HEADER VIRAL PROTEIN/IMMUNE SYSTEM 15-MAY-24 9BTI TITLE RHESUS FAB 40591-A.01 IN COMPLEX WITH T250.4 RNS SOSIP ENV COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 3 CHAIN: B, A, F; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 8 CHAIN: G, C, H; COMPND 9 SYNONYM: ENV POLYPROTEIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: FAB 40591-A.01 HEAVY CHAIN; COMPND 13 CHAIN: D; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: FAB 40591-A.01 LIGHT CHAIN; COMPND 17 CHAIN: E; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11676; SOURCE 10 GENE: ENV; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 15 ORGANISM_TAXID: 9544; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 20 ORGANISM_TAXID: 9544; 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 9BTI 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. 4.14 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) : 4.140 REMARK 3 NUMBER OF PARTICLES : 66103 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 9BTI 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_1000283891. 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 40591-A.01 IN REMARK 245 COMPLEX WITH T250.4 RNS SOSIP REMARK 245 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: B, G, D, E, A, C, F, H, I, J, REMARK 350 AND CHAINS: K, L, 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 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 B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 LEU B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 VAL B 518 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 LYS 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 ASP B 664 REMARK 465 GLY G 29 REMARK 465 PRO G 30 REMARK 465 LYS G 59 REMARK 465 GLY G 60 REMARK 465 TYR G 61 REMARK 465 ASP G 62 REMARK 465 HIS G 144 REMARK 465 THR G 145 REMARK 465 ASN G 146 REMARK 465 SER G 147 REMARK 465 SER G 148 REMARK 465 ILE G 149 REMARK 465 ASN G 356 REMARK 465 THR G 357 REMARK 465 THR G 395A REMARK 465 ASN G 395B REMARK 465 SER G 395C REMARK 465 THR G 395D REMARK 465 TRP G 395E REMARK 465 THR G 395F REMARK 465 ASN G 395G REMARK 465 SER G 395H REMARK 465 THR G 395I REMARK 465 THR G 395J REMARK 465 GLY G 395K REMARK 465 SER G 395L REMARK 465 ASN G 395M REMARK 465 GLY G 395N REMARK 465 THR G 395O REMARK 465 GLU G 395P REMARK 465 SER G 395Q REMARK 465 ASN G 395R REMARK 465 GLY G 460 REMARK 465 ASN G 461 REMARK 465 SER G 462 REMARK 465 THR G 463 REMARK 465 GLN G 464 REMARK 465 VAL G 505 REMARK 465 VAL G 506 REMARK 465 GLU 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 SER D 113 REMARK 465 ALA D 114 REMARK 465 SER D 115 REMARK 465 THR D 116 REMARK 465 LYS D 117 REMARK 465 GLY D 118 REMARK 465 PRO D 119 REMARK 465 SER D 120 REMARK 465 VAL D 121 REMARK 465 PHE D 122 REMARK 465 PRO D 123 REMARK 465 LEU D 124 REMARK 465 ALA D 125 REMARK 465 PRO D 126 REMARK 465 SER D 127 REMARK 465 SER D 128 REMARK 465 LYS D 129 REMARK 465 SER D 130 REMARK 465 THR D 131 REMARK 465 SER D 132 REMARK 465 GLY D 133 REMARK 465 GLY D 134 REMARK 465 THR D 135 REMARK 465 ALA D 136 REMARK 465 ALA D 137 REMARK 465 LEU D 138 REMARK 465 GLY D 139 REMARK 465 CYS D 140 REMARK 465 LEU D 141 REMARK 465 VAL D 142 REMARK 465 LYS D 143 REMARK 465 ASP D 144 REMARK 465 TYR D 145 REMARK 465 PHE D 146 REMARK 465 PRO D 147 REMARK 465 GLU D 148 REMARK 465 PRO D 149 REMARK 465 VAL D 150 REMARK 465 THR D 151 REMARK 465 VAL D 152 REMARK 465 SER D 153 REMARK 465 TRP D 154 REMARK 465 ASN D 155 REMARK 465 SER D 156 REMARK 465 GLY D 157 REMARK 465 ALA D 158 REMARK 465 LEU D 159 REMARK 465 THR D 160 REMARK 465 SER D 161 REMARK 465 GLY D 162 REMARK 465 VAL D 163 REMARK 465 HIS D 164 REMARK 465 THR D 165 REMARK 465 PHE D 166 REMARK 465 PRO D 167 REMARK 465 ALA D 168 REMARK 465 VAL D 169 REMARK 465 LEU D 170 REMARK 465 GLN D 171 REMARK 465 SER D 172 REMARK 465 SER D 173 REMARK 465 GLY D 174 REMARK 465 LEU D 175 REMARK 465 TYR D 176 REMARK 465 SER D 177 REMARK 465 LEU D 178 REMARK 465 SER D 179 REMARK 465 SER D 180 REMARK 465 VAL D 181 REMARK 465 VAL D 182 REMARK 465 THR D 183 REMARK 465 VAL D 184 REMARK 465 PRO D 185 REMARK 465 SER D 186 REMARK 465 SER D 187 REMARK 465 SER D 188 REMARK 465 LEU D 189 REMARK 465 GLY D 190 REMARK 465 THR D 191 REMARK 465 GLN D 192 REMARK 465 THR D 193 REMARK 465 TYR D 194 REMARK 465 ILE D 195 REMARK 465 CYS D 196 REMARK 465 ASN D 197 REMARK 465 VAL D 198 REMARK 465 ASN D 199 REMARK 465 HIS D 200 REMARK 465 LYS D 201 REMARK 465 PRO D 202 REMARK 465 SER D 203 REMARK 465 ASN D 204 REMARK 465 THR D 205 REMARK 465 LYS D 206 REMARK 465 VAL D 207 REMARK 465 ASP D 208 REMARK 465 LYS D 209 REMARK 465 LYS D 210 REMARK 465 VAL D 211 REMARK 465 GLU D 212 REMARK 465 PRO D 213 REMARK 465 LYS D 214 REMARK 465 SER D 215 REMARK 465 CYS D 216 REMARK 465 ASP D 217 REMARK 465 LYS D 218 REMARK 465 GLY D 219 REMARK 465 LEU D 220 REMARK 465 GLU D 221 REMARK 465 VAL D 222 REMARK 465 LEU D 223 REMARK 465 PHE D 224 REMARK 465 GLN D 225 REMARK 465 ARG E 108 REMARK 465 THR E 109 REMARK 465 VAL E 110 REMARK 465 ALA E 111 REMARK 465 ALA E 112 REMARK 465 PRO E 113 REMARK 465 SER E 114 REMARK 465 VAL E 115 REMARK 465 PHE E 116 REMARK 465 ILE E 117 REMARK 465 PHE E 118 REMARK 465 PRO E 119 REMARK 465 PRO E 120 REMARK 465 SER E 121 REMARK 465 ASP E 122 REMARK 465 GLU E 123 REMARK 465 GLN E 124 REMARK 465 LEU E 125 REMARK 465 LYS E 126 REMARK 465 SER E 127 REMARK 465 GLY E 128 REMARK 465 THR E 129 REMARK 465 ALA E 130 REMARK 465 SER E 131 REMARK 465 VAL E 132 REMARK 465 VAL E 133 REMARK 465 CYS E 134 REMARK 465 LEU E 135 REMARK 465 LEU E 136 REMARK 465 ASN E 137 REMARK 465 ASN E 138 REMARK 465 PHE E 139 REMARK 465 TYR E 140 REMARK 465 PRO E 141 REMARK 465 ARG E 142 REMARK 465 GLU E 143 REMARK 465 ALA E 144 REMARK 465 LYS E 145 REMARK 465 VAL E 146 REMARK 465 GLN E 147 REMARK 465 TRP E 148 REMARK 465 LYS E 149 REMARK 465 VAL E 150 REMARK 465 ASP E 151 REMARK 465 ASN E 152 REMARK 465 ALA E 153 REMARK 465 LEU E 154 REMARK 465 GLN E 155 REMARK 465 SER E 156 REMARK 465 GLY E 157 REMARK 465 ASN E 158 REMARK 465 SER E 159 REMARK 465 GLN E 160 REMARK 465 GLU E 161 REMARK 465 SER E 162 REMARK 465 VAL E 163 REMARK 465 THR E 164 REMARK 465 GLU E 165 REMARK 465 GLN E 166 REMARK 465 ASP E 167 REMARK 465 SER E 168 REMARK 465 LYS E 169 REMARK 465 ASP E 170 REMARK 465 SER E 171 REMARK 465 THR E 172 REMARK 465 TYR E 173 REMARK 465 SER E 174 REMARK 465 LEU E 175 REMARK 465 SER E 176 REMARK 465 SER E 177 REMARK 465 THR E 178 REMARK 465 LEU E 179 REMARK 465 THR E 180 REMARK 465 LEU E 181 REMARK 465 SER E 182 REMARK 465 LYS E 183 REMARK 465 ALA E 184 REMARK 465 ASP E 185 REMARK 465 TYR E 186 REMARK 465 GLU E 187 REMARK 465 LYS E 188 REMARK 465 HIS E 189 REMARK 465 LYS E 190 REMARK 465 VAL E 191 REMARK 465 TYR E 192 REMARK 465 ALA E 193 REMARK 465 CYS E 194 REMARK 465 GLU E 195 REMARK 465 VAL E 196 REMARK 465 THR E 197 REMARK 465 HIS E 198 REMARK 465 GLN E 199 REMARK 465 GLY E 200 REMARK 465 LEU E 201 REMARK 465 SER E 202 REMARK 465 SER E 203 REMARK 465 PRO E 204 REMARK 465 VAL E 205 REMARK 465 THR E 206 REMARK 465 LYS E 207 REMARK 465 SER E 208 REMARK 465 PHE E 209 REMARK 465 ASN E 210 REMARK 465 ARG E 211 REMARK 465 GLY E 212 REMARK 465 GLU E 213 REMARK 465 CYS E 214 REMARK 465 ALA A 512 REMARK 465 VAL A 513 REMARK 465 GLY A 514 REMARK 465 LEU A 515 REMARK 465 GLY A 516 REMARK 465 ALA A 517 REMARK 465 VAL A 518 REMARK 465 LEU A 544 REMARK 465 LEU A 545 REMARK 465 SER A 546 REMARK 465 GLY A 547 REMARK 465 ILE A 548 REMARK 465 VAL A 549 REMARK 465 GLN A 550 REMARK 465 GLN A 551 REMARK 465 GLN A 552 REMARK 465 SER A 553 REMARK 465 ASN A 554 REMARK 465 LEU A 555 REMARK 465 LEU A 556 REMARK 465 LYS A 557 REMARK 465 ALA A 558 REMARK 465 PRO A 559 REMARK 465 GLU A 560 REMARK 465 ALA A 561 REMARK 465 GLN A 562 REMARK 465 ASP A 664 REMARK 465 GLY C 29 REMARK 465 PRO C 30 REMARK 465 LYS C 59 REMARK 465 GLY C 60 REMARK 465 TYR C 61 REMARK 465 ASP C 62 REMARK 465 HIS C 144 REMARK 465 THR C 145 REMARK 465 ASN C 146 REMARK 465 SER C 147 REMARK 465 SER C 148 REMARK 465 ILE C 149 REMARK 465 ASN C 356 REMARK 465 THR C 357 REMARK 465 THR C 395A REMARK 465 ASN C 395B REMARK 465 SER C 395C REMARK 465 THR C 395D REMARK 465 TRP C 395E REMARK 465 THR C 395F REMARK 465 ASN C 395G REMARK 465 SER C 395H REMARK 465 THR C 395I REMARK 465 THR C 395J REMARK 465 GLY C 395K REMARK 465 SER C 395L REMARK 465 ASN C 395M REMARK 465 GLY C 395N REMARK 465 THR C 395O REMARK 465 GLU C 395P REMARK 465 SER C 395Q REMARK 465 ASN C 395R REMARK 465 GLY C 460 REMARK 465 ASN C 461 REMARK 465 SER C 462 REMARK 465 THR C 463 REMARK 465 GLN C 464 REMARK 465 VAL C 505 REMARK 465 VAL C 506 REMARK 465 GLU C 507 REMARK 465 ARG C 508 REMARK 465 ARG C 509 REMARK 465 ARG C 510 REMARK 465 ARG C 511 REMARK 465 ARG C 512 REMARK 465 ARG C 513 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 LEU F 544 REMARK 465 LEU F 545 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 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 LYS F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 ASP F 664 REMARK 465 GLY H 29 REMARK 465 PRO H 30 REMARK 465 LYS H 59 REMARK 465 GLY H 60 REMARK 465 TYR H 61 REMARK 465 ASP H 62 REMARK 465 SER H 143 REMARK 465 HIS H 144 REMARK 465 THR H 145 REMARK 465 ASN H 146 REMARK 465 SER H 147 REMARK 465 SER H 148 REMARK 465 ILE H 149 REMARK 465 ASN H 356 REMARK 465 THR H 357 REMARK 465 THR H 395A REMARK 465 ASN H 395B REMARK 465 SER H 395C REMARK 465 THR H 395D REMARK 465 TRP H 395E REMARK 465 THR H 395F REMARK 465 ASN H 395G REMARK 465 SER H 395H REMARK 465 THR H 395I REMARK 465 THR H 395J REMARK 465 GLY H 395K REMARK 465 SER H 395L REMARK 465 ASN H 395M REMARK 465 GLY H 395N REMARK 465 THR H 395O REMARK 465 GLU H 395P REMARK 465 SER H 395Q REMARK 465 ASN H 395R REMARK 465 GLY H 460 REMARK 465 ASN H 461 REMARK 465 SER H 462 REMARK 465 THR H 463 REMARK 465 GLN H 464 REMARK 465 VAL H 505 REMARK 465 VAL H 506 REMARK 465 GLU H 507 REMARK 465 ARG H 508 REMARK 465 ARG H 509 REMARK 465 ARG H 510 REMARK 465 ARG H 511 REMARK 465 ARG H 512 REMARK 465 ARG H 513 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 OG1 THR H 373 O CYS H 385 2.09 REMARK 500 OG1 THR A 606 O VAL C 36 2.11 REMARK 500 OG1 THR C 297 O ILE C 443 2.16 REMARK 500 OG SER G 256 O LEU G 259 2.18 REMARK 500 REMARK 500 REMARK: NULL 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 CYS C 501 CA - CB - SG ANGL. DEV. = 7.7 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 VAL B 539 70.65 45.31 REMARK 500 ARG B 542 -162.18 52.75 REMARK 500 LEU B 565 149.84 67.29 REMARK 500 ALA G 65 -9.48 76.04 REMARK 500 HIS G 66 -79.32 44.15 REMARK 500 ALA G 70 -166.29 -79.02 REMARK 500 THR G 163 -167.81 -77.50 REMARK 500 LYS G 168 135.97 71.81 REMARK 500 SER G 199 117.43 -164.78 REMARK 500 PRO G 253 73.47 -69.81 REMARK 500 GLN G 258 -7.32 73.68 REMARK 500 LEU G 259 116.16 -160.77 REMARK 500 ASN G 262 19.68 58.86 REMARK 500 GLU G 269 75.32 59.49 REMARK 500 ARG G 336 -8.37 74.44 REMARK 500 CYS G 378 55.38 -92.57 REMARK 500 THR G 387 -6.15 75.49 REMARK 500 MET G 426 -3.44 73.62 REMARK 500 VAL D 48 -60.53 -101.54 REMARK 500 GLU D 100B 109.19 -47.78 REMARK 500 ASP D 100C -53.22 -123.19 REMARK 500 PHE D 100E -169.36 60.78 REMARK 500 ASP E 50 18.82 58.58 REMARK 500 SER E 51 -5.61 68.16 REMARK 500 SER E 52 -15.87 -140.17 REMARK 500 ALA A 526 -104.88 48.98 REMARK 500 THR A 538 -176.28 -172.28 REMARK 500 LEU A 565 156.70 68.35 REMARK 500 GLU C 32 31.32 -96.55 REMARK 500 ALA C 65 163.06 67.54 REMARK 500 ALA C 73 -10.25 75.79 REMARK 500 CYS C 74 -101.42 24.94 REMARK 500 ASN C 80 73.95 53.44 REMARK 500 ASN C 88 -1.88 69.65 REMARK 500 THR C 163 -166.58 -79.13 REMARK 500 PRO C 253 60.86 -68.70 REMARK 500 GLN C 258 -11.44 73.89 REMARK 500 GLU C 269 124.08 64.79 REMARK 500 ASN C 276 118.30 -161.29 REMARK 500 ARG C 336 -68.80 63.60 REMARK 500 PHE C 391 33.60 -98.71 REMARK 500 MET C 426 -7.33 74.97 REMARK 500 PHE F 519 -100.98 65.30 REMARK 500 LEU F 523 161.30 67.41 REMARK 500 LEU F 565 151.33 67.52 REMARK 500 ILE F 622 -60.36 -120.08 REMARK 500 ALA H 65 -8.92 75.54 REMARK 500 HIS H 66 -92.28 29.37 REMARK 500 THR H 77 -99.67 55.23 REMARK 500 GLN H 82 -152.55 48.36 REMARK 500 REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 CYS C 418 ARG C 419 -148.10 REMARK 500 CYS C 501 LYS C 502 148.55 REMARK 500 CYS H 119 VAL H 120 -141.23 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG G 166 0.18 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44891 RELATED DB: EMDB REMARK 900 RHESUS FAB 40591-A.01 IN COMPLEX WITH T250.4 RNS SOSIP ENV DBREF1 9BTI B 512 664 UNP A0A8A0W558_9HIV1 DBREF2 9BTI B A0A8A0W558 504 656 DBREF1 9BTI G 31 511 UNP A0A8A0W558_9HIV1 DBREF2 9BTI G A0A8A0W558 29 503 DBREF 9BTI D 1 225 PDB 9BTI 9BTI 1 225 DBREF 9BTI E 1 214 PDB 9BTI 9BTI 1 214 DBREF1 9BTI A 512 664 UNP A0A8A0W558_9HIV1 DBREF2 9BTI A A0A8A0W558 504 656 DBREF1 9BTI C 31 511 UNP A0A8A0W558_9HIV1 DBREF2 9BTI C A0A8A0W558 29 503 DBREF1 9BTI F 512 664 UNP A0A8A0W558_9HIV1 DBREF2 9BTI F A0A8A0W558 504 656 DBREF1 9BTI H 31 511 UNP A0A8A0W558_9HIV1 DBREF2 9BTI H A0A8A0W558 29 503 SEQADV 9BTI ASN B 535 UNP A0A8A0W55 ILE 527 CONFLICT SEQADV 9BTI PRO B 559 UNP A0A8A0W55 ILE 551 CONFLICT SEQADV 9BTI GLY B 569 UNP A0A8A0W55 THR 561 CONFLICT SEQADV 9BTI PHE B 573 UNP A0A8A0W55 ILE 565 CONFLICT SEQADV 9BTI GLU B 588 UNP A0A8A0W55 LYS 580 CONFLICT SEQADV 9BTI VAL B 589 UNP A0A8A0W55 ASP 581 CONFLICT SEQADV 9BTI CYS B 605 UNP A0A8A0W55 THR 597 CONFLICT SEQADV 9BTI THR B 613 UNP A0A8A0W55 SER 605 CONFLICT SEQADV 9BTI GLY B 636 UNP A0A8A0W55 SER 628 CONFLICT SEQADV 9BTI GLU B 648 UNP A0A8A0W55 GLN 640 CONFLICT SEQADV 9BTI PHE B 651 UNP A0A8A0W55 ASN 643 CONFLICT SEQADV 9BTI ILE B 655 UNP A0A8A0W55 LYS 647 CONFLICT SEQADV 9BTI GLY G 29 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI PRO G 30 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI ASN G 33 UNP A0A8A0W55 LYS 31 CONFLICT SEQADV 9BTI ASN G 80 UNP A0A8A0W55 ARG 78 CONFLICT SEQADV 9BTI ILE G 84 UNP A0A8A0W55 MET 82 CONFLICT SEQADV 9BTI ASN G 99 UNP A0A8A0W55 SER 97 CONFLICT SEQADV 9BTI LEU G 175 UNP A0A8A0W55 PHE 168 CONFLICT SEQADV 9BTI LEU G 179 UNP A0A8A0W55 THR 172 CONFLICT SEQADV 9BTI VAL G 182 UNP A0A8A0W55 GLU 175 CONFLICT SEQADV 9BTI CYS G 201 UNP A0A8A0W55 ILE 194 CONFLICT SEQADV 9BTI ILE G 204 UNP A0A8A0W55 ALA 197 CONFLICT SEQADV 9BTI THR G 236 UNP A0A8A0W55 LYS 229 CONFLICT SEQADV 9BTI SER G 274 UNP A0A8A0W55 VAL 267 CONFLICT SEQADV 9BTI ILE G 277 UNP A0A8A0W55 THR 270 CONFLICT SEQADV 9BTI THR G 278 UNP A0A8A0W55 ILE 271 CONFLICT SEQADV 9BTI MET G 302 UNP A0A8A0W55 ASN 295 CONFLICT SEQADV 9BTI LEU G 320 UNP A0A8A0W55 THR 311 CONFLICT SEQADV 9BTI PRO G 329 UNP A0A8A0W55 ALA 321 CONFLICT SEQADV 9BTI ARG G 350 UNP A0A8A0W55 SER 342 CONFLICT SEQADV 9BTI THR G 358 UNP A0A8A0W55 LYS 349 CONFLICT SEQADV 9BTI SER G 364 UNP A0A8A0W55 HIS 355 CONFLICT SEQADV 9BTI THR G 372 UNP A0A8A0W55 ILE 363 CONFLICT SEQADV 9BTI ASN G 377 UNP A0A8A0W55 VAL 368 CONFLICT SEQADV 9BTI ARG G 419 UNP A0A8A0W55 GLU 412 CONFLICT SEQADV 9BTI ILE G 423 UNP A0A8A0W55 PHE 416 CONFLICT SEQADV 9BTI CYS G 433 UNP A0A8A0W55 ALA 426 CONFLICT SEQADV 9BTI ASN G 448 UNP A0A8A0W55 ASP 441 CONFLICT SEQADV 9BTI GLY G 460 UNP A0A8A0W55 PRO 452 CONFLICT SEQADV 9BTI CYS G 501 UNP A0A8A0W55 ALA 493 CONFLICT SEQADV 9BTI ARG G 509 UNP A0A8A0W55 GLU 501 CONFLICT SEQADV 9BTI ARG G 510 UNP A0A8A0W55 LYS 502 CONFLICT SEQADV 9BTI ARG G 512 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI ARG G 513 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI ASN A 535 UNP A0A8A0W55 ILE 527 CONFLICT SEQADV 9BTI PRO A 559 UNP A0A8A0W55 ILE 551 CONFLICT SEQADV 9BTI GLY A 569 UNP A0A8A0W55 THR 561 CONFLICT SEQADV 9BTI PHE A 573 UNP A0A8A0W55 ILE 565 CONFLICT SEQADV 9BTI GLU A 588 UNP A0A8A0W55 LYS 580 CONFLICT SEQADV 9BTI VAL A 589 UNP A0A8A0W55 ASP 581 CONFLICT SEQADV 9BTI CYS A 605 UNP A0A8A0W55 THR 597 CONFLICT SEQADV 9BTI THR A 613 UNP A0A8A0W55 SER 605 CONFLICT SEQADV 9BTI GLY A 636 UNP A0A8A0W55 SER 628 CONFLICT SEQADV 9BTI GLU A 648 UNP A0A8A0W55 GLN 640 CONFLICT SEQADV 9BTI PHE A 651 UNP A0A8A0W55 ASN 643 CONFLICT SEQADV 9BTI ILE A 655 UNP A0A8A0W55 LYS 647 CONFLICT SEQADV 9BTI GLY C 29 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI PRO C 30 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI ASN C 33 UNP A0A8A0W55 LYS 31 CONFLICT SEQADV 9BTI ASN C 80 UNP A0A8A0W55 ARG 78 CONFLICT SEQADV 9BTI ILE C 84 UNP A0A8A0W55 MET 82 CONFLICT SEQADV 9BTI ASN C 99 UNP A0A8A0W55 SER 97 CONFLICT SEQADV 9BTI LEU C 175 UNP A0A8A0W55 PHE 168 CONFLICT SEQADV 9BTI LEU C 179 UNP A0A8A0W55 THR 172 CONFLICT SEQADV 9BTI VAL C 182 UNP A0A8A0W55 GLU 175 CONFLICT SEQADV 9BTI CYS C 201 UNP A0A8A0W55 ILE 194 CONFLICT SEQADV 9BTI ILE C 204 UNP A0A8A0W55 ALA 197 CONFLICT SEQADV 9BTI THR C 236 UNP A0A8A0W55 LYS 229 CONFLICT SEQADV 9BTI SER C 274 UNP A0A8A0W55 VAL 267 CONFLICT SEQADV 9BTI ILE C 277 UNP A0A8A0W55 THR 270 CONFLICT SEQADV 9BTI THR C 278 UNP A0A8A0W55 ILE 271 CONFLICT SEQADV 9BTI MET C 302 UNP A0A8A0W55 ASN 295 CONFLICT SEQADV 9BTI LEU C 320 UNP A0A8A0W55 THR 311 CONFLICT SEQADV 9BTI PRO C 329 UNP A0A8A0W55 ALA 321 CONFLICT SEQADV 9BTI ARG C 350 UNP A0A8A0W55 SER 342 CONFLICT SEQADV 9BTI THR C 358 UNP A0A8A0W55 LYS 349 CONFLICT SEQADV 9BTI SER C 364 UNP A0A8A0W55 HIS 355 CONFLICT SEQADV 9BTI THR C 372 UNP A0A8A0W55 ILE 363 CONFLICT SEQADV 9BTI ASN C 377 UNP A0A8A0W55 VAL 368 CONFLICT SEQADV 9BTI ARG C 419 UNP A0A8A0W55 GLU 412 CONFLICT SEQADV 9BTI ILE C 423 UNP A0A8A0W55 PHE 416 CONFLICT SEQADV 9BTI CYS C 433 UNP A0A8A0W55 ALA 426 CONFLICT SEQADV 9BTI ASN C 448 UNP A0A8A0W55 ASP 441 CONFLICT SEQADV 9BTI GLY C 460 UNP A0A8A0W55 PRO 452 CONFLICT SEQADV 9BTI CYS C 501 UNP A0A8A0W55 ALA 493 CONFLICT SEQADV 9BTI ARG C 509 UNP A0A8A0W55 GLU 501 CONFLICT SEQADV 9BTI ARG C 510 UNP A0A8A0W55 LYS 502 CONFLICT SEQADV 9BTI ARG C 512 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI ARG C 513 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI ASN F 535 UNP A0A8A0W55 ILE 527 CONFLICT SEQADV 9BTI PRO F 559 UNP A0A8A0W55 ILE 551 CONFLICT SEQADV 9BTI GLY F 569 UNP A0A8A0W55 THR 561 CONFLICT SEQADV 9BTI PHE F 573 UNP A0A8A0W55 ILE 565 CONFLICT SEQADV 9BTI GLU F 588 UNP A0A8A0W55 LYS 580 CONFLICT SEQADV 9BTI VAL F 589 UNP A0A8A0W55 ASP 581 CONFLICT SEQADV 9BTI CYS F 605 UNP A0A8A0W55 THR 597 CONFLICT SEQADV 9BTI THR F 613 UNP A0A8A0W55 SER 605 CONFLICT SEQADV 9BTI GLY F 636 UNP A0A8A0W55 SER 628 CONFLICT SEQADV 9BTI GLU F 648 UNP A0A8A0W55 GLN 640 CONFLICT SEQADV 9BTI PHE F 651 UNP A0A8A0W55 ASN 643 CONFLICT SEQADV 9BTI ILE F 655 UNP A0A8A0W55 LYS 647 CONFLICT SEQADV 9BTI GLY H 29 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI PRO H 30 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI ASN H 33 UNP A0A8A0W55 LYS 31 CONFLICT SEQADV 9BTI ASN H 80 UNP A0A8A0W55 ARG 78 CONFLICT SEQADV 9BTI ILE H 84 UNP A0A8A0W55 MET 82 CONFLICT SEQADV 9BTI ASN H 99 UNP A0A8A0W55 SER 97 CONFLICT SEQADV 9BTI LEU H 175 UNP A0A8A0W55 PHE 168 CONFLICT SEQADV 9BTI LEU H 179 UNP A0A8A0W55 THR 172 CONFLICT SEQADV 9BTI VAL H 182 UNP A0A8A0W55 GLU 175 CONFLICT SEQADV 9BTI CYS H 201 UNP A0A8A0W55 ILE 194 CONFLICT SEQADV 9BTI ILE H 204 UNP A0A8A0W55 ALA 197 CONFLICT SEQADV 9BTI THR H 236 UNP A0A8A0W55 LYS 229 CONFLICT SEQADV 9BTI SER H 274 UNP A0A8A0W55 VAL 267 CONFLICT SEQADV 9BTI ILE H 277 UNP A0A8A0W55 THR 270 CONFLICT SEQADV 9BTI THR H 278 UNP A0A8A0W55 ILE 271 CONFLICT SEQADV 9BTI MET H 302 UNP A0A8A0W55 ASN 295 CONFLICT SEQADV 9BTI LEU H 320 UNP A0A8A0W55 THR 311 CONFLICT SEQADV 9BTI PRO H 329 UNP A0A8A0W55 ALA 321 CONFLICT SEQADV 9BTI ARG H 350 UNP A0A8A0W55 SER 342 CONFLICT SEQADV 9BTI THR H 358 UNP A0A8A0W55 LYS 349 CONFLICT SEQADV 9BTI SER H 364 UNP A0A8A0W55 HIS 355 CONFLICT SEQADV 9BTI THR H 372 UNP A0A8A0W55 ILE 363 CONFLICT SEQADV 9BTI ASN H 377 UNP A0A8A0W55 VAL 368 CONFLICT SEQADV 9BTI ARG H 419 UNP A0A8A0W55 GLU 412 CONFLICT SEQADV 9BTI ILE H 423 UNP A0A8A0W55 PHE 416 CONFLICT SEQADV 9BTI CYS H 433 UNP A0A8A0W55 ALA 426 CONFLICT SEQADV 9BTI ASN H 448 UNP A0A8A0W55 ASP 441 CONFLICT SEQADV 9BTI GLY H 460 UNP A0A8A0W55 PRO 452 CONFLICT SEQADV 9BTI CYS H 501 UNP A0A8A0W55 ALA 493 CONFLICT SEQADV 9BTI ARG H 509 UNP A0A8A0W55 GLU 501 CONFLICT SEQADV 9BTI ARG H 510 UNP A0A8A0W55 LYS 502 CONFLICT SEQADV 9BTI ARG H 512 UNP A0A8A0W55 EXPRESSION TAG SEQADV 9BTI ARG H 513 UNP A0A8A0W55 EXPRESSION TAG SEQRES 1 B 153 ALA VAL GLY LEU GLY ALA VAL PHE PHE GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ASN THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU LYS ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 GLN LEU LEU ARG LEU GLY VAL TRP GLY PHE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA LEU GLU ARG TYR LEU GLU VAL 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 THR VAL PRO TRP ASN SER THR TRP SER SEQRES 9 B 153 ASN LYS ASN TYR THR ASP ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP ARG GLU ILE GLY ASN TYR THR ASP GLU SEQRES 11 B 153 ILE TYR ARG LEU ILE GLU GLU SER GLN PHE GLN GLN GLU SEQRES 12 B 153 ILE ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 G 479 GLY PRO ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY SEQRES 2 G 479 VAL PRO VAL TRP ARG GLU ALA ASP THR THR LEU PHE CYS SEQRES 3 G 479 ALA SER ASP ALA LYS GLY TYR ASP THR GLU ALA HIS ASN SEQRES 4 G 479 VAL TRP ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN SEQRES 5 G 479 PRO GLN GLU ILE TYR LEU GLU ASN VAL THR GLU ASN PHE SEQRES 6 G 479 ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR SEQRES 7 G 479 ASP ILE ILE SER LEU TRP ASP GLU SER LEU LYS PRO CYS SEQRES 8 G 479 VAL LYS LEU THR PRO LEU CYS VAL THR LEU ASP CYS GLN SEQRES 9 G 479 ALA PHE ASN SER SER SER HIS THR ASN SER SER ILE ALA SEQRES 10 G 479 MET GLN GLU MET LYS ASN CYS SER PHE ASN VAL THR THR SEQRES 11 G 479 GLU LEU ARG ASP LYS LYS LYS LYS GLU TYR SER LEU PHE SEQRES 12 G 479 TYR LYS LEU ASP ILE VAL GLN ILE ASN LYS ASN GLY ARG SEQRES 13 G 479 GLN TYR ARG LEU ILE ASN CYS ASN THR SER ALA CYS THR SEQRES 14 G 479 GLN ILE CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE SEQRES 15 G 479 HIS PHE CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS SEQRES 16 G 479 ASN GLU LYS HIS PHE ASN GLY THR GLY PRO CYS LYS ASN SEQRES 17 G 479 VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL SEQRES 18 G 479 VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU SEQRES 19 G 479 GLU GLU VAL VAL ILE ARG SER GLU ASN ILE THR ASP ASN SEQRES 20 G 479 ALA LYS THR ILE ILE VAL GLN LEU ALA LYS PRO VAL LYS SEQRES 21 G 479 ILE ASN CYS THR ARG PRO ASN ASN MET THR ARG LYS SER SEQRES 22 G 479 ILE ARG ILE GLY PRO GLY GLN THR PHE TYR ALA LEU GLY SEQRES 23 G 479 ASP ILE ILE GLY ASN ILE ARG LYS PRO TYR CYS ASN VAL SEQRES 24 G 479 SER LYS ARG GLU TRP ASN ASN THR LEU GLN GLN VAL ALA SEQRES 25 G 479 ALA GLN LEU ARG LYS SER PHE ASN ASN THR THR ILE VAL SEQRES 26 G 479 PHE GLU LYS SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 27 G 479 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 28 G 479 THR SER GLY LEU PHE ASN SER THR TRP THR ASN SER THR SEQRES 29 G 479 TRP THR ASN SER THR THR GLY SER ASN GLY THR GLU SER SEQRES 30 G 479 ASN ASP THR ILE THR LEU GLN CYS ARG ILE LYS GLN ILE SEQRES 31 G 479 ILE ASN MET TRP GLN ARG VAL GLY ARG CYS MET TYR ALA SEQRES 32 G 479 PRO PRO ILE PRO GLY VAL ILE ARG CYS GLU SER ASN ILE SEQRES 33 G 479 THR GLY LEU LEU LEU THR ARG ASP GLY GLY ASN SER THR SEQRES 34 G 479 GLN ASN GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 G 479 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 G 479 GLN ILE GLU PRO LEU GLY VAL ALA PRO THR HIS CYS LYS SEQRES 37 G 479 ARG ARG VAL VAL GLU ARG ARG ARG ARG ARG ARG SEQRES 1 D 245 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 245 PRO GLY GLY SER LEU ARG LEU SER CYS THR PHE SER GLY SEQRES 3 D 245 ARG SER TYR HIS ASN TYR GLY MET ALA TRP VAL ARG GLN SEQRES 4 D 245 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5 D 245 SER GLY SER SER TYR THR ASP TYR ILE GLY SER VAL ARG SEQRES 6 D 245 GLY ARG PHE THR ILE SER ARG GLU ASN ALA MET ASN SER SEQRES 7 D 245 LEU SER LEU HIS MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 D 245 GLY VAL TYR PHE CYS ALA SER GLN GLY PRO ASP PRO TRP SEQRES 9 D 245 TYR GLU ASP ASP PHE GLY TYR HIS TYR GLU VAL LEU SER SEQRES 10 D 245 ASN ARG PHE ASP VAL TRP GLY PRO GLY VAL LEU VAL THR SEQRES 11 D 245 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 12 D 245 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 13 D 245 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 14 D 245 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 15 D 245 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 16 D 245 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 17 D 245 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 18 D 245 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 19 D 245 SER CYS ASP LYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 E 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 E 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 E 214 GLN THR VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 E 214 PRO GLY LYS ALA PRO LYS PHE LEU ILE TYR ASP SER SER SEQRES 5 E 214 THR LEU ALA THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 E 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 E 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN HIS SEQRES 8 E 214 TYR SER ARG PRO VAL THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 E 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 E 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 E 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 E 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 E 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 E 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 E 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 E 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 E 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 153 ALA VAL GLY LEU GLY ALA VAL PHE PHE GLY PHE LEU GLY SEQRES 2 A 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ASN THR LEU SEQRES 3 A 153 THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL GLN SEQRES 4 A 153 GLN GLN SER ASN LEU LEU LYS ALA PRO GLU ALA GLN GLN SEQRES 5 A 153 GLN LEU LEU ARG LEU GLY VAL TRP GLY PHE LYS GLN LEU SEQRES 6 A 153 GLN ALA ARG VAL LEU ALA LEU GLU ARG TYR LEU GLU VAL SEQRES 7 A 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 A 153 ILE CYS CYS THR THR VAL PRO TRP ASN SER THR TRP SER SEQRES 9 A 153 ASN LYS ASN TYR THR ASP ILE TRP ASP ASN MET THR TRP SEQRES 10 A 153 LEU GLN TRP ASP ARG GLU ILE GLY ASN TYR THR ASP GLU SEQRES 11 A 153 ILE TYR ARG LEU ILE GLU GLU SER GLN PHE GLN GLN GLU SEQRES 12 A 153 ILE ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 C 479 GLY PRO ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY SEQRES 2 C 479 VAL PRO VAL TRP ARG GLU ALA ASP THR THR LEU PHE CYS SEQRES 3 C 479 ALA SER ASP ALA LYS GLY TYR ASP THR GLU ALA HIS ASN SEQRES 4 C 479 VAL TRP ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN SEQRES 5 C 479 PRO GLN GLU ILE TYR LEU GLU ASN VAL THR GLU ASN PHE SEQRES 6 C 479 ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR SEQRES 7 C 479 ASP ILE ILE SER LEU TRP ASP GLU SER LEU LYS PRO CYS SEQRES 8 C 479 VAL LYS LEU THR PRO LEU CYS VAL THR LEU ASP CYS GLN SEQRES 9 C 479 ALA PHE ASN SER SER SER HIS THR ASN SER SER ILE ALA SEQRES 10 C 479 MET GLN GLU MET LYS ASN CYS SER PHE ASN VAL THR THR SEQRES 11 C 479 GLU LEU ARG ASP LYS LYS LYS LYS GLU TYR SER LEU PHE SEQRES 12 C 479 TYR LYS LEU ASP ILE VAL GLN ILE ASN LYS ASN GLY ARG SEQRES 13 C 479 GLN TYR ARG LEU ILE ASN CYS ASN THR SER ALA CYS THR SEQRES 14 C 479 GLN ILE CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE SEQRES 15 C 479 HIS PHE CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS SEQRES 16 C 479 ASN GLU LYS HIS PHE ASN GLY THR GLY PRO CYS LYS ASN SEQRES 17 C 479 VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL SEQRES 18 C 479 VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU SEQRES 19 C 479 GLU GLU VAL VAL ILE ARG SER GLU ASN ILE THR ASP ASN SEQRES 20 C 479 ALA LYS THR ILE ILE VAL GLN LEU ALA LYS PRO VAL LYS SEQRES 21 C 479 ILE ASN CYS THR ARG PRO ASN ASN MET THR ARG LYS SER SEQRES 22 C 479 ILE ARG ILE GLY PRO GLY GLN THR PHE TYR ALA LEU GLY SEQRES 23 C 479 ASP ILE ILE GLY ASN ILE ARG LYS PRO TYR CYS ASN VAL SEQRES 24 C 479 SER LYS ARG GLU TRP ASN ASN THR LEU GLN GLN VAL ALA SEQRES 25 C 479 ALA GLN LEU ARG LYS SER PHE ASN ASN THR THR ILE VAL SEQRES 26 C 479 PHE GLU LYS SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 27 C 479 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 28 C 479 THR SER GLY LEU PHE ASN SER THR TRP THR ASN SER THR SEQRES 29 C 479 TRP THR ASN SER THR THR GLY SER ASN GLY THR GLU SER SEQRES 30 C 479 ASN ASP THR ILE THR LEU GLN CYS ARG ILE LYS GLN ILE SEQRES 31 C 479 ILE ASN MET TRP GLN ARG VAL GLY ARG CYS MET TYR ALA SEQRES 32 C 479 PRO PRO ILE PRO GLY VAL ILE ARG CYS GLU SER ASN ILE SEQRES 33 C 479 THR GLY LEU LEU LEU THR ARG ASP GLY GLY ASN SER THR SEQRES 34 C 479 GLN ASN GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 C 479 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 C 479 GLN ILE GLU PRO LEU GLY VAL ALA PRO THR HIS CYS LYS SEQRES 37 C 479 ARG ARG VAL VAL GLU ARG ARG ARG ARG ARG ARG SEQRES 1 F 153 ALA VAL GLY LEU GLY ALA VAL PHE PHE GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ASN THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU LYS ALA PRO GLU ALA GLN GLN SEQRES 5 F 153 GLN LEU LEU ARG LEU GLY VAL TRP GLY PHE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA LEU GLU ARG TYR LEU GLU VAL 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 THR VAL PRO TRP ASN SER THR TRP SER SEQRES 9 F 153 ASN LYS ASN TYR THR ASP ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP ARG GLU ILE GLY ASN TYR THR ASP GLU SEQRES 11 F 153 ILE TYR ARG LEU ILE GLU GLU SER GLN PHE GLN GLN GLU SEQRES 12 F 153 ILE ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 H 479 GLY PRO ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY SEQRES 2 H 479 VAL PRO VAL TRP ARG GLU ALA ASP THR THR LEU PHE CYS SEQRES 3 H 479 ALA SER ASP ALA LYS GLY TYR ASP THR GLU ALA HIS ASN SEQRES 4 H 479 VAL TRP ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN SEQRES 5 H 479 PRO GLN GLU ILE TYR LEU GLU ASN VAL THR GLU ASN PHE SEQRES 6 H 479 ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR SEQRES 7 H 479 ASP ILE ILE SER LEU TRP ASP GLU SER LEU LYS PRO CYS SEQRES 8 H 479 VAL LYS LEU THR PRO LEU CYS VAL THR LEU ASP CYS GLN SEQRES 9 H 479 ALA PHE ASN SER SER SER HIS THR ASN SER SER ILE ALA SEQRES 10 H 479 MET GLN GLU MET LYS ASN CYS SER PHE ASN VAL THR THR SEQRES 11 H 479 GLU LEU ARG ASP LYS LYS LYS LYS GLU TYR SER LEU PHE SEQRES 12 H 479 TYR LYS LEU ASP ILE VAL GLN ILE ASN LYS ASN GLY ARG SEQRES 13 H 479 GLN TYR ARG LEU ILE ASN CYS ASN THR SER ALA CYS THR SEQRES 14 H 479 GLN ILE CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE SEQRES 15 H 479 HIS PHE CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS SEQRES 16 H 479 ASN GLU LYS HIS PHE ASN GLY THR GLY PRO CYS LYS ASN SEQRES 17 H 479 VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL SEQRES 18 H 479 VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU SEQRES 19 H 479 GLU GLU VAL VAL ILE ARG SER GLU ASN ILE THR ASP ASN SEQRES 20 H 479 ALA LYS THR ILE ILE VAL GLN LEU ALA LYS PRO VAL LYS SEQRES 21 H 479 ILE ASN CYS THR ARG PRO ASN ASN MET THR ARG LYS SER SEQRES 22 H 479 ILE ARG ILE GLY PRO GLY GLN THR PHE TYR ALA LEU GLY SEQRES 23 H 479 ASP ILE ILE GLY ASN ILE ARG LYS PRO TYR CYS ASN VAL SEQRES 24 H 479 SER LYS ARG GLU TRP ASN ASN THR LEU GLN GLN VAL ALA SEQRES 25 H 479 ALA GLN LEU ARG LYS SER PHE ASN ASN THR THR ILE VAL SEQRES 26 H 479 PHE GLU LYS SER SER GLY GLY ASP LEU GLU VAL THR THR SEQRES 27 H 479 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 28 H 479 THR SER GLY LEU PHE ASN SER THR TRP THR ASN SER THR SEQRES 29 H 479 TRP THR ASN SER THR THR GLY SER ASN GLY THR GLU SER SEQRES 30 H 479 ASN ASP THR ILE THR LEU GLN CYS ARG ILE LYS GLN ILE SEQRES 31 H 479 ILE ASN MET TRP GLN ARG VAL GLY ARG CYS MET TYR ALA SEQRES 32 H 479 PRO PRO ILE PRO GLY VAL ILE ARG CYS GLU SER ASN ILE SEQRES 33 H 479 THR GLY LEU LEU LEU THR ARG ASP GLY GLY ASN SER THR SEQRES 34 H 479 GLN ASN GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG SEQRES 35 H 479 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 36 H 479 GLN ILE GLU PRO LEU GLY VAL ALA PRO THR HIS CYS LYS SEQRES 37 H 479 ARG ARG VAL VAL GLU ARG ARG ARG ARG ARG ARG HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET MAN I 4 11 HET NAG J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET NAG L 1 14 HET NAG L 2 14 HET NAG M 1 14 HET NAG M 2 14 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 BMA O 3 11 HET MAN O 4 11 HET MAN O 5 11 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 MAN R 4 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 NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HET MAN X 4 11 HET MAN X 5 11 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG a 1 14 HET NAG a 2 14 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 BMA e 3 11 HET NAG f 1 14 HET NAG f 2 14 HET BMA f 3 11 HET MAN f 4 11 HET MAN f 5 11 HET NAG g 1 14 HET NAG g 2 14 HET NAG h 1 14 HET NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET BMA i 3 11 HET MAN i 4 11 HET MAN i 5 11 HET MAN i 6 11 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 C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HET NAG C 606 14 HET NAG H 601 14 HET NAG H 602 14 HET NAG H 603 14 HET NAG H 604 14 HET NAG H 605 14 HET NAG H 606 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 72(C8 H15 N O6) FORMUL 9 BMA 9(C6 H12 O6) FORMUL 9 MAN 11(C6 H12 O6) HELIX 1 AA1 THR B 529 SER B 534 1 6 HELIX 2 AA2 GLY B 569 TRP B 596 1 28 HELIX 3 AA3 ASN B 618 TRP B 623 1 6 HELIX 4 AA4 THR B 627 GLY B 636 1 10 HELIX 5 AA5 TYR B 638 ALA B 662 1 25 HELIX 6 AA6 ASN G 98 LEU G 116 1 19 HELIX 7 AA7 LEU G 122 CYS G 126 5 5 HELIX 8 AA8 GLU G 337 ARG G 350 1 14 HELIX 9 AA9 LYS G 351 PHE G 353 5 3 HELIX 10 AB1 MET G 475 LEU G 483 1 9 HELIX 11 AB2 SER D 28 HIS D 30 5 3 HELIX 12 AB3 GLY D 61 ARG D 64 5 4 HELIX 13 AB4 ASN D 73 MET D 75 5 3 HELIX 14 AB5 ARG D 83 THR D 87 5 5 HELIX 15 AB6 GLN E 79 PHE E 83 5 5 HELIX 16 AB7 GLY A 521 ALA A 526 5 6 HELIX 17 AB8 THR A 529 ASN A 535 5 7 HELIX 18 AB9 GLY A 569 TRP A 596 1 28 HELIX 19 AC1 ASN A 618 ASP A 624 1 7 HELIX 20 AC2 THR A 627 GLY A 636 1 10 HELIX 21 AC3 TYR A 638 LEU A 663 1 26 HELIX 22 AC4 ASN C 98 LYS C 117 1 20 HELIX 23 AC5 LEU C 122 CYS C 126 5 5 HELIX 24 AC6 ASN C 195 THR C 198 5 4 HELIX 25 AC7 ARG C 336 ARG C 350 1 15 HELIX 26 AC8 LYS C 351 ASN C 354 5 4 HELIX 27 AC9 ASP C 368 THR C 373 1 6 HELIX 28 AD1 ARG C 476 TYR C 484 1 9 HELIX 29 AD2 THR F 529 VAL F 539 5 11 HELIX 30 AD3 GLY F 569 GLY F 594 1 26 HELIX 31 AD4 ASN F 618 TRP F 623 1 6 HELIX 32 AD5 THR F 627 LEU F 663 1 37 HELIX 33 AD6 ASN H 98 LEU H 116 1 19 HELIX 34 AD7 LEU H 122 CYS H 126 5 5 HELIX 35 AD8 ASN H 195 THR H 198 5 4 HELIX 36 AD9 ARG H 336 PHE H 353 1 18 HELIX 37 AE1 ARG H 476 TYR H 484 1 9 SHEET 1 AA1 3 ILE B 603 PRO B 609 0 SHEET 2 AA1 3 TRP G 35 TYR G 40 -1 O VAL G 36 N VAL B 608 SHEET 3 AA1 3 LEU G 494 THR G 499 -1 O GLY G 495 N TYR G 39 SHEET 1 AA2 5 TRP G 45 GLU G 47 0 SHEET 2 AA2 5 TYR G 486 ILE G 491 -1 O GLN G 490 N ARG G 46 SHEET 3 AA2 5 PHE G 223 CYS G 228 -1 N ALA G 224 O VAL G 489 SHEET 4 AA2 5 VAL G 242 VAL G 245 -1 O SER G 243 N LYS G 227 SHEET 5 AA2 5 ILE G 84 TYR G 85 -1 N ILE G 84 O THR G 244 SHEET 1 AA3 3 CYS G 74 VAL G 75 0 SHEET 2 AA3 3 PHE G 53 SER G 56 1 N SER G 56 O VAL G 75 SHEET 3 AA3 3 ILE G 215 CYS G 218 -1 O HIS G 216 N ALA G 55 SHEET 1 AA4 2 GLU G 91 ASN G 94 0 SHEET 2 AA4 2 THR G 236 CYS G 239 -1 O CYS G 239 N GLU G 91 SHEET 1 AA5 3 ASP G 130 ALA G 133 0 SHEET 2 AA5 3 MET G 154 ASN G 160 -1 O SER G 158 N ASP G 130 SHEET 3 AA5 3 LYS G 171 TYR G 177 -1 O SER G 174 N CYS G 157 SHEET 1 AA6 2 ILE G 181 GLN G 183 0 SHEET 2 AA6 2 TYR G 191 LEU G 193 -1 O ARG G 192 N VAL G 182 SHEET 1 AA7 3 THR G 202 GLN G 203 0 SHEET 2 AA7 3 MET G 434 TYR G 435 1 O TYR G 435 N THR G 202 SHEET 3 AA7 3 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AA8 7 LEU G 260 LEU G 261 0 SHEET 2 AA8 7 ILE G 443 ARG G 456 -1 O THR G 450 N LEU G 260 SHEET 3 AA8 7 ILE G 284 ARG G 298 -1 N ILE G 294 O SER G 447 SHEET 4 AA8 7 TYR G 330 SER G 334 -1 O ASN G 332 N ASN G 295 SHEET 5 AA8 7 THR G 413 ILE G 420 -1 O LEU G 416 N CYS G 331 SHEET 6 AA8 7 PHE G 382 CYS G 385 -1 N TYR G 384 O ARG G 419 SHEET 7 AA8 7 HIS G 374 ASN G 377 -1 N PHE G 376 O PHE G 383 SHEET 1 AA9 6 VAL G 271 SER G 274 0 SHEET 2 AA9 6 ILE G 284 ARG G 298 -1 O ILE G 285 N ARG G 273 SHEET 3 AA9 6 ILE G 443 ARG G 456 -1 O SER G 447 N ILE G 294 SHEET 4 AA9 6 THR G 467 PRO G 470 -1 O ARG G 469 N THR G 455 SHEET 5 AA9 6 VAL G 360 PHE G 361 1 N VAL G 360 O PHE G 468 SHEET 6 AA9 6 SER G 393 THR G 394 -1 O SER G 393 N PHE G 361 SHEET 1 AB1 2 ASN G 301 GLY G 312 0 SHEET 2 AB1 2 GLN G 315 ILE G 323 -1 O GLY G 321 N THR G 303 SHEET 1 AB2 4 GLN D 3 SER D 7 0 SHEET 2 AB2 4 LEU D 20 SER D 25 -1 O THR D 23 N VAL D 5 SHEET 3 AB2 4 SER D 77 LEU D 80 -1 O LEU D 78 N CYS D 22 SHEET 4 AB2 4 ILE D 69 GLU D 72 -1 N SER D 70 O SER D 79 SHEET 1 AB3 6 LEU D 11 VAL D 12 0 SHEET 2 AB3 6 VAL D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AB3 6 GLY D 88 PRO D 97 -1 N TYR D 90 O VAL D 107 SHEET 4 AB3 6 TYR D 32 GLN D 39 -1 N ALA D 35 O ALA D 93 SHEET 5 AB3 6 GLU D 46 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AB3 6 ASP D 58 TYR D 59 -1 O ASP D 58 N SER D 50 SHEET 1 AB4 4 LEU D 11 VAL D 12 0 SHEET 2 AB4 4 VAL D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AB4 4 GLY D 88 PRO D 97 -1 N TYR D 90 O VAL D 107 SHEET 4 AB4 4 PHE D 100P TRP D 103 -1 O VAL D 102 N SER D 94 SHEET 1 AB5 4 MET E 4 SER E 7 0 SHEET 2 AB5 4 VAL E 19 ALA E 25 -1 O ARG E 24 N THR E 5 SHEET 3 AB5 4 THR E 72 ILE E 75 -1 O LEU E 73 N ILE E 21 SHEET 4 AB5 4 PHE E 62 GLY E 64 -1 N SER E 63 O THR E 74 SHEET 1 AB6 2 SER E 10 SER E 12 0 SHEET 2 AB6 2 LYS E 103 GLU E 105 1 O LYS E 103 N LEU E 11 SHEET 1 AB7 4 THR E 53 LEU E 54 0 SHEET 2 AB7 4 LYS E 45 TYR E 49 -1 N TYR E 49 O THR E 53 SHEET 3 AB7 4 LEU E 33 GLN E 38 -1 N GLN E 37 O LYS E 45 SHEET 4 AB7 4 THR E 85 GLN E 90 -1 O GLN E 89 N ALA E 34 SHEET 1 AB8 3 ILE A 603 PRO A 609 0 SHEET 2 AB8 3 TRP C 35 TYR C 40 -1 O VAL C 38 N CYS A 604 SHEET 3 AB8 3 LEU C 494 THR C 499 -1 O GLY C 495 N TYR C 39 SHEET 1 AB9 5 TRP C 45 GLU C 47 0 SHEET 2 AB9 5 TYR C 486 ILE C 491 -1 O GLN C 490 N ARG C 46 SHEET 3 AB9 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AB9 5 VAL C 242 VAL C 245 -1 O VAL C 245 N ILE C 225 SHEET 5 AB9 5 ILE C 84 TYR C 85 -1 N ILE C 84 O THR C 244 SHEET 1 AC1 2 PHE C 53 ALA C 55 0 SHEET 2 AC1 2 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AC2 2 GLU C 91 ASN C 94 0 SHEET 2 AC2 2 THR C 236 CYS C 239 -1 O CYS C 239 N GLU C 91 SHEET 1 AC3 3 LEU C 129 ASP C 130 0 SHEET 2 AC3 3 MET C 154 THR C 162 -1 O SER C 158 N ASP C 130 SHEET 3 AC3 3 LYS C 169 TYR C 177 -1 O GLU C 172 N PHE C 159 SHEET 1 AC4 2 ILE C 181 GLN C 183 0 SHEET 2 AC4 2 TYR C 191 LEU C 193 -1 O ARG C 192 N VAL C 182 SHEET 1 AC5 3 THR C 202 GLN C 203 0 SHEET 2 AC5 3 MET C 434 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AC5 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AC6 6 VAL C 271 ARG C 273 0 SHEET 2 AC6 6 ILE C 284 GLN C 287 -1 O ILE C 285 N ARG C 273 SHEET 3 AC6 6 GLY C 451 ARG C 456 -1 O LEU C 454 N ILE C 284 SHEET 4 AC6 6 THR C 467 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AC6 6 ILE C 359 PHE C 361 1 N VAL C 360 O PHE C 468 SHEET 6 AC6 6 THR C 394 TRP C 395 -1 O TRP C 395 N ILE C 359 SHEET 1 AC7 4 GLN C 315 ILE C 323 0 SHEET 2 AC7 4 LYS C 293 GLY C 312 -1 N ILE C 307 O PHE C 317 SHEET 3 AC7 4 TYR C 330 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 4 AC7 4 THR C 413 GLN C 417 -1 O LEU C 416 N CYS C 331 SHEET 1 AC8 3 GLN C 315 ILE C 323 0 SHEET 2 AC8 3 LYS C 293 GLY C 312 -1 N ILE C 307 O PHE C 317 SHEET 3 AC8 3 GLY C 441 ASN C 448 -1 O SER C 447 N ILE C 294 SHEET 1 AC9 3 HIS C 374 CYS C 378 0 SHEET 2 AC9 3 GLU C 381 CYS C 385 -1 O CYS C 385 N HIS C 374 SHEET 3 AC9 3 ARG C 419 ILE C 420 -1 O ARG C 419 N TYR C 384 SHEET 1 AD1 3 ILE F 603 PRO F 609 0 SHEET 2 AD1 3 TRP H 35 TYR H 40 -1 O VAL H 38 N CYS F 604 SHEET 3 AD1 3 LEU H 494 THR H 499 -1 O THR H 499 N TRP H 35 SHEET 1 AD2 4 TRP H 45 GLU H 47 0 SHEET 2 AD2 4 TYR H 486 ILE H 491 -1 O GLN H 490 N ARG H 46 SHEET 3 AD2 4 PHE H 223 CYS H 228 -1 N ALA H 224 O VAL H 489 SHEET 4 AD2 4 VAL H 242 VAL H 245 -1 O SER H 243 N LYS H 227 SHEET 1 AD3 2 PHE H 53 SER H 56 0 SHEET 2 AD3 2 ILE H 215 CYS H 218 -1 O HIS H 216 N ALA H 55 SHEET 1 AD4 2 GLU H 91 ASN H 94 0 SHEET 2 AD4 2 THR H 236 CYS H 239 -1 O CYS H 239 N GLU H 91 SHEET 1 AD5 3 ASP H 130 ALA H 133 0 SHEET 2 AD5 3 MET H 154 THR H 162 -1 O SER H 158 N ASP H 130 SHEET 3 AD5 3 LYS H 169 TYR H 177 -1 O LYS H 170 N VAL H 161 SHEET 1 AD6 2 ILE H 181 VAL H 182 0 SHEET 2 AD6 2 ARG H 192 LEU H 193 -1 O ARG H 192 N VAL H 182 SHEET 1 AD7 3 THR H 202 GLN H 203 0 SHEET 2 AD7 3 MET H 434 TYR H 435 1 O TYR H 435 N THR H 202 SHEET 3 AD7 3 ILE H 423 ILE H 424 -1 N ILE H 424 O MET H 434 SHEET 1 AD8 4 LEU H 259 LEU H 261 0 SHEET 2 AD8 4 ILE H 443 LEU H 452 -1 O THR H 450 N LEU H 260 SHEET 3 AD8 4 ILE H 285 ARG H 298 -1 N LEU H 288 O THR H 450 SHEET 4 AD8 4 VAL H 271 ARG H 273 -1 N VAL H 271 O GLN H 287 SHEET 1 AD9 5 LEU H 259 LEU H 261 0 SHEET 2 AD9 5 ILE H 443 LEU H 452 -1 O THR H 450 N LEU H 260 SHEET 3 AD9 5 ILE H 285 ARG H 298 -1 N LEU H 288 O THR H 450 SHEET 4 AD9 5 TYR H 330 SER H 334 -1 O ASN H 332 N ASN H 295 SHEET 5 AD9 5 THR H 413 GLN H 417 -1 O ILE H 414 N VAL H 333 SHEET 1 AE1 2 ASN H 301 GLY H 312 0 SHEET 2 AE1 2 GLN H 315 ILE H 323 -1 O ALA H 319 N LYS H 305 SHEET 1 AE2 4 SER H 393 TRP H 395 0 SHEET 2 AE2 4 ILE H 359 PHE H 361 -1 N PHE H 361 O SER H 393 SHEET 3 AE2 4 THR H 467 PRO H 470 1 O PHE H 468 N VAL H 360 SHEET 4 AE2 4 LEU H 454 ARG H 456 -1 N THR H 455 O ARG H 469 SHEET 1 AE3 3 HIS H 374 CYS H 378 0 SHEET 2 AE3 3 GLU H 381 CYS H 385 -1 O CYS H 385 N HIS H 374 SHEET 3 AE3 3 ARG H 419 ILE H 420 -1 O ARG H 419 N TYR H 384 SSBOND 1 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 2 CYS B 605 CYS G 501 1555 1555 2.03 SSBOND 3 CYS G 54 CYS G 74 1555 1555 2.03 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 201 CYS G 433 1555 1555 2.04 SSBOND 8 CYS G 218 CYS G 247 1555 1555 2.03 SSBOND 9 CYS G 228 CYS G 239 1555 1555 2.04 SSBOND 10 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 11 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 12 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 13 CYS E 23 CYS E 88 1555 1555 2.04 SSBOND 14 CYS A 598 CYS A 604 1555 1555 2.03 SSBOND 15 CYS A 605 CYS C 501 1555 1555 2.05 SSBOND 16 CYS C 54 CYS C 74 1555 1555 2.04 SSBOND 17 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 18 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 19 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 20 CYS C 201 CYS C 433 1555 1555 2.04 SSBOND 21 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 22 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 23 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 24 CYS C 385 CYS C 418 1555 1555 2.05 SSBOND 25 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 26 CYS F 605 CYS H 501 1555 1555 2.03 SSBOND 27 CYS H 54 CYS H 74 1555 1555 2.03 SSBOND 28 CYS H 119 CYS H 205 1555 1555 2.04 SSBOND 29 CYS H 126 CYS H 196 1555 1555 2.04 SSBOND 30 CYS H 131 CYS H 157 1555 1555 2.03 SSBOND 31 CYS H 201 CYS H 433 1555 1555 2.03 SSBOND 32 CYS H 218 CYS H 247 1555 1555 2.03 SSBOND 33 CYS H 228 CYS H 239 1555 1555 2.04 SSBOND 34 CYS H 378 CYS H 445 1555 1555 2.03 SSBOND 35 CYS H 385 CYS H 418 1555 1555 2.04 LINK ND2 ASN G 88 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN G 135 C1 NAG G 605 1555 1555 1.44 LINK ND2 ASN G 156 C1 NAG L 1 1555 1555 1.44 LINK ND2 ASN G 160 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN G 197 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN G 234 C1 NAG G 601 1555 1555 1.44 LINK ND2 ASN G 241 C1 NAG G 602 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN G 295 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN G 339 C1 NAG G 604 1555 1555 1.44 LINK ND2 ASN G 386 C1 NAG G 606 1555 1555 1.44 LINK ND2 ASN G 392 C1 NAG G 603 1555 1555 1.44 LINK ND2 ASN G 448 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN C 135 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 601 1555 1555 1.45 LINK ND2 ASN C 241 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG W 1 1555 1555 1.45 LINK ND2 ASN C 301 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN H 88 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN H 135 C1 NAG H 605 1555 1555 1.44 LINK ND2 ASN H 156 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN H 160 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN H 197 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN H 234 C1 NAG H 601 1555 1555 1.44 LINK ND2 ASN H 241 C1 NAG H 602 1555 1555 1.44 LINK ND2 ASN H 262 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN H 295 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN H 301 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN H 332 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN H 339 C1 NAG H 604 1555 1555 1.44 LINK ND2 ASN H 386 C1 NAG H 606 1555 1555 1.44 LINK ND2 ASN H 392 C1 NAG H 603 1555 1555 1.44 LINK ND2 ASN H 448 C1 NAG b 1 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.46 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG L 1 C1 NAG L 2 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 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.46 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.45 LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.45 LINK O6 BMA O 3 C1 MAN O 5 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 1.45 LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.46 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 1.45 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 W 2 C1 BMA W 3 1555 1555 1.46 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.45 LINK O3 BMA X 3 C1 MAN X 4 1555 1555 1.44 LINK O6 BMA X 3 C1 MAN X 5 1555 1555 1.45 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.45 LINK O4 NAG a 1 C1 NAG a 2 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 1.45 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 e 2 C1 BMA e 3 1555 1555 1.46 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.45 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.45 LINK O3 BMA f 3 C1 MAN f 4 1555 1555 1.45 LINK O6 BMA f 3 C1 MAN f 5 1555 1555 1.45 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.45 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.44 LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.45 LINK O6 BMA i 3 C1 MAN i 4 1555 1555 1.45 LINK O6 MAN i 4 C1 MAN i 5 1555 1555 1.45 LINK O2 MAN i 5 C1 MAN i 6 1555 1555 1.45 CISPEP 1 SER E 7 PRO E 8 0 -6.29 CISPEP 2 ARG E 94 PRO E 95 0 -1.06 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