5 HIS G 330 SER G 334 -1 O HIS G 330 N THR G 297 SHEET 5 AB6 5 THR G 408 THR G 415 -1 O ILE G 414 N ILE G 333 SHEET 1 AB7 2 ASN G 301 ARG G 308 0 SHEET 2 AB7 2 THR G 316 ILE G 323 -1 O ALA G 319 N LYS G 305 SHEET 1 AB8 3 ILE G 359 PHE G 361 0 SHEET 2 AB8 3 GLU G 466 PRO G 470 1 O PHE G 468 N ILE G 360 SHEET 3 AB8 3 LEU G 454 ARG G 456 -1 N THR G 455 O ARG G 469 SHEET 1 AB9 2 PHE G 383 CYS G 385 0 SHEET 2 AB9 2 CYS G 418 ILE G 420 -1 O ARG G 419 N TYR G 384 SHEET 1 AC1 3 LEU D 494 THR D 499 0 SHEET 2 AC1 3 TRP D 35 TYR D 40 -1 N TRP D 35 O THR D 499 SHEET 3 AC1 3 ILE E 603 PRO E 609 -1 O VAL E 608 N VAL D 36 SHEET 1 AC2 4 TRP D 45 GLU D 47 0 SHEET 2 AC2 4 TYR D 486 VAL D 491 -1 O GLU D 490 N ARG D 46 SHEET 3 AC2 4 ALA D 224 CYS D 228 -1 N ALA D 224 O VAL D 489 SHEET 4 AC2 4 VAL D 242 VAL D 245 -1 O SER D 243 N LYS D 227 SHEET 1 AC3 2 PHE D 53 ALA D 55 0 SHEET 2 AC3 2 HIS D 216 CYS D 218 -1 O HIS D 216 N ALA D 55 SHEET 1 AC4 2 GLU D 91 ASN D 92 0 SHEET 2 AC4 2 PRO D 238 CYS D 239 -1 O CYS D 239 N GLU D 91 SHEET 1 AC5 3 LEU D 129 ASN D 130 0 SHEET 2 AC5 3 GLU D 190 LEU D 193 -1 O TYR D 191 N LEU D 129 SHEET 3 AC5 3 ILE D 181 PRO D 183 -1 N VAL D 182 O ARG D 192 SHEET 1 AC6 2 ILE D 154 THR D 162 0 SHEET 2 AC6 2 LYS D 169 TYR D 177 -1 O ALA D 174 N CYS D 157 SHEET 1 AC7 3 THR D 202 GLN D 203 0 SHEET 2 AC7 3 MET D 434 TYR D 435 1 O TYR D 435 N THR D 202 SHEET 3 AC7 3 ILE D 423 ILE D 424 -1 N ILE D 424 O MET D 434 SHEET 1 AC8 5 ILE D 271 ARG D 273 0 SHEET 2 AC8 5 ILE D 284 HIS D 287 -1 O ILE D 285 N ARG D 273 SHEET 3 AC8 5 LEU D 453 ARG D 456 -1 O LEU D 454 N ILE D 284 SHEET 4 AC8 5 GLU D 466 PRO D 470 -1 O ARG D 469 N THR D 455 SHEET 5 AC8 5 ILE D 359 PHE D 361 1 N ILE D 360 O GLU D 466 SHEET 1 AC9 4 ILE D 414 THR D 415 0 SHEET 2 AC9 4 HIS D 330 ILE D 333 -1 N ILE D 333 O ILE D 414 SHEET 3 AC9 4 VAL D 292 ARG D 298 -1 N THR D 295 O ASN D 332 SHEET 4 AC9 4 ILE D 443 ILE D 449 -1 O SER D 447 N ILE D 294 SHEET 1 AD1 2 ARG D 304 ARG D 308 0 SHEET 2 AD1 2 THR D 316 LEU D 320 -1 O ALA D 319 N LYS D 305 SHEET 1 AD2 3 HIS D 374 ASN D 377 0 SHEET 2 AD2 3 PHE D 382 CYS D 385 -1 O CYS D 385 N HIS D 374 SHEET 3 AD2 3 CYS D 418 ILE D 420 -1 O ARG D 419 N TYR D 384 SHEET 1 AD3 3 ILE F 496 THR F 499 0 SHEET 2 AD3 3 TRP F 35 TYR F 39 -1 N TRP F 35 O THR F 499 SHEET 3 AD3 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL F 38 SHEET 1 AD4 4 TRP F 45 GLU F 47 0 SHEET 2 AD4 4 VAL F 488 VAL F 491 -1 O GLU F 490 N ARG F 46 SHEET 3 AD4 4 TYR F 223 CYS F 228 -1 N ALA F 224 O VAL F 489 SHEET 4 AD4 4 VAL F 242 VAL F 245 -1 O VAL F 245 N ILE F 225 SHEET 1 AD5 2 ASN F 92 ASN F 94 0 SHEET 2 AD5 2 THR F 236 PRO F 238 -1 O GLY F 237 N PHE F 93 SHEET 1 AD6 5 LYS F 169 TYR F 177 0 SHEET 2 AD6 5 ILE F 154 THR F 162 -1 N LYS F 155 O PHE F 176 SHEET 3 AD6 5 LEU F 129 ASP F 133 -1 N SER F 132 O ASN F 156 SHEET 4 AD6 5 GLU F 190 LEU F 193 -1 O TYR F 191 N LEU F 129 SHEET 5 AD6 5 ILE F 181 PRO F 183 -1 N VAL F 182 O ARG F 192 SHEET 1 AD7 3 ILE F 201 GLN F 203 0 SHEET 2 AD7 3 ALA F 433 TYR F 435 1 O ALA F 433 N THR F 202 SHEET 3 AD7 3 ILE F 423 ILE F 424 -1 N ILE F 424 O MET F 434 SHEET 1 AD8 5 LEU F 259 LEU F 261 0 SHEET 2 AD8 5 LYS F 446 ARG F 456 -1 O THR F 450 N LEU F 260 SHEET 3 AD8 5 THR F 283 THR F 297 -1 N LEU F 288 O THR F 450 SHEET 4 AD8 5 GLU F 466 PRO F 470 0 SHEET 5 AD8 5 ILE F 359 PHE F 361 1 N ILE F 360 O PHE F 468 SHEET 1 AD9 7 ILE F 271 ARG F 273 0 SHEET 2 AD9 7 THR F 283 THR F 297 -1 O ILE F 285 N ARG F 273 SHEET 3 AD9 7 LYS F 446 ARG F 456 -1 O THR F 450 N LEU F 288 SHEET 4 AD9 7 HIS F 330 ILE F 333 0 SHEET 5 AD9 7 ILE F 414 ARG F 419 -1 O ILE F 414 N ILE F 333 SHEET 6 AD9 7 GLU F 381 CYS F 385 -1 N TYR F 384 O ARG F 419 SHEET 7 AD9 7 HIS F 374 CYS F 378 -1 N HIS F 374 O CYS F 385 SHEET 1 AE1 2 MET F 302 VAL F 307 0 SHEET 2 AE1 2 PHE F 317 ILE F 322 -1 O ALA F 319 N LYS F 305 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 3 CYS G 54 CYS G 74 1555 1555 2.04 SSBOND 4 CYS G 119 CYS G 205 1555 1555 2.03 SSBOND 5 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 6 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 7 CYS G 218 CYS G 247 1555 1555 2.03 SSBOND 8 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 9 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 10 CYS G 385 CYS G 418 1555 1555 2.04 SSBOND 11 CYS G 501 CYS C 605 1555 1555 2.04 SSBOND 12 CYS C 598 CYS C 604 1555 1555 2.03 SSBOND 13 CYS D 54 CYS D 74 1555 1555 2.03 SSBOND 14 CYS D 119 CYS D 205 1555 1555 2.03 SSBOND 15 CYS D 126 CYS D 196 1555 1555 2.03 SSBOND 16 CYS D 131 CYS D 157 1555 1555 2.03 SSBOND 17 CYS D 218 CYS D 247 1555 1555 2.03 SSBOND 18 CYS D 228 CYS D 239 1555 1555 2.03 SSBOND 19 CYS D 296 CYS D 331 1555 1555 2.04 SSBOND 20 CYS D 378 CYS D 445 1555 1555 2.03 SSBOND 21 CYS D 385 CYS D 418 1555 1555 2.03 SSBOND 22 CYS D 501 CYS E 605 1555 1555 2.04 SSBOND 23 CYS E 598 CYS E 604 1555 1555 2.03 SSBOND 24 CYS F 54 CYS F 74 1555 1555 2.05 SSBOND 25 CYS F 119 CYS F 205 1555 1555 2.03 SSBOND 26 CYS F 126 CYS F 196 1555 1555 2.03 SSBOND 27 CYS F 131 CYS F 157 1555 1555 2.03 SSBOND 28 CYS F 218 CYS F 247 1555 1555 2.03 SSBOND 29 CYS F 228 CYS F 239 1555 1555 2.03 SSBOND 30 CYS F 296 CYS F 331 1555 1555 2.03 SSBOND 31 CYS F 378 CYS F 445 1555 1555 2.03 SSBOND 32 CYS F 385 CYS F 418 1555 1555 2.03 SSBOND 33 CYS F 501 CYS B 605 1555 1555 2.03 SSBOND 34 CYS B 598 CYS B 604 1555 1555 2.03 LINK C ASP H 100B N TYS H 100C 1555 1555 1.33 LINK C TYS H 100C N TYR H 100D 1555 1555 1.33 LINK ND2 ASN G 88 C1 NAG G 611 1555 1555 1.44 LINK ND2 ASN G 130 C1 NAG G 616 1555 1555 1.44 LINK ND2 ASN G 156 C1 NAG G 601 1555 1555 1.44 LINK ND2 ASN G 160 C1 NAG K 1 1555 1555 1.45 LINK ND2 ASN G 197 C1 NAG A 1 1555 1555 1.45 LINK ND2 ASN G 230 C1 NAG G 613 1555 1555 1.44 LINK ND2 ASN G 234 C1 NAG G 614 1555 1555 1.44 LINK ND2 ASN G 241 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG J 1 1555 1555 1.45 LINK ND2 ASN G 276 C1 NAG G 602 1555 1555 1.44 LINK ND2 ASN G 289 C1 NAG G 609 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG G 603 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG G 610 1555 1555 1.44 LINK ND2 ASN G 356 C1 NAG G 604 1555 1555 1.44 LINK ND2 ASN G 362 C1 NAG G 605 1555 1555 1.44 LINK ND2 ASN G 386 C1 NAG G 606 1555 1555 1.44 LINK ND2 ASN G 393 C1 NAG G 615 1555 1555 1.44 LINK ND2 ASN G 442 C1 NAG G 607 1555 1555 1.44 LINK ND2 ASN G 448 C1 NAG G 608 1555 1555 1.44 LINK ND2 ASN G 502 C1 NAG G 612 1555 1555 1.44 LINK ND2 ASN C 611 C1 NAG C 702 1555 1555 1.44 LINK ND2 ASN C 637 C1 NAG C 701 1555 1555 1.44 LINK ND2 ASN D 88 C1 NAG D 611 1555 1555 1.44 LINK ND2 ASN D 130 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN D 156 C1 NAG D 601 1555 1555 1.44 LINK ND2 ASN D 160 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN D 197 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN D 230 C1 NAG D 613 1555 1555 1.45 LINK ND2 ASN D 234 C1 NAG D 614 1555 1555 1.44 LINK ND2 ASN D 241 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN D 262 C1 NAG Q 1 1555 1555 1.45 LINK ND2 ASN D 276 C1 NAG D 602 1555 1555 1.44 LINK ND2 ASN D 289 C1 NAG D 609 1555 1555 1.45 LINK ND2 ASN D 301 C1 NAG D 603 1555 1555 1.44 LINK ND2 ASN D 332 C1 NAG D 610 1555 1555 1.44 LINK ND2 ASN D 356 C1 NAG D 604 1555 1555 1.44 LINK ND2 ASN D 362 C1 NAG D 605 1555 1555 1.44 LINK ND2 ASN D 386 C1 NAG D 606 1555 1555 1.44 LINK ND2 ASN D 393 C1 NAG D 615 1555 1555 1.44 LINK ND2 ASN D 442 C1 NAG D 607 1555 1555 1.44 LINK ND2 ASN D 448 C1 NAG D 608 1555 1555 1.44 LINK ND2 ASN D 502 C1 NAG D 612 1555 1555 1.44 LINK ND2 ASN E 611 C1 NAG E 702 1555 1555 1.44 LINK ND2 ASN E 616 C1 NAG E 703 1555 1555 1.45 LINK ND2 ASN E 625 C1 NAG E 704 1555 1555 1.44 LINK ND2 ASN E 637 C1 NAG E 701 1555 1555 1.44 LINK ND2 ASN F 88 C1 NAG F 610 1555 1555 1.44 LINK ND2 ASN F 130 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN F 156 C1 NAG F 601 1555 1555 1.44 LINK ND2 ASN F 160 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN F 197 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN F 230 C1 NAG F 612 1555 1555 1.44 LINK ND2 ASN F 234 C1 NAG F 613 1555 1555 1.44 LINK ND2 ASN F 241 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN F 262 C1 NAG T 1 1555 1555 1.45 LINK ND2 ASN F 276 C1 NAG F 602 1555 1555 1.44 LINK ND2 ASN F 289 C1 NAG F 608 1555 1555 1.44 LINK ND2 ASN F 301 C1 NAG F 603 1555 1555 1.44 LINK ND2 ASN F 332 C1 NAG F 609 1555 1555 1.44 LINK ND2 ASN F 356 C1 NAG F 604 1555 1555 1.44 LINK ND2 ASN F 362 C1 NAG F 615 1555 1555 1.44 LINK ND2 ASN F 386 C1 NAG F 605 1555 1555 1.44 LINK ND2 ASN F 393 C1 NAG F 614 1555 1555 1.44 LINK ND2 ASN F 442 C1 NAG F 606 1555 1555 1.44 LINK ND2 ASN F 448 C1 NAG F 607 1555 1555 1.44 LINK ND2 ASN F 502 C1 NAG F 611 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG B 702 1555 1555 1.45 LINK ND2 ASN B 616 C1 NAG B 703 1555 1555 1.44 LINK ND2 ASN B 625 C1 NAG B 704 1555 1555 1.46 LINK ND2 ASN B 637 C1 NAG B 701 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 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 1.46 LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.46 LINK O6 BMA J 3 C1 MAN J 5 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.46 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.45 LINK O6 BMA K 3 C1 MAN K 4 1555 1555 1.46 LINK O3 BMA K 3 C1 MAN K 6 1555 1555 1.46 LINK O6 MAN K 4 C1 MAN K 5 1555 1555 1.45 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 O6 BMA M 3 C1 MAN M 4 1555 1555 1.44 LINK O3 BMA M 3 C1 MAN M 8 1555 1555 1.46 LINK O6 MAN M 4 C1 MAN M 5 1555 1555 1.45 LINK O3 MAN M 4 C1 MAN M 7 1555 1555 1.45 LINK O2 MAN M 5 C1 MAN M 6 1555 1555 1.44 LINK O2 MAN M 8 C1 MAN M 9 1555 1555 1.47 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 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 Q 2 C1 BMA Q 3 1555 1555 1.46 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.46 LINK O6 BMA Q 3 C1 MAN Q 5 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.46 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 1.46 LINK O3 BMA T 3 C1 MAN T 4 1555 1555 1.46 LINK O6 BMA T 3 C1 MAN T 5 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 O6 BMA U 3 C1 MAN U 4 1555 1555 1.45 LINK O3 MAN U 4 C1 MAN U 5 1555 1555 1.44 LINK O6 MAN U 4 C1 MAN U 7 1555 1555 1.45 LINK O2 MAN U 5 C1 MAN U 6 1555 1555 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 CISPEP 1 THR L 7 PRO L 8 0 -2.22 CISPEP 2 PRO L 94 PRO L 95 0 -4.91 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