HEADER VIRAL PROTEIN/IMMUNE SYSTEM 15-MAY-24 9BTJ TITLE RHESUS FAB 6561-A.01 IN COMPLEX WITH HIV-1 CE1176.A3 RNS SOSIP ENV COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 6561-A.01 LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB 6561-A.01 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 11 CHAIN: G, A, D; COMPND 12 SYNONYM: ENV POLYPROTEIN; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 16 CHAIN: B, C, E; COMPND 17 SYNONYM: ENV POLYPROTEIN; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 8 ORGANISM_TAXID: 9544; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 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 9BTJ 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. 4.22 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) : 4.220 REMARK 3 NUMBER OF PARTICLES : 150641 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 9BTJ 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_1000283892. 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 6561-A.01 IN COMPLEX REMARK 245 WITH HIV-1 CE1176.A3 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 K2 SUMMIT (4K 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) : 6948.00 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: L, H, G, B, A, C, D, E, F, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, j, k, l, REMARK 350 AND CHAINS: m, n, o 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 THR L 105 REMARK 465 VAL L 106 REMARK 465 LEU L 107 REMARK 465 GLY L 108 REMARK 465 GLN L 109 REMARK 465 PRO L 110 REMARK 465 LYS L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 THR L 117 REMARK 465 LEU L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 SER L 123 REMARK 465 GLU L 124 REMARK 465 GLU L 125 REMARK 465 LEU L 126 REMARK 465 GLN L 127 REMARK 465 ALA L 128 REMARK 465 ASN L 129 REMARK 465 LYS L 130 REMARK 465 ALA L 131 REMARK 465 THR L 132 REMARK 465 LEU L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 ILE L 137 REMARK 465 SER L 138 REMARK 465 ASP L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 GLY L 143 REMARK 465 ALA L 144 REMARK 465 VAL L 145 REMARK 465 THR L 146 REMARK 465 VAL L 147 REMARK 465 ALA L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 ALA L 151 REMARK 465 ASP L 152 REMARK 465 SER L 153 REMARK 465 SER L 154 REMARK 465 PRO L 155 REMARK 465 VAL L 156 REMARK 465 LYS L 157 REMARK 465 ALA L 158 REMARK 465 GLY L 159 REMARK 465 VAL L 160 REMARK 465 GLU L 161 REMARK 465 THR L 162 REMARK 465 THR L 163 REMARK 465 THR L 164 REMARK 465 PRO L 165 REMARK 465 SER L 166 REMARK 465 LYS L 167 REMARK 465 GLN L 168 REMARK 465 SER L 169 REMARK 465 ASN L 170 REMARK 465 ASN L 171 REMARK 465 LYS L 172 REMARK 465 TYR L 173 REMARK 465 ALA L 174 REMARK 465 ALA L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 TYR L 178 REMARK 465 LEU L 179 REMARK 465 SER L 180 REMARK 465 LEU L 181 REMARK 465 THR L 182 REMARK 465 PRO L 183 REMARK 465 GLU L 184 REMARK 465 GLN L 185 REMARK 465 TRP L 186 REMARK 465 LYS L 187 REMARK 465 SER L 188 REMARK 465 HIS L 189 REMARK 465 ARG L 190 REMARK 465 SER L 191 REMARK 465 TYR L 192 REMARK 465 SER L 193 REMARK 465 CYS L 194 REMARK 465 GLN L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLU L 199 REMARK 465 GLY L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 VAL L 203 REMARK 465 GLU L 204 REMARK 465 LYS L 205 REMARK 465 THR L 206 REMARK 465 VAL L 207 REMARK 465 ALA L 208 REMARK 465 PRO L 209 REMARK 465 THR L 210 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 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 GLY G 29 REMARK 465 PRO G 30 REMARK 465 ALA G 31 REMARK 465 GLU G 32 REMARK 465 SER G 144 REMARK 465 SER G 145 REMARK 465 ASN G 146 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 B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 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 LEU B 568 REMARK 465 GLY A 29 REMARK 465 PRO A 30 REMARK 465 ALA A 31 REMARK 465 GLU A 32 REMARK 465 ASN A 142 REMARK 465 GLY A 143 REMARK 465 SER A 144 REMARK 465 SER A 145 REMARK 465 ASN A 146 REMARK 465 ARG A 508 REMARK 465 ARG A 509 REMARK 465 ARG A 510 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 ARG A 513 REMARK 465 ALA C 512 REMARK 465 VAL C 513 REMARK 465 GLY C 514 REMARK 465 ILE C 515 REMARK 465 GLY C 516 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 LEU C 568 REMARK 465 GLY D 29 REMARK 465 PRO D 30 REMARK 465 ALA D 31 REMARK 465 GLU D 32 REMARK 465 SER D 144 REMARK 465 SER D 145 REMARK 465 ASN D 146 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 512 REMARK 465 VAL E 513 REMARK 465 GLY E 514 REMARK 465 ILE E 515 REMARK 465 GLY E 516 REMARK 465 ALA E 517 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 LEU E 568 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 G 297 O ILE G 443 2.14 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 LYS L 42 -96.80 55.80 REMARK 500 THR L 92 -137.07 47.96 REMARK 500 PHE L 98 -172.01 63.70 REMARK 500 TYR H 33 -127.86 63.59 REMARK 500 TYR H 58 76.73 -100.88 REMARK 500 VAL H 102 -64.26 -90.76 REMARK 500 TRP H 103 157.05 63.03 REMARK 500 ARG H 105 -150.18 37.19 REMARK 500 LYS G 63 164.90 65.51 REMARK 500 ASP G 78 136.26 -172.99 REMARK 500 LYS G 166 -64.25 64.55 REMARK 500 PRO G 183 44.36 -77.57 REMARK 500 LEU G 184 -75.97 46.37 REMARK 500 CYS G 247 -178.58 -173.35 REMARK 500 ASN G 262 41.23 37.55 REMARK 500 THR G 387 75.25 -100.56 REMARK 500 PRO G 438 172.36 -59.21 REMARK 500 CYS B 598 57.10 -95.18 REMARK 500 VAL A 65 27.64 45.13 REMARK 500 ASP A 78 135.99 -173.15 REMARK 500 PRO A 183 43.50 -84.64 REMARK 500 LEU A 184 -76.38 39.98 REMARK 500 ASN A 262 47.62 36.73 REMARK 500 SER A 300 139.48 -172.60 REMARK 500 THR A 387 51.82 -94.16 REMARK 500 PHE C 519 -135.68 39.61 REMARK 500 LEU C 545 -9.25 71.77 REMARK 500 VAL D 65 27.73 44.79 REMARK 500 ASP D 78 137.39 -171.99 REMARK 500 ASN D 185 -156.09 57.35 REMARK 500 ASN D 195 34.50 -99.67 REMARK 500 ASN D 262 40.40 37.91 REMARK 500 LYS D 268 -60.46 -94.31 REMARK 500 SER D 300 146.33 -176.95 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG F 1 REMARK 610 NAG V 1 REMARK 610 NAG W 1 REMARK 610 NAG Y 1 REMARK 610 NAG c 1 REMARK 610 NAG h 1 REMARK 610 NAG i 1 REMARK 610 NAG k 1 REMARK 610 NAG l 1 REMARK 610 NAG n 1 REMARK 610 NAG G 603 REMARK 610 NAG G 605 REMARK 610 NAG G 609 REMARK 610 NAG G 610 REMARK 610 NAG G 613 REMARK 610 NAG G 614 REMARK 610 NAG G 616 REMARK 610 NAG A 603 REMARK 610 NAG A 605 REMARK 610 NAG A 613 REMARK 610 NAG A 614 REMARK 610 NAG D 603 REMARK 610 NAG D 605 REMARK 610 NAG D 609 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44892 RELATED DB: EMDB REMARK 900 RHESUS FAB 6561-A.01 IN COMPLEX WITH HIV-1 CE1176.A3 RNS SOSIP ENV DBREF 9BTJ L 1 213 PDB 9BTJ 9BTJ 1 213 DBREF 9BTJ H 1 225 PDB 9BTJ 9BTJ 1 225 DBREF 9BTJ G 33 508 UNP C6G0D7 C6G0D7_9HIV1 32 499 DBREF 9BTJ B 512 664 UNP C6G0E7 C6G0E7_9HIV1 503 655 DBREF 9BTJ A 33 508 UNP C6G0D7 C6G0D7_9HIV1 32 499 DBREF 9BTJ C 512 664 UNP C6G0E7 C6G0E7_9HIV1 503 655 DBREF 9BTJ D 33 508 UNP C6G0D7 C6G0D7_9HIV1 32 499 DBREF 9BTJ E 512 664 UNP C6G0E7 C6G0E7_9HIV1 503 655 SEQADV 9BTJ GLY G 29 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ PRO G 30 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ALA G 31 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ GLU G 32 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ASN G 130 UNP C6G0D7 THR 129 CONFLICT SEQADV 9BTJ CYS G 201 UNP C6G0D7 ILE 196 CONFLICT SEQADV 9BTJ THR G 202 UNP C6G0D7 ALA 197 CONFLICT SEQADV 9BTJ ILE G 204 UNP C6G0D7 ALA 199 CONFLICT SEQADV 9BTJ VAL G 286 UNP C6G0D7 ILE 281 CONFLICT SEQADV 9BTJ LEU G 288 UNP C6G0D7 PHE 283 CONFLICT SEQADV 9BTJ MET G 302 UNP C6G0D7 ASN 297 CONFLICT SEQADV 9BTJ LEU G 320 UNP C6G0D7 THR 313 CONFLICT SEQADV 9BTJ PRO G 329 UNP C6G0D7 ALA 323 CONFLICT SEQADV 9BTJ ILE G 333 UNP C6G0D7 VAL 327 CONFLICT SEQADV 9BTJ CYS G 433 UNP C6G0D7 ALA 424 CONFLICT SEQADV 9BTJ ASN G 448 UNP C6G0D7 THR 439 CONFLICT SEQADV 9BTJ SER G 481 UNP C6G0D7 ASN 472 CONFLICT SEQADV 9BTJ CYS G 501 UNP C6G0D7 ALA 492 CONFLICT SEQADV 9BTJ ARG G 509 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG G 510 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG G 511 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG G 512 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG G 513 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ASN B 535 UNP C6G0E7 ILE 526 CONFLICT SEQADV 9BTJ PRO B 559 UNP C6G0E7 ILE 550 CONFLICT SEQADV 9BTJ GLY B 569 UNP C6G0E7 THR 560 CONFLICT SEQADV 9BTJ PHE B 573 UNP C6G0E7 ILE 564 CONFLICT SEQADV 9BTJ GLU B 588 UNP C6G0E7 LYS 579 CONFLICT SEQADV 9BTJ VAL B 589 UNP C6G0E7 ASP 580 CONFLICT SEQADV 9BTJ CYS B 605 UNP C6G0E7 THR 596 CONFLICT SEQADV 9BTJ THR B 613 UNP C6G0E7 SER 604 CONFLICT SEQADV 9BTJ THR B 618 UNP C6G0E7 SER 609 CONFLICT SEQADV 9BTJ GLY B 636 UNP C6G0E7 ASP 627 CONFLICT SEQADV 9BTJ PHE B 651 UNP C6G0E7 ILE 642 CONFLICT SEQADV 9BTJ ILE B 655 UNP C6G0E7 LYS 646 CONFLICT SEQADV 9BTJ GLY A 29 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ PRO A 30 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ALA A 31 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ GLU A 32 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ASN A 130 UNP C6G0D7 THR 129 CONFLICT SEQADV 9BTJ CYS A 201 UNP C6G0D7 ILE 196 CONFLICT SEQADV 9BTJ THR A 202 UNP C6G0D7 ALA 197 CONFLICT SEQADV 9BTJ ILE A 204 UNP C6G0D7 ALA 199 CONFLICT SEQADV 9BTJ VAL A 286 UNP C6G0D7 ILE 281 CONFLICT SEQADV 9BTJ LEU A 288 UNP C6G0D7 PHE 283 CONFLICT SEQADV 9BTJ MET A 302 UNP C6G0D7 ASN 297 CONFLICT SEQADV 9BTJ LEU A 320 UNP C6G0D7 THR 313 CONFLICT SEQADV 9BTJ PRO A 329 UNP C6G0D7 ALA 323 CONFLICT SEQADV 9BTJ ILE A 333 UNP C6G0D7 VAL 327 CONFLICT SEQADV 9BTJ CYS A 433 UNP C6G0D7 ALA 424 CONFLICT SEQADV 9BTJ ASN A 448 UNP C6G0D7 THR 439 CONFLICT SEQADV 9BTJ SER A 481 UNP C6G0D7 ASN 472 CONFLICT SEQADV 9BTJ CYS A 501 UNP C6G0D7 ALA 492 CONFLICT SEQADV 9BTJ ARG A 509 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG A 510 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG A 511 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG A 512 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG A 513 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ASN C 535 UNP C6G0E7 ILE 526 CONFLICT SEQADV 9BTJ PRO C 559 UNP C6G0E7 ILE 550 CONFLICT SEQADV 9BTJ GLY C 569 UNP C6G0E7 THR 560 CONFLICT SEQADV 9BTJ PHE C 573 UNP C6G0E7 ILE 564 CONFLICT SEQADV 9BTJ GLU C 588 UNP C6G0E7 LYS 579 CONFLICT SEQADV 9BTJ VAL C 589 UNP C6G0E7 ASP 580 CONFLICT SEQADV 9BTJ CYS C 605 UNP C6G0E7 THR 596 CONFLICT SEQADV 9BTJ THR C 613 UNP C6G0E7 SER 604 CONFLICT SEQADV 9BTJ THR C 618 UNP C6G0E7 SER 609 CONFLICT SEQADV 9BTJ GLY C 636 UNP C6G0E7 ASP 627 CONFLICT SEQADV 9BTJ PHE C 651 UNP C6G0E7 ILE 642 CONFLICT SEQADV 9BTJ ILE C 655 UNP C6G0E7 LYS 646 CONFLICT SEQADV 9BTJ GLY D 29 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ PRO D 30 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ALA D 31 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ GLU D 32 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ASN D 130 UNP C6G0D7 THR 129 CONFLICT SEQADV 9BTJ CYS D 201 UNP C6G0D7 ILE 196 CONFLICT SEQADV 9BTJ THR D 202 UNP C6G0D7 ALA 197 CONFLICT SEQADV 9BTJ ILE D 204 UNP C6G0D7 ALA 199 CONFLICT SEQADV 9BTJ VAL D 286 UNP C6G0D7 ILE 281 CONFLICT SEQADV 9BTJ LEU D 288 UNP C6G0D7 PHE 283 CONFLICT SEQADV 9BTJ MET D 302 UNP C6G0D7 ASN 297 CONFLICT SEQADV 9BTJ LEU D 320 UNP C6G0D7 THR 313 CONFLICT SEQADV 9BTJ PRO D 329 UNP C6G0D7 ALA 323 CONFLICT SEQADV 9BTJ ILE D 333 UNP C6G0D7 VAL 327 CONFLICT SEQADV 9BTJ CYS D 433 UNP C6G0D7 ALA 424 CONFLICT SEQADV 9BTJ ASN D 448 UNP C6G0D7 THR 439 CONFLICT SEQADV 9BTJ SER D 481 UNP C6G0D7 ASN 472 CONFLICT SEQADV 9BTJ CYS D 501 UNP C6G0D7 ALA 492 CONFLICT SEQADV 9BTJ ARG D 509 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG D 510 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG D 511 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG D 512 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ARG D 513 UNP C6G0D7 EXPRESSION TAG SEQADV 9BTJ ASN E 535 UNP C6G0E7 ILE 526 CONFLICT SEQADV 9BTJ PRO E 559 UNP C6G0E7 ILE 550 CONFLICT SEQADV 9BTJ GLY E 569 UNP C6G0E7 THR 560 CONFLICT SEQADV 9BTJ PHE E 573 UNP C6G0E7 ILE 564 CONFLICT SEQADV 9BTJ GLU E 588 UNP C6G0E7 LYS 579 CONFLICT SEQADV 9BTJ VAL E 589 UNP C6G0E7 ASP 580 CONFLICT SEQADV 9BTJ CYS E 605 UNP C6G0E7 THR 596 CONFLICT SEQADV 9BTJ THR E 613 UNP C6G0E7 SER 604 CONFLICT SEQADV 9BTJ THR E 618 UNP C6G0E7 SER 609 CONFLICT SEQADV 9BTJ GLY E 636 UNP C6G0E7 ASP 627 CONFLICT SEQADV 9BTJ PHE E 651 UNP C6G0E7 ILE 642 CONFLICT SEQADV 9BTJ ILE E 655 UNP C6G0E7 LYS 646 CONFLICT SEQRES 1 L 217 GLN PRO VAL VAL THR GLN SER PRO SER ALA SER ALA SER SEQRES 2 L 217 LEU GLY ALA SER VAL LYS LEU THR CYS THR LEU GLY SER SEQRES 3 L 217 GLY ASN THR ASN TYR ALA ILE ALA TRP HIS GLN GLN GLN SEQRES 4 L 217 GLU GLY LYS ALA PRO ARG PHE LEU MET ARG VAL GLU SER SEQRES 5 L 217 GLY GLY SER HIS SER LYS GLY ASP GLY ILE PRO HIS ARG SEQRES 6 L 217 PHE SER GLY SER SER SER GLY ALA GLU ARG TYR LEU THR SEQRES 7 L 217 ILE SER ASN LEU GLN SER GLU ASP GLU ALA ASP TYR PHE SEQRES 8 L 217 CYS GLN THR TRP THR THR GLY THR HIS VAL PHE GLY VAL SEQRES 9 L 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 L 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 H 246 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 H 246 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 246 GLY SER ILE SER ASP ARG TYR TYR TRP ASN TRP ILE ARG SEQRES 4 H 246 GLN ARG PRO GLY LYS PRO LEU GLU TRP LEU GLY ASN ILE SEQRES 5 H 246 TYR GLY PHE SER GLU ARG THR TYR HIS ASN PRO SER PHE SEQRES 6 H 246 LYS SER ARG VAL THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 H 246 GLN PHE PHE LEU SER LEU SER SER VAL THR ALA ALA ASP SEQRES 8 H 246 THR ALA VAL TYR TYR CYS VAL ARG ASP ARG LEU LEU GLU SEQRES 9 H 246 GLU TYR TYS GLU GLU ASP TYS ASP ASN TRP TYR ARG VAL SEQRES 10 H 246 PHE ASP ALA LEU GLU VAL TRP GLY ARG GLY LEU LEU VAL SEQRES 11 H 246 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 12 H 246 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 13 H 246 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 14 H 246 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 15 H 246 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 16 H 246 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 17 H 246 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 18 H 246 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 19 H 246 LYS SER CYS ASP LYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 G 477 GLY PRO ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY SEQRES 2 G 477 VAL PRO VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS SEQRES 3 G 477 ALA SER ASP ALA LYS ALA TYR GLU LYS GLU VAL HIS ASN SEQRES 4 G 477 VAL TRP ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN SEQRES 5 G 477 PRO GLN GLU MET VAL LEU GLU ASN VAL THR GLU ASN PHE SEQRES 6 G 477 ASN MET TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU SEQRES 7 G 477 ASP VAL ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS SEQRES 8 G 477 VAL LYS LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR SEQRES 9 G 477 ASN THR THR VAL SER ASN GLY SER SER ASN SER ASN ALA SEQRES 10 G 477 ASN PHE GLU GLU MET LYS ASN CYS SER PHE ASN ALA THR SEQRES 11 G 477 THR GLU ILE LYS ASP LYS LYS LYS ASN GLU TYR ALA LEU SEQRES 12 G 477 PHE TYR LYS LEU ASP ILE VAL PRO LEU ASN ASN SER SER SEQRES 13 G 477 GLY LYS TYR ARG LEU ILE ASN CYS ASN THR SER ALA CYS SEQRES 14 G 477 THR GLN ILE CYS PRO LYS VAL THR PHE GLU PRO ILE PRO SEQRES 15 G 477 ILE HIS TYR CYS ALA PRO ALA GLY TYR ALA ILE LEU LYS SEQRES 16 G 477 CYS ASN ASN LYS THR PHE ASN GLY THR GLY PRO CYS ASN SEQRES 17 G 477 ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 G 477 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 G 477 GLU LYS GLU ILE ILE ILE ARG SER GLU ASN LEU THR ASN SEQRES 20 G 477 ASN ALA LYS THR ILE ILE VAL HIS LEU ASN GLU SER VAL SEQRES 21 G 477 GLY ILE VAL CYS THR ARG PRO SER ASN MET THR ARG LYS SEQRES 22 G 477 SER ILE ARG ILE GLY PRO GLY GLN THR PHE TYR ALA LEU SEQRES 23 G 477 GLY ASP ILE ILE GLY ASP ILE ARG GLN PRO HIS CYS ASN SEQRES 24 G 477 ILE SER LYS GLN ASN TRP ASN ARG THR LEU GLN GLN VAL SEQRES 25 G 477 GLY ARG LYS LEU ALA GLU HIS PHE PRO ASN ARG ASN ILE SEQRES 26 G 477 THR PHE ASN HIS SER SER GLY GLY ASP LEU GLU ILE THR SEQRES 27 G 477 THR HIS SER PHE ASN CYS ARG GLY GLU PHE PHE TYR CYS SEQRES 28 G 477 ASN THR SER GLY LEU PHE ASN GLY THR TYR HIS PRO ASN SEQRES 29 G 477 GLY THR TYR ASN GLU THR ALA VAL ASN SER SER ASP THR SEQRES 30 G 477 ILE THR LEU GLN CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 31 G 477 TRP GLN GLU VAL GLY ARG CYS MET TYR ALA PRO PRO ILE SEQRES 32 G 477 ALA GLY ASN ILE THR CYS ASN SER ASN ILE THR GLY LEU SEQRES 33 G 477 LEU LEU THR ARG ASP GLY GLY ILE ASN GLN THR GLY GLU SEQRES 34 G 477 GLU ILE PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 35 G 477 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE SEQRES 36 G 477 LYS PRO LEU GLY ILE ALA PRO THR LYS CYS LYS ARG ARG SEQRES 37 G 477 VAL VAL GLU ARG ARG ARG ARG ARG ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU 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 ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS MET LEU GLN LEU GLY VAL TRP GLY PHE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA ILE 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 ASN VAL PRO TRP ASN SER THR TRP SER SEQRES 9 B 153 ASN ARG THR GLN GLU ASP ILE TRP ASN ASN MET THR TRP SEQRES 10 B 153 MET GLU TRP GLU ARG GLU ILE GLY ASN TYR THR HIS THR SEQRES 11 B 153 ILE TYR SER LEU LEU GLU GLU SER GLN PHE GLN GLN GLU SEQRES 12 B 153 ILE ASN GLU LYS ASP LEU LEU ALA LEU ASP SEQRES 1 A 477 GLY PRO ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY SEQRES 2 A 477 VAL PRO VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS SEQRES 3 A 477 ALA SER ASP ALA LYS ALA TYR GLU LYS GLU VAL HIS ASN SEQRES 4 A 477 VAL TRP ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN SEQRES 5 A 477 PRO GLN GLU MET VAL LEU GLU ASN VAL THR GLU ASN PHE SEQRES 6 A 477 ASN MET TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU SEQRES 7 A 477 ASP VAL ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS SEQRES 8 A 477 VAL LYS LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR SEQRES 9 A 477 ASN THR THR VAL SER ASN GLY SER SER ASN SER ASN ALA SEQRES 10 A 477 ASN PHE GLU GLU MET LYS ASN CYS SER PHE ASN ALA THR SEQRES 11 A 477 THR GLU ILE LYS ASP LYS LYS LYS ASN GLU TYR ALA LEU SEQRES 12 A 477 PHE TYR LYS LEU ASP ILE VAL PRO LEU ASN ASN SER SER SEQRES 13 A 477 GLY LYS TYR ARG LEU ILE ASN CYS ASN THR SER ALA CYS SEQRES 14 A 477 THR GLN ILE CYS PRO LYS VAL THR PHE GLU PRO ILE PRO SEQRES 15 A 477 ILE HIS TYR CYS ALA PRO ALA GLY TYR ALA ILE LEU LYS SEQRES 16 A 477 CYS ASN ASN LYS THR PHE ASN GLY THR GLY PRO CYS ASN SEQRES 17 A 477 ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 A 477 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 A 477 GLU LYS GLU ILE ILE ILE ARG SER GLU ASN LEU THR ASN SEQRES 20 A 477 ASN ALA LYS THR ILE ILE VAL HIS LEU ASN GLU SER VAL SEQRES 21 A 477 GLY ILE VAL CYS THR ARG PRO SER ASN MET THR ARG LYS SEQRES 22 A 477 SER ILE ARG ILE GLY PRO GLY GLN THR PHE TYR ALA LEU SEQRES 23 A 477 GLY ASP ILE ILE GLY ASP ILE ARG GLN PRO HIS CYS ASN SEQRES 24 A 477 ILE SER LYS GLN ASN TRP ASN ARG THR LEU GLN GLN VAL SEQRES 25 A 477 GLY ARG LYS LEU ALA GLU HIS PHE PRO ASN ARG ASN ILE SEQRES 26 A 477 THR PHE ASN HIS SER SER GLY GLY ASP LEU GLU ILE THR SEQRES 27 A 477 THR HIS SER PHE ASN CYS ARG GLY GLU PHE PHE TYR CYS SEQRES 28 A 477 ASN THR SER GLY LEU PHE ASN GLY THR TYR HIS PRO ASN SEQRES 29 A 477 GLY THR TYR ASN GLU THR ALA VAL ASN SER SER ASP THR SEQRES 30 A 477 ILE THR LEU GLN CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 31 A 477 TRP GLN GLU VAL GLY ARG CYS MET TYR ALA PRO PRO ILE SEQRES 32 A 477 ALA GLY ASN ILE THR CYS ASN SER ASN ILE THR GLY LEU SEQRES 33 A 477 LEU LEU THR ARG ASP GLY GLY ILE ASN GLN THR GLY GLU SEQRES 34 A 477 GLU ILE PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 35 A 477 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE SEQRES 36 A 477 LYS PRO LEU GLY ILE ALA PRO THR LYS CYS LYS ARG ARG SEQRES 37 A 477 VAL VAL GLU ARG ARG ARG ARG ARG ARG SEQRES 1 C 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 C 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ASN THR LEU SEQRES 3 C 153 THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL GLN SEQRES 4 C 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 C 153 HIS MET LEU GLN LEU GLY VAL TRP GLY PHE LYS GLN LEU SEQRES 6 C 153 GLN ALA ARG VAL LEU ALA ILE GLU ARG TYR LEU GLU VAL SEQRES 7 C 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 C 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER THR TRP SER SEQRES 9 C 153 ASN ARG THR GLN GLU ASP ILE TRP ASN ASN MET THR TRP SEQRES 10 C 153 MET GLU TRP GLU ARG GLU ILE GLY ASN TYR THR HIS THR SEQRES 11 C 153 ILE TYR SER LEU LEU GLU GLU SER GLN PHE GLN GLN GLU SEQRES 12 C 153 ILE ASN GLU LYS ASP LEU LEU ALA LEU ASP SEQRES 1 D 477 GLY PRO ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY SEQRES 2 D 477 VAL PRO VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS SEQRES 3 D 477 ALA SER ASP ALA LYS ALA TYR GLU LYS GLU VAL HIS ASN SEQRES 4 D 477 VAL TRP ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN SEQRES 5 D 477 PRO GLN GLU MET VAL LEU GLU ASN VAL THR GLU ASN PHE SEQRES 6 D 477 ASN MET TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU SEQRES 7 D 477 ASP VAL ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS SEQRES 8 D 477 VAL LYS LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR SEQRES 9 D 477 ASN THR THR VAL SER ASN GLY SER SER ASN SER ASN ALA SEQRES 10 D 477 ASN PHE GLU GLU MET LYS ASN CYS SER PHE ASN ALA THR SEQRES 11 D 477 THR GLU ILE LYS ASP LYS LYS LYS ASN GLU TYR ALA LEU SEQRES 12 D 477 PHE TYR LYS LEU ASP ILE VAL PRO LEU ASN ASN SER SER SEQRES 13 D 477 GLY LYS TYR ARG LEU ILE ASN CYS ASN THR SER ALA CYS SEQRES 14 D 477 THR GLN ILE CYS PRO LYS VAL THR PHE GLU PRO ILE PRO SEQRES 15 D 477 ILE HIS TYR CYS ALA PRO ALA GLY TYR ALA ILE LEU LYS SEQRES 16 D 477 CYS ASN ASN LYS THR PHE ASN GLY THR GLY PRO CYS ASN SEQRES 17 D 477 ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO SEQRES 18 D 477 VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA SEQRES 19 D 477 GLU LYS GLU ILE ILE ILE ARG SER GLU ASN LEU THR ASN SEQRES 20 D 477 ASN ALA LYS THR ILE ILE VAL HIS LEU ASN GLU SER VAL SEQRES 21 D 477 GLY ILE VAL CYS THR ARG PRO SER ASN MET THR ARG LYS SEQRES 22 D 477 SER ILE ARG ILE GLY PRO GLY GLN THR PHE TYR ALA LEU SEQRES 23 D 477 GLY ASP ILE ILE GLY ASP ILE ARG GLN PRO HIS CYS ASN SEQRES 24 D 477 ILE SER LYS GLN ASN TRP ASN ARG THR LEU GLN GLN VAL SEQRES 25 D 477 GLY ARG LYS LEU ALA GLU HIS PHE PRO ASN ARG ASN ILE SEQRES 26 D 477 THR PHE ASN HIS SER SER GLY GLY ASP LEU GLU ILE THR SEQRES 27 D 477 THR HIS SER PHE ASN CYS ARG GLY GLU PHE PHE TYR CYS SEQRES 28 D 477 ASN THR SER GLY LEU PHE ASN GLY THR TYR HIS PRO ASN SEQRES 29 D 477 GLY THR TYR ASN GLU THR ALA VAL ASN SER SER ASP THR SEQRES 30 D 477 ILE THR LEU GLN CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 31 D 477 TRP GLN GLU VAL GLY ARG CYS MET TYR ALA PRO PRO ILE SEQRES 32 D 477 ALA GLY ASN ILE THR CYS ASN SER ASN ILE THR GLY LEU SEQRES 33 D 477 LEU LEU THR ARG ASP GLY GLY ILE ASN GLN THR GLY GLU SEQRES 34 D 477 GLU ILE PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 35 D 477 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE SEQRES 36 D 477 LYS PRO LEU GLY ILE ALA PRO THR LYS CYS LYS ARG ARG SEQRES 37 D 477 VAL VAL GLU ARG ARG ARG ARG ARG ARG SEQRES 1 E 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 E 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ASN THR LEU SEQRES 3 E 153 THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL GLN SEQRES 4 E 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 E 153 HIS MET LEU GLN LEU GLY VAL TRP GLY PHE LYS GLN LEU SEQRES 6 E 153 GLN ALA ARG VAL LEU ALA ILE GLU ARG TYR LEU GLU VAL SEQRES 7 E 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 E 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER THR TRP SER SEQRES 9 E 153 ASN ARG THR GLN GLU ASP ILE TRP ASN ASN MET THR TRP SEQRES 10 E 153 MET GLU TRP GLU ARG GLU ILE GLY ASN TYR THR HIS THR SEQRES 11 E 153 ILE TYR SER LEU LEU GLU GLU SER GLN PHE GLN GLN GLU SEQRES 12 E 153 ILE ASN GLU LYS ASP LEU LEU ALA LEU ASP HET TYS H 100B 16 HET TYS H 100F 16 HET NAG F 1 14 HET NAG F 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 NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET NAG K 1 14 HET NAG K 2 14 HET 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 MAN N 4 11 HET MAN N 5 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 MAN O 6 11 HET MAN O 7 11 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET MAN P 4 11 HET MAN P 5 11 HET MAN P 6 11 HET MAN P 7 11 HET MAN P 8 11 HET NAG Q 1 14 HET NAG Q 2 14 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 MAN U 8 11 HET MAN U 9 11 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 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 BMA d 3 11 HET MAN d 4 11 HET MAN d 5 11 HET NAG e 1 14 HET NAG e 2 14 HET BMA e 3 11 HET MAN e 4 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 MAN f 6 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 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 BMA m 3 11 HET NAG n 1 14 HET NAG n 2 14 HET BMA n 3 11 HET MAN n 4 11 HET MAN n 5 11 HET NAG o 1 14 HET NAG o 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 B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG A 609 14 HET NAG A 610 14 HET NAG A 611 14 HET NAG A 612 14 HET NAG A 613 14 HET NAG A 614 14 HET NAG A 615 14 HET NAG C 701 14 HET NAG C 702 14 HET NAG C 703 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 E 701 14 HET NAG E 702 14 HET NAG E 703 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 2 TYS 2(C9 H11 N O6 S) FORMUL 9 NAG 117(C8 H15 N O6) FORMUL 10 BMA 13(C6 H12 O6) FORMUL 10 MAN 29(C6 H12 O6) HELIX 1 AA1 GLN L 79 GLU L 83 5 5 HELIX 2 AA2 THR H 83 THR H 87 5 5 HELIX 3 AA3 ASN G 98 SER G 115 1 18 HELIX 4 AA4 LEU G 122 CYS G 126 5 5 HELIX 5 AA5 LYS G 335 PHE G 353 1 19 HELIX 6 AA6 ASP G 368 THR G 373 1 6 HELIX 7 AA7 ASN G 402 VAL G 406 5 5 HELIX 8 AA8 ARG G 476 SER G 481 1 6 HELIX 9 AA9 THR B 529 SER B 534 1 6 HELIX 10 AB1 LEU B 537 LEU B 544 1 8 HELIX 11 AB2 VAL B 570 TRP B 596 1 27 HELIX 12 AB3 THR B 618 ASN B 624 1 7 HELIX 13 AB4 THR B 627 ILE B 635 1 9 HELIX 14 AB5 TYR B 638 ALA B 662 1 25 HELIX 15 AB6 ASN A 98 LYS A 117 1 20 HELIX 16 AB7 ASN A 195 ASN A 197 5 3 HELIX 17 AB8 LYS A 335 PHE A 353 1 19 HELIX 18 AB9 ASP A 368 THR A 373 1 6 HELIX 19 AC1 ARG A 476 SER A 481 1 6 HELIX 20 AC2 GLY C 531 THR C 536 5 6 HELIX 21 AC3 LEU C 537 ARG C 542 1 6 HELIX 22 AC4 VAL C 570 TRP C 596 1 27 HELIX 23 AC5 THR C 618 ASN C 624 1 7 HELIX 24 AC6 THR C 627 ILE C 635 1 9 HELIX 25 AC7 TYR C 638 ALA C 662 1 25 HELIX 26 AC8 ASN D 98 LYS D 117 1 20 HELIX 27 AC9 ASN D 195 ASN D 197 5 3 HELIX 28 AD1 LYS D 335 PHE D 353 1 19 HELIX 29 AD2 ASP D 368 THR D 373 1 6 HELIX 30 AD3 ARG D 476 SER D 481 1 6 HELIX 31 AD4 GLY E 531 THR E 536 5 6 HELIX 32 AD5 LEU E 537 LEU E 544 1 8 HELIX 33 AD6 VAL E 570 TRP E 596 1 27 HELIX 34 AD7 THR E 618 ASN E 624 1 7 HELIX 35 AD8 THR E 627 ILE E 635 1 9 HELIX 36 AD9 TYR E 638 ALA E 662 1 25 SHEET 1 AA1 4 VAL L 3 THR L 5 0 SHEET 2 AA1 4 LYS L 20 GLY L 26 -1 O THR L 24 N THR L 5 SHEET 3 AA1 4 GLU L 70 THR L 74 -1 O LEU L 73 N LEU L 21 SHEET 4 AA1 4 GLY L 64 SER L 67 -1 N SER L 65 O TYR L 72 SHEET 1 AA2 3 ARG L 45 ARG L 49 0 SHEET 2 AA2 3 ALA L 34 GLN L 37 -1 N GLN L 37 O ARG L 45 SHEET 3 AA2 3 CYS L 88 GLN L 89 -1 O GLN L 89 N ALA L 34 SHEET 1 AA3 4 GLN H 3 SER H 7 0 SHEET 2 AA3 4 THR H 17 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA3 4 GLN H 77 SER H 82A-1 O LEU H 80 N LEU H 20 SHEET 4 AA3 4 VAL H 67 THR H 68 -1 N THR H 68 O SER H 81 SHEET 1 AA4 3 GLU H 46 ILE H 51 0 SHEET 2 AA4 3 TRP H 35 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 3 AA4 3 VAL H 89 ARG H 94 -1 O VAL H 89 N GLN H 39 SHEET 1 AA5 7 TRP H 100I ARG H 100K 0 SHEET 2 AA5 7 GLU H 100 GLU H 100C-1 N TYS H 100B O TYR H 100J SHEET 3 AA5 7 LYS G 168 TYR G 177 -1 O LYS G 169 N TYR H 100A SHEET 4 AA5 7 MET G 154 THR G 162 -1 N LYS G 155 O PHE G 176 SHEET 5 AA5 7 LEU G 129 THR G 132 -1 N ASN G 130 O SER G 158 SHEET 6 AA5 7 LYS G 190 LEU G 193 -1 O TYR G 191 N LEU G 129 SHEET 7 AA5 7 ILE G 181 VAL G 182 -1 N VAL G 182 O ARG G 192 SHEET 1 AA6 6 GLU G 83 MET G 84 0 SHEET 2 AA6 6 SER G 243 VAL G 245 -1 O THR G 244 N MET G 84 SHEET 3 AA6 6 TYR G 223 LYS G 227 -1 N LYS G 227 O SER G 243 SHEET 4 AA6 6 TYR G 486 THR G 499 -1 O VAL G 489 N ALA G 224 SHEET 5 AA6 6 TRP G 35 GLU G 47 -1 N VAL G 44 O LYS G 492 SHEET 6 AA6 6 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL G 38 SHEET 1 AA7 3 VAL G 75 PRO G 76 0 SHEET 2 AA7 3 PHE G 53 SER G 56 1 N SER G 56 O VAL G 75 SHEET 3 AA7 3 HIS G 216 CYS G 218 -1 O HIS G 216 N ALA G 55 SHEET 1 AA8 2 GLU G 91 ASN G 94 0 SHEET 2 AA8 2 THR G 236 CYS G 239 -1 O CYS G 239 N GLU G 91 SHEET 1 AA9 7 LEU G 259 LEU G 261 0 SHEET 2 AA9 7 THR G 444 ARG G 456 -1 O THR G 450 N LEU G 260 SHEET 3 AA9 7 ILE G 284 THR G 297 -1 N VAL G 292 O ILE G 449 SHEET 4 AA9 7 HIS G 330 SER G 334 -1 O ASN G 332 N VAL G 295 SHEET 5 AA9 7 THR G 413 ILE G 420 -1 O ILE G 414 N ILE G 333 SHEET 6 AA9 7 GLU G 381 CYS G 385 -1 N TYR G 384 O ARG G 419 SHEET 7 AA9 7 HIS G 374 CYS G 378 -1 N HIS G 374 O CYS G 385 SHEET 1 AB1 6 ILE G 271 ARG G 273 0 SHEET 2 AB1 6 ILE G 284 THR G 297 -1 O ILE G 285 N ARG G 273 SHEET 3 AB1 6 THR G 444 ARG G 456 -1 O ILE G 449 N VAL G 292 SHEET 4 AB1 6 GLU G 466 PRO G 470 -1 O ARG G 469 N THR G 455 SHEET 5 AB1 6 ILE G 359 PHE G 361 1 N THR G 360 O GLU G 466 SHEET 6 AB1 6 THR G 394 TYR G 395 -1 O TYR G 395 N ILE G 359 SHEET 1 AB2 2 ARG G 304 GLY G 312 0 SHEET 2 AB2 2 GLN G 315 LEU G 320 -1 O PHE G 317 N ILE G 307 SHEET 1 AB3 3 LEU A 494 THR A 499 0 SHEET 2 AB3 3 TRP A 35 TYR A 40 -1 N TYR A 39 O GLY A 495 SHEET 3 AB3 3 ILE C 603 PRO C 609 -1 O THR C 606 N VAL A 36 SHEET 1 AB4 5 TRP A 45 GLU A 47 0 SHEET 2 AB4 5 VAL A 488 ILE A 491 -1 O GLU A 490 N LYS A 46 SHEET 3 AB4 5 TYR A 223 LYS A 227 -1 N ALA A 224 O VAL A 489 SHEET 4 AB4 5 SER A 243 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AB4 5 GLU A 83 VAL A 85 -1 N MET A 84 O THR A 244 SHEET 1 AB5 2 PHE A 53 ALA A 55 0 SHEET 2 AB5 2 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AB6 2 GLU A 91 ASN A 94 0 SHEET 2 AB6 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AB7 3 LEU A 129 THR A 132 0 SHEET 2 AB7 3 MET A 154 THR A 162 -1 O SER A 158 N ASN A 130 SHEET 3 AB7 3 LYS A 169 TYR A 177 -1 O ALA A 174 N CYS A 157 SHEET 1 AB8 2 ILE A 181 VAL A 182 0 SHEET 2 AB8 2 ARG A 192 LEU A 193 -1 O ARG A 192 N VAL A 182 SHEET 1 AB9 6 LEU A 259 LEU A 261 0 SHEET 2 AB9 6 ILE A 443 ARG A 456 -1 O THR A 450 N LEU A 260 SHEET 3 AB9 6 THR A 283 ARG A 298 -1 N ILE A 284 O LEU A 454 SHEET 4 AB9 6 GLU A 466 PRO A 470 0 SHEET 5 AB9 6 ILE A 359 PHE A 361 1 N THR A 360 O GLU A 466 SHEET 6 AB9 6 GLY A 393 TYR A 395 -1 O GLY A 393 N PHE A 361 SHEET 1 AC1 5 ILE A 271 ARG A 273 0 SHEET 2 AC1 5 THR A 283 ARG A 298 -1 O HIS A 287 N ILE A 271 SHEET 3 AC1 5 ILE A 443 ARG A 456 -1 O LEU A 454 N ILE A 284 SHEET 4 AC1 5 HIS A 330 SER A 334 0 SHEET 5 AC1 5 THR A 413 THR A 415 -1 O ILE A 414 N ILE A 333 SHEET 1 AC2 2 MET A 302 GLY A 312 0 SHEET 2 AC2 2 GLN A 315 ILE A 322 -1 O GLY A 321 N THR A 303 SHEET 1 AC3 3 HIS A 374 CYS A 378 0 SHEET 2 AC3 3 GLU A 381 CYS A 385 -1 O CYS A 385 N HIS A 374 SHEET 3 AC3 3 CYS A 418 ILE A 420 -1 O ARG A 419 N TYR A 384 SHEET 1 AC4 2 ILE A 423 ILE A 424 0 SHEET 2 AC4 2 MET A 434 TYR A 435 -1 O MET A 434 N ILE A 424 SHEET 1 AC5 3 LEU D 494 THR D 499 0 SHEET 2 AC5 3 TRP D 35 TYR D 40 -1 N TRP D 35 O THR D 499 SHEET 3 AC5 3 ILE E 603 PRO E 609 -1 O VAL E 608 N VAL D 36 SHEET 1 AC6 5 TRP D 45 GLU D 47 0 SHEET 2 AC6 5 TYR D 486 ILE D 491 -1 O GLU D 490 N LYS D 46 SHEET 3 AC6 5 TYR D 223 LYS D 227 -1 N LEU D 226 O LYS D 487 SHEET 4 AC6 5 SER D 243 VAL D 245 -1 O SER D 243 N LYS D 227 SHEET 5 AC6 5 GLU D 83 VAL D 85 -1 N MET D 84 O THR D 244 SHEET 1 AC7 2 PHE D 53 ALA D 55 0 SHEET 2 AC7 2 HIS D 216 CYS D 218 -1 O HIS D 216 N ALA D 55 SHEET 1 AC8 2 GLU D 91 ASN D 94 0 SHEET 2 AC8 2 THR D 236 CYS D 239 -1 O CYS D 239 N GLU D 91 SHEET 1 AC9 3 ASN D 130 ASN D 133 0 SHEET 2 AC9 3 MET D 154 THR D 162 -1 O SER D 158 N ASN D 130 SHEET 3 AC9 3 LYS D 169 TYR D 177 -1 O ALA D 174 N CYS D 157 SHEET 1 AD1 2 ILE D 181 VAL D 182 0 SHEET 2 AD1 2 ARG D 192 LEU D 193 -1 O ARG D 192 N VAL D 182 SHEET 1 AD2 4 LEU D 259 LEU D 261 0 SHEET 2 AD2 4 ILE D 449 ARG D 456 -1 O GLY D 451 N LEU D 260 SHEET 3 AD2 4 ILE D 284 HIS D 287 -1 N ILE D 284 O LEU D 454 SHEET 4 AD2 4 ILE D 271 ARG D 273 -1 N ARG D 273 O ILE D 285 SHEET 1 AD3 5 LEU D 259 LEU D 261 0 SHEET 2 AD3 5 ILE D 449 ARG D 456 -1 O GLY D 451 N LEU D 260 SHEET 3 AD3 5 GLU D 465 PRO D 470 -1 O ARG D 469 N THR D 455 SHEET 4 AD3 5 ASN D 358 PHE D 361 1 N ASN D 358 O GLU D 466 SHEET 5 AD3 5 GLY D 393 TYR D 395 -1 O TYR D 395 N ILE D 359 SHEET 1 AD4 6 ASN D 377 CYS D 378 0 SHEET 2 AD4 6 GLU D 381 CYS D 385 -1 O GLU D 381 N CYS D 378 SHEET 3 AD4 6 THR D 413 ILE D 420 -1 O ARG D 419 N TYR D 384 SHEET 4 AD4 6 HIS D 330 SER D 334 -1 N ILE D 333 O ILE D 414 SHEET 5 AD4 6 ILE D 294 ARG D 298 -1 N VAL D 295 O ASN D 332 SHEET 6 AD4 6 ILE D 443 SER D 447 -1 O SER D 447 N ILE D 294 SHEET 1 AD5 2 MET D 302 ARG D 308 0 SHEET 2 AD5 2 THR D 316 ILE D 322 -1 O GLY D 321 N THR D 303 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 2 CYS H 22 CYS H 92 1555 1555 2.04 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 2.03 SSBOND 8 CYS G 218 CYS G 247 1555 1555 2.04 SSBOND 9 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 10 CYS G 296 CYS G 331 1555 1555 2.04 SSBOND 11 CYS G 378 CYS G 445 1555 1555 2.04 SSBOND 12 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 13 CYS G 501 CYS B 605 1555 1555 2.03 SSBOND 14 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 15 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 16 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 17 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 18 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 19 CYS A 201 CYS A 433 1555 1555 2.03 SSBOND 20 CYS A 218 CYS A 247 1555 1555 2.04 SSBOND 21 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 22 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 23 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 24 CYS A 385 CYS A 418 1555 1555 2.05 SSBOND 25 CYS A 501 CYS C 605 1555 1555 2.03 SSBOND 26 CYS C 598 CYS C 604 1555 1555 2.03 SSBOND 27 CYS D 54 CYS D 74 1555 1555 2.03 SSBOND 28 CYS D 119 CYS D 205 1555 1555 2.03 SSBOND 29 CYS D 126 CYS D 196 1555 1555 2.03 SSBOND 30 CYS D 131 CYS D 157 1555 1555 2.03 SSBOND 31 CYS D 201 CYS D 433 1555 1555 2.03 SSBOND 32 CYS D 218 CYS D 247 1555 1555 2.04 SSBOND 33 CYS D 228 CYS D 239 1555 1555 2.03 SSBOND 34 CYS D 296 CYS D 331 1555 1555 2.04 SSBOND 35 CYS D 378 CYS D 445 1555 1555 2.03 SSBOND 36 CYS D 385 CYS D 418 1555 1555 2.03 SSBOND 37 CYS D 501 CYS E 605 1555 1555 2.03 SSBOND 38 CYS E 598 CYS E 604 1555 1555 2.03 LINK C TYR H 100A N TYS H 100B 1555 1555 1.33 LINK C TYS H 100B N GLU H 100C 1555 1555 1.33 LINK C ASP H 100E N TYS H 100F 1555 1555 1.33 LINK C TYS H 100F N ASP H 100G 1555 1555 1.33 LINK ND2 ASN G 88 C1 NAG G 611 1555 1555 1.45 LINK ND2 ASN G 130 C1 NAG G 601 1555 1555 1.45 LINK ND2 ASN G 133 C1 NAG G 612 1555 1555 1.45 LINK ND2 ASN G 156 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN G 160 C1 NAG P 1 1555 1555 1.46 LINK ND2 ASN G 230 C1 NAG G 602 1555 1555 1.44 LINK ND2 ASN G 241 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN G 276 C1 NAG G 604 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG G 606 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG G 607 1555 1555 1.44 LINK ND2 ASN G 339 C1 NAG N 1 1555 1555 1.46 LINK ND2 ASN G 358 C1 NAG K 1 1555 1555 1.45 LINK ND2 ASN G 386 C1 NAG G 608 1555 1555 1.45 LINK ND2 ASN G 392 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN G 398 C1 NAG G 615 1555 1555 1.46 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 616 C1 NAG B 703 1555 1555 1.44 LINK ND2 ASN B 625 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 88 C1 NAG A 611 1555 1555 1.44 LINK ND2 ASN A 130 C1 NAG A 601 1555 1555 1.45 LINK ND2 ASN A 133 C1 NAG A 612 1555 1555 1.46 LINK ND2 ASN A 156 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN A 230 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 241 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG A 606 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG A 607 1555 1555 1.45 LINK ND2 ASN A 358 C1 NAG A 615 1555 1555 1.45 LINK ND2 ASN A 386 C1 NAG A 608 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG X 1 1555 1555 1.45 LINK ND2 ASN A 442 C1 NAG A 609 1555 1555 1.45 LINK ND2 ASN A 448 C1 NAG A 610 1555 1555 1.44 LINK ND2 ASN C 611 C1 NAG C 701 1555 1555 1.44 LINK ND2 ASN C 616 C1 NAG C 703 1555 1555 1.46 LINK ND2 ASN C 625 C1 NAG C 702 1555 1555 1.45 LINK ND2 ASN C 637 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN D 88 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN D 130 C1 NAG D 601 1555 1555 1.44 LINK ND2 ASN D 133 C1 NAG D 611 1555 1555 1.45 LINK ND2 ASN D 156 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN D 160 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN D 230 C1 NAG D 602 1555 1555 1.44 LINK ND2 ASN D 241 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN D 262 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN D 276 C1 NAG D 604 1555 1555 1.44 LINK ND2 ASN D 301 C1 NAG D 606 1555 1555 1.44 LINK ND2 ASN D 332 C1 NAG D 607 1555 1555 1.45 LINK ND2 ASN D 386 C1 NAG D 608 1555 1555 1.44 LINK ND2 ASN D 392 C1 NAG m 1 1555 1555 1.44 LINK ND2 ASN D 398 C1 NAG j 1 1555 1555 1.45 LINK ND2 ASN D 448 C1 NAG D 610 1555 1555 1.44 LINK ND2 ASN E 611 C1 NAG E 701 1555 1555 1.44 LINK ND2 ASN E 616 C1 NAG E 703 1555 1555 1.46 LINK ND2 ASN E 625 C1 NAG E 702 1555 1555 1.45 LINK ND2 ASN E 637 C1 NAG o 1 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.45 LINK O6 BMA I 3 C1 MAN I 5 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.47 LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.46 LINK O6 BMA N 3 C1 MAN N 5 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 1.44 LINK O6 BMA O 3 C1 MAN O 4 1555 1555 1.45 LINK O3 BMA O 3 C1 MAN O 7 1555 1555 1.46 LINK O3 MAN O 4 C1 MAN O 5 1555 1555 1.45 LINK O6 MAN O 4 C1 MAN O 6 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.45 LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.45 LINK O6 BMA P 3 C1 MAN P 6 1555 1555 1.45 LINK O2 MAN P 4 C1 MAN P 5 1555 1555 1.45 LINK O3 MAN P 6 C1 MAN P 7 1555 1555 1.46 LINK O6 MAN P 6 C1 MAN P 8 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.44 LINK O3 BMA T 3 C1 MAN T 4 1555 1555 1.45 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 BMA U 3 C1 MAN U 8 1555 1555 1.45 LINK O6 MAN U 4 C1 MAN U 5 1555 1555 1.45 LINK O3 MAN U 4 C1 MAN U 7 1555 1555 1.45 LINK O2 MAN U 5 C1 MAN U 6 1555 1555 1.44 LINK O2 MAN U 8 C1 MAN U 9 1555 1555 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.46 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 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.44 LINK O3 BMA d 3 C1 MAN d 4 1555 1555 1.45 LINK O6 BMA d 3 C1 MAN d 5 1555 1555 1.45 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.45 LINK O3 BMA e 3 C1 MAN e 4 1555 1555 1.45 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 6 1555 1555 1.45 LINK O2 MAN f 4 C1 MAN f 5 1555 1555 1.45 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.44 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.45 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 m 2 C1 BMA m 3 1555 1555 1.46 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 O3 BMA n 3 C1 MAN n 4 1555 1555 1.45 LINK O6 BMA n 3 C1 MAN n 5 1555 1555 1.45 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.44 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