HEADER VIRAL PROTEIN/IMMUNE SYSTEM 02-MAY-24 9BNK TITLE CRYO-EM STRUCTURE OF RHESUS ANTIBODY V031-A.01 IN COMPLEX WITH HIV-1 TITLE 2 ENV BG505 DS-SOSIP COMPND MOL_ID: 1; COMPND 2 MOLECULE: V031-A.01 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: V031-A.01 LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HUMAN IMMUNODEFICIENCY VIRUS 1 ENVELOPE GLYCOPROTEIN GP120; COMPND 11 CHAIN: G, E, F; 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, A; COMPND 17 SYNONYM: ENV POLYPROTEIN; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 4 ORGANISM_TAXID: 9544; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 10 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 11 ORGANISM_TAXID: 9544; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 17 ORGANISM_TAXID: 11676; SOURCE 18 GENE: ENV; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 24 ORGANISM_TAXID: 11676; SOURCE 25 GENE: ENV; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NEUTRALIZING ANTIBODY, HIV-1 V2 APEX, SHIV-ELICITED, VIRAL PROTEIN, KEYWDS 2 IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.S.ROARK,L.SHAPIRO,P.D.KWONG REVDAT 1 07-MAY-25 9BNK 0 JRNL AUTH R.S.ROARK,L.SHAPIRO,P.D.KWONG JRNL TITL HIV-1 NEUTRALIZING ANTIBODIES IN SHIV-INFECTED MACAQUES 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. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.100 REMARK 3 NUMBER OF PARTICLES : 353856 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9BNK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000283665. 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 : COMPLEX OF V031-A.01 WITH HIV-1 REMARK 245 BG505 ENVELOPE TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 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) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5800.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, G, B, E, F, C, A, D, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 ARG H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLU H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 SER H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 VAL H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 ARG H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 ILE H 213 REMARK 465 LYS H 214 REMARK 465 THR H 215 REMARK 465 CYS H 216 REMARK 465 GLY H 217 REMARK 465 GLY H 218 REMARK 465 GLY H 219 REMARK 465 LEU H 220 REMARK 465 GLU H 221 REMARK 465 VAL H 222 REMARK 465 LEU H 223 REMARK 465 PHE H 224 REMARK 465 GLN H 225 REMARK 465 ARG L 108 REMARK 465 THR L 109 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 GLU L 122 REMARK 465 ASP L 123 REMARK 465 GLN L 124 REMARK 465 VAL L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 VAL L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 SER L 145 REMARK 465 VAL L 146 REMARK 465 LYS L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 GLY L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 LYS L 155 REMARK 465 THR L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 ASN L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 SER L 183 REMARK 465 THR L 184 REMARK 465 GLU L 185 REMARK 465 TYR L 186 REMARK 465 GLN L 187 REMARK 465 SER L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 ALA G 60 REMARK 465 TYR G 61 REMARK 465 GLU G 62 REMARK 465 THR G 63 REMARK 465 GLU G 64 REMARK 465 GLU G 185A REMARK 465 ASN G 185B REMARK 465 GLN G 185C REMARK 465 GLY G 185D REMARK 465 ASN G 185E REMARK 465 ARG G 185F REMARK 465 SER G 185G REMARK 465 ASN G 185H REMARK 465 ASN G 185I REMARK 465 SER G 185J REMARK 465 ASN G 185K REMARK 465 SER G 401 REMARK 465 VAL G 402 REMARK 465 GLN G 403 REMARK 465 GLY G 404 REMARK 465 SER G 405 REMARK 465 ASN G 406 REMARK 465 SER G 407 REMARK 465 THR G 408 REMARK 465 GLY G 409 REMARK 465 SER G 410 REMARK 465 ASN G 411 REMARK 465 VAL B 518 REMARK 465 PHE B 519 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 ILE 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 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 LYS E 65 REMARK 465 GLU E 185A REMARK 465 ASN E 185B REMARK 465 GLN E 185C REMARK 465 GLY E 185D REMARK 465 ASN E 185E REMARK 465 ARG E 185F REMARK 465 SER E 185G REMARK 465 ASN E 185H REMARK 465 ASN E 185I REMARK 465 SER E 185J REMARK 465 THR E 400 REMARK 465 SER E 401 REMARK 465 VAL E 402 REMARK 465 GLN E 403 REMARK 465 GLY E 404 REMARK 465 SER E 405 REMARK 465 ASN E 406 REMARK 465 SER E 407 REMARK 465 THR E 408 REMARK 465 GLY E 409 REMARK 465 SER E 410 REMARK 465 LYS F 59 REMARK 465 ALA F 60 REMARK 465 TYR F 61 REMARK 465 GLU F 62 REMARK 465 THR F 63 REMARK 465 GLU F 64 REMARK 465 LYS F 65 REMARK 465 THR F 400 REMARK 465 SER F 401 REMARK 465 VAL F 402 REMARK 465 GLN F 403 REMARK 465 GLY F 404 REMARK 465 SER F 405 REMARK 465 ASN F 406 REMARK 465 SER F 407 REMARK 465 THR F 408 REMARK 465 GLY F 409 REMARK 465 SER F 410 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 ILE 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 LEU C 565 REMARK 465 LEU C 566 REMARK 465 LYS C 567 REMARK 465 LEU C 568 REMARK 465 VAL A 518 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 ARG A 557 REMARK 465 ALA A 558 REMARK 465 ILE A 559 REMARK 465 GLU A 560 REMARK 465 ALA A 561 REMARK 465 GLN A 562 REMARK 465 GLN A 563 REMARK 465 HIS A 564 REMARK 465 LEU A 565 REMARK 465 LEU A 566 REMARK 465 LYS A 567 REMARK 465 LEU A 568 REMARK 465 ASN A 625 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 ARG G 480 CB - CA - C ANGL. DEV. = -13.9 DEGREES REMARK 500 ASP B 659 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS F 501 CA - CB - SG ANGL. DEV. = 7.1 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 LEU H 48 -62.54 -94.62 REMARK 500 ASN H 54 31.26 -92.38 REMARK 500 TYS H 100D -74.99 -69.70 REMARK 500 SER H 100M 40.72 -105.18 REMARK 500 VAL L 51 -49.36 65.91 REMARK 500 ASN G 88 17.71 56.48 REMARK 500 LEU G 122 33.86 -97.01 REMARK 500 THR G 198 -166.95 -124.35 REMARK 500 PRO G 253 45.56 -81.16 REMARK 500 LYS G 282 7.30 80.01 REMARK 500 ASN G 283 72.01 56.30 REMARK 500 SER G 364 161.56 -48.78 REMARK 500 SER B 615 -30.07 -130.74 REMARK 500 ALA E 73 52.57 -92.87 REMARK 500 LEU E 122 35.20 -99.96 REMARK 500 ASN E 136 62.67 64.69 REMARK 500 THR E 198 -140.80 -92.39 REMARK 500 TRP E 427 -160.85 62.13 REMARK 500 CYS E 433 -168.53 178.70 REMARK 500 ASN E 462 29.29 43.56 REMARK 500 LEU E 483 35.08 -96.66 REMARK 500 THR F 71 -10.57 69.72 REMARK 500 HIS F 72 12.87 54.88 REMARK 500 LEU F 122 36.21 -99.95 REMARK 500 THR F 163 -168.78 -101.22 REMARK 500 ASN F 187G 74.63 -103.08 REMARK 500 PHE F 353 -169.85 -119.30 REMARK 500 MET F 426 -16.18 70.43 REMARK 500 TRP F 427 36.53 -142.44 REMARK 500 CYS F 433 -168.37 -104.29 REMARK 500 THR F 465 62.85 38.39 REMARK 500 LEU F 483 31.52 -95.74 REMARK 500 TYR C 638 20.81 -140.58 REMARK 500 LEU A 523 19.63 50.54 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44728 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF RHESUS ANTIBODY V031-A.01 IN COMPLEX WITH HIV- REMARK 900 1 ENV BG505 DS-SOSIP DBREF 9BNK H 1 225 PDB 9BNK 9BNK 1 225 DBREF 9BNK L 1 214 PDB 9BNK 9BNK 1 214 DBREF 9BNK G 32 506 UNP Q2N0S6 Q2N0S6_9HIV1 31 503 DBREF 9BNK B 518 664 UNP Q2N0S6 Q2N0S6_9HIV1 515 661 DBREF 9BNK E 32 506 UNP Q2N0S6 Q2N0S6_9HIV1 31 503 DBREF 9BNK F 32 506 UNP Q2N0S6 Q2N0S6_9HIV1 31 503 DBREF 9BNK C 518 664 UNP Q2N0S6 Q2N0S6_9HIV1 515 661 DBREF 9BNK A 518 664 UNP Q2N0S6 Q2N0S6_9HIV1 515 661 SEQADV 9BNK CYS G 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 9BNK ASN G 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 9BNK CYS G 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 9BNK CYS G 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 9BNK CYS B 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9BNK CYS E 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 9BNK ASN E 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 9BNK CYS E 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 9BNK CYS E 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 9BNK CYS F 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 9BNK ASN F 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 9BNK CYS F 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 9BNK CYS F 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 9BNK CYS C 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9BNK CYS A 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 H 248 LEU VAL THR LEU LYS GLU SER GLY PRO ALA LEU VAL THR SEQRES 2 H 248 PRO THR GLN THR LEU THR LEU THR CYS THR LEU SER GLY SEQRES 3 H 248 PHE SER LEU THR THR THR GLY MET ARG VAL ASN TRP ILE SEQRES 4 H 248 ARG GLN ALA PRO GLY LYS ALA LEU GLU TRP LEU ALA ARG SEQRES 5 H 248 ILE ASP TYR ASN GLU ALA ARG PHE TYR SER SER SER LEU SEQRES 6 H 248 LYS THR ARG LEU SER ILE SER THR ASP ALA SER LYS ASN SEQRES 7 H 248 GLN VAL VAL LEU ARG MET THR ASN MET ALA PRO VAL ASP SEQRES 8 H 248 THR GLY THR TYR TYR CYS ALA ARG SER GLN GLN HIS TYR SEQRES 9 H 248 TYR GLU ASP ALA TYS THR PHE ASP TRP TYR TYR PHE HIS SEQRES 10 H 248 SER ARG ASP ASN GLY LEU ASP SER TRP GLY GLN GLY VAL SEQRES 11 H 248 VAL VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 12 H 248 VAL PHE PRO LEU ALA PRO SER SER ARG SER THR SER GLU SEQRES 13 H 248 SER THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 14 H 248 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SER LEU SEQRES 15 H 248 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 16 H 248 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 17 H 248 SER SER SER LEU GLY THR GLN THR TYR VAL CYS ASN VAL SEQRES 18 H 248 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 19 H 248 GLU ILE LYS THR CYS GLY GLY GLY LEU GLU VAL LEU PHE SEQRES 20 H 248 GLN SEQRES 1 L 219 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 L 219 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 219 GLN SER LEU LEU ASP SER ASP GLY TYR THR HIS LEU SER SEQRES 4 L 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 219 ILE SER LEU VAL SER ASN ARG ALA SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 LYS LEU ASN ARG VAL GLU ALA GLU ASP VAL GLY LEU TYR SEQRES 8 L 219 TYR CYS MET GLN GLY LEU GLN THR PRO TYR THR PHE GLY SEQRES 9 L 219 GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER GLU ASP GLN VAL SEQRES 11 L 219 LYS SER GLY THR VAL SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA SER VAL LYS TRP LYS VAL ASP SEQRES 13 L 219 GLY ALA LEU LYS THR GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP ASN THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER SER THR GLU TYR GLN SER HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 473 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 G 473 TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP SEQRES 3 G 473 ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA SEQRES 4 G 473 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 G 473 ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP SEQRES 6 G 473 LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SEQRES 7 G 473 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 G 473 THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR SEQRES 9 G 473 ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN SEQRES 10 G 473 CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS SEQRES 11 G 473 GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL SEQRES 12 G 473 GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER SEQRES 13 G 473 ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA SEQRES 14 G 473 CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 15 G 473 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 16 G 473 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 17 G 473 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 18 G 473 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 19 G 473 ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR SEQRES 20 G 473 ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO SEQRES 21 G 473 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG SEQRES 22 G 473 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA SEQRES 23 G 473 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 24 G 473 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 25 G 473 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 26 G 473 ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU SEQRES 27 G 473 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 28 G 473 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 29 G 473 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 30 G 473 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 31 G 473 ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR ALA SEQRES 32 G 473 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 33 G 473 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 34 G 473 SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 35 G 473 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 36 G 473 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 37 G 473 LYS ARG ARG VAL VAL SEQRES 1 B 147 VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET SEQRES 2 B 147 GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG ASN SEQRES 3 B 147 LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN LEU LEU SEQRES 4 B 147 ARG ALA ILE GLU ALA GLN GLN HIS LEU LEU LYS LEU THR SEQRES 5 B 147 VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA SEQRES 6 B 147 VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE SEQRES 7 B 147 TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL SEQRES 8 B 147 PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SER GLU SEQRES 9 B 147 ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU SEQRES 10 B 147 ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU SEQRES 11 B 147 GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU SEQRES 12 B 147 LEU ALA LEU ASP SEQRES 1 E 473 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 E 473 TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP SEQRES 3 E 473 ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA SEQRES 4 E 473 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 E 473 ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP SEQRES 6 E 473 LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SEQRES 7 E 473 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 E 473 THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR SEQRES 9 E 473 ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN SEQRES 10 E 473 CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS SEQRES 11 E 473 GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL SEQRES 12 E 473 GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER SEQRES 13 E 473 ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA SEQRES 14 E 473 CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 15 E 473 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 16 E 473 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 17 E 473 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 18 E 473 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 19 E 473 ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR SEQRES 20 E 473 ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO SEQRES 21 E 473 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG SEQRES 22 E 473 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA SEQRES 23 E 473 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 24 E 473 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 25 E 473 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 26 E 473 ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU SEQRES 27 E 473 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 28 E 473 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 29 E 473 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 30 E 473 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 31 E 473 ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR ALA SEQRES 32 E 473 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 33 E 473 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 34 E 473 SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 35 E 473 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 36 E 473 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 37 E 473 LYS ARG ARG VAL VAL SEQRES 1 F 473 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 F 473 TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP SEQRES 3 F 473 ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA SEQRES 4 F 473 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 F 473 ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP SEQRES 6 F 473 LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SEQRES 7 F 473 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 F 473 THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR SEQRES 9 F 473 ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN SEQRES 10 F 473 CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS SEQRES 11 F 473 GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL SEQRES 12 F 473 GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER SEQRES 13 F 473 ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA SEQRES 14 F 473 CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 15 F 473 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 16 F 473 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 17 F 473 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 18 F 473 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 19 F 473 ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR SEQRES 20 F 473 ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO SEQRES 21 F 473 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG SEQRES 22 F 473 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA SEQRES 23 F 473 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 24 F 473 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 25 F 473 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 26 F 473 ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU SEQRES 27 F 473 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 28 F 473 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 29 F 473 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 30 F 473 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 31 F 473 ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR ALA SEQRES 32 F 473 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 33 F 473 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 34 F 473 SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 35 F 473 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 36 F 473 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 37 F 473 LYS ARG ARG VAL VAL SEQRES 1 C 147 VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET SEQRES 2 C 147 GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG ASN SEQRES 3 C 147 LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN LEU LEU SEQRES 4 C 147 ARG ALA ILE GLU ALA GLN GLN HIS LEU LEU LYS LEU THR SEQRES 5 C 147 VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA SEQRES 6 C 147 VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE SEQRES 7 C 147 TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL SEQRES 8 C 147 PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SER GLU SEQRES 9 C 147 ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU SEQRES 10 C 147 ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU SEQRES 11 C 147 GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU SEQRES 12 C 147 LEU ALA LEU ASP SEQRES 1 A 147 VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET SEQRES 2 A 147 GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG ASN SEQRES 3 A 147 LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN LEU LEU SEQRES 4 A 147 ARG ALA ILE GLU ALA GLN GLN HIS LEU LEU LYS LEU THR SEQRES 5 A 147 VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA SEQRES 6 A 147 VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE SEQRES 7 A 147 TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL SEQRES 8 A 147 PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SER GLU SEQRES 9 A 147 ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU SEQRES 10 A 147 ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU SEQRES 11 A 147 GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU SEQRES 12 A 147 LEU ALA LEU ASP HET TYS H 100D 16 HET NAG D 1 14 HET NAG D 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 J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HET MAN K 4 11 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 NAG O 1 14 HET NAG O 2 14 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 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 NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET MAN V 5 11 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 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 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 B 701 14 HET NAG B 702 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG E 606 14 HET NAG E 607 14 HET NAG E 608 14 HET NAG E 609 14 HET NAG E 610 14 HET NAG E 611 14 HET NAG E 612 14 HET NAG E 613 14 HET NAG E 614 14 HET NAG F 601 14 HET NAG F 602 14 HET NAG F 603 14 HET NAG F 604 14 HET NAG F 605 14 HET NAG F 606 14 HET NAG F 607 14 HET NAG F 608 14 HET NAG F 609 14 HET NAG F 610 14 HET NAG C 701 14 HET NAG C 702 14 HET NAG A 701 14 HET NAG A 702 14 HET NAG A 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 1 TYS C9 H11 N O6 S FORMUL 9 NAG 77(C8 H15 N O6) FORMUL 10 BMA 8(C6 H12 O6) FORMUL 10 MAN 8(C6 H12 O6) HELIX 1 AA1 ALA H 83 THR H 87 5 5 HELIX 2 AA2 ASN G 98 LYS G 117 1 20 HELIX 3 AA3 LEU G 122 CYS G 126 5 5 HELIX 4 AA4 LYS G 335 GLY G 354 1 20 HELIX 5 AA5 ASP G 368 THR G 373 1 6 HELIX 6 AA6 THR G 387 LEU G 390 5 4 HELIX 7 AA7 ASP G 474 SER G 481 1 8 HELIX 8 AA8 THR B 529 SER B 534 1 6 HELIX 9 AA9 LEU B 537 ARG B 542 1 6 HELIX 10 AB1 ASN B 543 LEU B 545 5 3 HELIX 11 AB2 THR B 569 ILE B 595 1 27 HELIX 12 AB3 ASN B 611 SER B 615 5 5 HELIX 13 AB4 LEU B 619 ASP B 624 1 6 HELIX 14 AB5 THR B 627 LYS B 633 1 7 HELIX 15 AB6 TYR B 638 LEU B 663 1 26 HELIX 16 AB7 ASN E 98 LYS E 117 1 20 HELIX 17 AB8 LEU E 122 CYS E 126 5 5 HELIX 18 AB9 LYS E 335 ARG E 350 1 16 HELIX 19 AC1 LYS E 351 PHE E 353 5 3 HELIX 20 AC2 ASP E 368 THR E 373 1 6 HELIX 21 AC3 THR E 387 LEU E 390 5 4 HELIX 22 AC4 SER E 460 THR E 464 5 5 HELIX 23 AC5 MET E 475 LEU E 483 1 9 HELIX 24 AC6 ASN F 98 LYS F 117 1 20 HELIX 25 AC7 LEU F 122 CYS F 126 5 5 HELIX 26 AC8 ASN F 195 ASN F 197 5 3 HELIX 27 AC9 LYS F 335 PHE F 353 1 19 HELIX 28 AD1 ASP F 368 THR F 373 1 6 HELIX 29 AD2 MET F 475 SER F 481 1 7 HELIX 30 AD3 THR C 529 SER C 534 1 6 HELIX 31 AD4 LEU C 537 ASN C 543 1 7 HELIX 32 AD5 VAL C 570 ILE C 595 1 26 HELIX 33 AD6 ASN C 611 ASN C 616 1 6 HELIX 34 AD7 LEU C 619 ASN C 625 1 7 HELIX 35 AD8 THR C 627 SER C 636 1 10 HELIX 36 AD9 TYR C 638 LEU C 661 1 24 HELIX 37 AE1 THR A 529 SER A 534 1 6 HELIX 38 AE2 LEU A 537 ARG A 542 1 6 HELIX 39 AE3 VAL A 570 TRP A 596 1 27 HELIX 40 AE4 ASN A 611 ASN A 616 1 6 HELIX 41 AE5 ASN A 618 ASP A 624 1 7 HELIX 42 AE6 THR A 627 SER A 636 1 10 HELIX 43 AE7 TYR A 638 LEU A 661 1 24 SHEET 1 AA1 4 THR H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 23 N LYS H 5 SHEET 3 AA1 4 GLN H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 LEU H 67 ASP H 72 -1 N SER H 68 O ARG H 81 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 VAL H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 GLY H 88 GLN H 96 -1 N TYR H 90 O VAL H 107 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N GLN H 39 O THR H 89 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O LEU H 48 N TRP H 36 SHEET 6 AA2 6 ARG H 57 TYR H 59 -1 O PHE H 58 N ARG H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 VAL H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 GLY H 88 GLN H 96 -1 N TYR H 90 O VAL H 107 SHEET 4 AA3 4 LEU H 100R TRP H 103 -1 O SER H 102 N ARG H 94 SHEET 1 AA4 2 TYR H 100 GLU H 100A 0 SHEET 2 AA4 2 TRP H 100H TYR H 100I-1 O TYR H 100I N TYR H 100 SHEET 1 AA5 4 MET L 4 THR L 7 0 SHEET 2 AA5 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA5 4 ASP L 70 LEU L 75 -1 O LEU L 75 N ALA L 19 SHEET 4 AA5 4 SER L 65 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AA6 6 SER L 10 VAL L 13 0 SHEET 2 AA6 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA6 6 GLY L 84 GLN L 90 -1 N GLY L 84 O VAL L 104 SHEET 4 AA6 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA6 6 GLN L 45 SER L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA6 6 ASN L 53 ARG L 54 -1 O ASN L 53 N SER L 49 SHEET 1 AA7 3 GLY G 495 THR G 499 0 SHEET 2 AA7 3 TRP G 35 TYR G 39 -1 N TYR G 39 O GLY G 495 SHEET 3 AA7 3 ILE B 603 CYS B 604 -1 O CYS B 604 N VAL G 38 SHEET 1 AA8 5 TRP G 45 ASP G 47 0 SHEET 2 AA8 5 TYR G 486 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 AA8 5 PHE G 223 CYS G 228 -1 N ALA G 224 O VAL G 489 SHEET 4 AA8 5 VAL G 242 VAL G 245 -1 O SER G 243 N LYS G 227 SHEET 5 AA8 5 GLU G 83 LEU G 86 -1 N ILE G 84 O THR G 244 SHEET 1 AA9 2 GLU G 91 ASN G 94 0 SHEET 2 AA9 2 THR G 236 CYS G 239 -1 O CYS G 239 N GLU G 91 SHEET 1 AB1 3 LEU G 129 GLN G 130 0 SHEET 2 AB1 3 GLU G 190 LEU G 193 -1 O TYR G 191 N LEU G 129 SHEET 3 AB1 3 VAL G 181 GLN G 183 -1 N VAL G 182 O ARG G 192 SHEET 1 AB2 2 LEU G 154 THR G 162 0 SHEET 2 AB2 2 LYS G 169 TYR G 177 -1 O GLN G 170 N MET G 161 SHEET 1 AB3 3 THR G 202 GLN G 203 0 SHEET 2 AB3 3 MET G 434 TYR G 435 1 O TYR G 435 N THR G 202 SHEET 3 AB3 3 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AB4 7 LEU G 259 LEU G 261 0 SHEET 2 AB4 7 GLY G 441 LEU G 452 -1 O THR G 450 N LEU G 260 SHEET 3 AB4 7 VAL G 292 ASN G 302 -1 N ASN G 302 O GLY G 441 SHEET 4 AB4 7 HIS G 330 SER G 334 -1 O HIS G 330 N THR G 297 SHEET 5 AB4 7 SER G 413 LYS G 421 -1 O ILE G 414 N VAL G 333 SHEET 6 AB4 7 GLU G 381 CYS G 385 -1 N TYR G 384 O ARG G 419 SHEET 7 AB4 7 HIS G 374 CYS G 378 -1 N HIS G 374 O CYS G 385 SHEET 1 AB5 2 MET G 271 ARG G 273 0 SHEET 2 AB5 2 LEU G 285 GLN G 287 -1 O LEU G 285 N ARG G 273 SHEET 1 AB6 2 ARG G 304 GLY G 312 0 SHEET 2 AB6 2 GLN G 315 THR G 320 -1 O PHE G 317 N ILE G 307 SHEET 1 AB7 4 SER G 393 TRP G 395 0 SHEET 2 AB7 4 ILE G 359 PHE G 361 -1 N ILE G 359 O TRP G 395 SHEET 3 AB7 4 GLU G 466 PRO G 470 1 O PHE G 468 N ARG G 360 SHEET 4 AB7 4 LEU G 454 ARG G 456 -1 N THR G 455 O ARG G 469 SHEET 1 AB8 6 GLU E 83 LEU E 86 0 SHEET 2 AB8 6 VAL E 242 VAL E 245 -1 O THR E 244 N ILE E 84 SHEET 3 AB8 6 PHE E 223 CYS E 228 -1 N LYS E 227 O SER E 243 SHEET 4 AB8 6 TYR E 486 THR E 499 -1 O VAL E 489 N ALA E 224 SHEET 5 AB8 6 TRP E 35 LYS E 46 -1 N TRP E 35 O THR E 499 SHEET 6 AB8 6 ILE C 603 PRO C 609 -1 O CYS C 604 N VAL E 38 SHEET 1 AB9 2 GLU E 91 ASN E 94 0 SHEET 2 AB9 2 THR E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 AC1 5 LYS E 169 TYR E 177 0 SHEET 2 AC1 5 LEU E 154 THR E 162 -1 N CYS E 157 O SER E 174 SHEET 3 AC1 5 LEU E 129 ASN E 133 -1 N THR E 132 O ASN E 156 SHEET 4 AC1 5 LYS E 189 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC1 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC2 3 THR E 202 GLN E 203 0 SHEET 2 AC2 3 MET E 434 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC2 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC3 7 LEU E 259 LEU E 261 0 SHEET 2 AC3 7 ILE E 443 ARG E 456 -1 O GLY E 451 N LEU E 260 SHEET 3 AC3 7 ILE E 284 ARG E 298 -1 N VAL E 292 O ILE E 449 SHEET 4 AC3 7 HIS E 330 SER E 334 -1 O HIS E 330 N THR E 297 SHEET 5 AC3 7 SER E 413 LYS E 421 -1 O ILE E 414 N VAL E 333 SHEET 6 AC3 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AC3 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 AC4 6 MET E 271 ARG E 273 0 SHEET 2 AC4 6 ILE E 284 ARG E 298 -1 O LEU E 285 N ARG E 273 SHEET 3 AC4 6 ILE E 443 ARG E 456 -1 O ILE E 449 N VAL E 292 SHEET 4 AC4 6 GLU E 466 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AC4 6 ILE E 359 PHE E 361 1 N ARG E 360 O PHE E 468 SHEET 6 AC4 6 SER E 393 TRP E 395 -1 O SER E 393 N PHE E 361 SHEET 1 AC5 2 ASN E 302 ILE E 307 0 SHEET 2 AC5 2 PHE E 317 ILE E 322 -1 O ALA E 319 N LYS E 305 SHEET 1 AC6 3 LEU F 494 THR F 499 0 SHEET 2 AC6 3 TRP F 35 TYR F 40 -1 N TRP F 35 O THR F 499 SHEET 3 AC6 3 ILE A 603 PRO A 609 -1 O VAL A 608 N VAL F 36 SHEET 1 AC7 5 TRP F 45 LYS F 46 0 SHEET 2 AC7 5 TYR F 486 ILE F 491 -1 O LYS F 490 N LYS F 46 SHEET 3 AC7 5 PHE F 223 CYS F 228 -1 N ALA F 224 O VAL F 489 SHEET 4 AC7 5 VAL F 242 VAL F 245 -1 O SER F 243 N LYS F 227 SHEET 5 AC7 5 GLU F 83 LEU F 86 -1 N LEU F 86 O VAL F 242 SHEET 1 AC8 2 GLU F 91 ASN F 94 0 SHEET 2 AC8 2 THR F 236 CYS F 239 -1 O CYS F 239 N GLU F 91 SHEET 1 AC9 3 LEU F 129 CYS F 131 0 SHEET 2 AC9 3 LYS F 189 LEU F 193 -1 O TYR F 191 N LEU F 129 SHEET 3 AC9 3 VAL F 181 GLN F 183 -1 N VAL F 182 O ARG F 192 SHEET 1 AD1 2 LEU F 154 THR F 162 0 SHEET 2 AD1 2 LYS F 169 TYR F 177 -1 O GLN F 170 N MET F 161 SHEET 1 AD2 3 THR F 202 GLN F 203 0 SHEET 2 AD2 3 MET F 434 TYR F 435 1 O TYR F 435 N THR F 202 SHEET 3 AD2 3 ILE F 423 ILE F 424 -1 N ILE F 424 O MET F 434 SHEET 1 AD3 7 LEU F 259 LEU F 261 0 SHEET 2 AD3 7 GLY F 441 ARG F 456 -1 O GLY F 451 N LEU F 260 SHEET 3 AD3 7 ASN F 283 ASN F 302 -1 N ILE F 284 O LEU F 454 SHEET 4 AD3 7 HIS F 330 SER F 334 -1 O HIS F 330 N THR F 297 SHEET 5 AD3 7 SER F 413 ILE F 420 -1 O ILE F 414 N VAL F 333 SHEET 6 AD3 7 GLU F 381 CYS F 385 -1 N TYR F 384 O ARG F 419 SHEET 7 AD3 7 HIS F 374 CYS F 378 -1 N CYS F 378 O GLU F 381 SHEET 1 AD4 6 MET F 271 ARG F 273 0 SHEET 2 AD4 6 ASN F 283 ASN F 302 -1 O GLN F 287 N MET F 271 SHEET 3 AD4 6 GLY F 441 ARG F 456 -1 O LEU F 454 N ILE F 284 SHEET 4 AD4 6 GLU F 466 PRO F 470 -1 O ARG F 469 N THR F 455 SHEET 5 AD4 6 ILE F 359 PHE F 361 1 N ARG F 360 O GLU F 466 SHEET 6 AD4 6 SER F 393 TRP F 395 -1 O TRP F 395 N ILE F 359 SHEET 1 AD5 2 ARG F 304 ILE F 307 0 SHEET 2 AD5 2 PHE F 317 THR F 320 -1 O PHE F 317 N ILE F 307 SSBOND 1 CYS G 54 CYS G 74 1555 1555 2.03 SSBOND 2 CYS G 119 CYS G 205 1555 1555 2.03 SSBOND 3 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 4 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 5 CYS G 201 CYS G 433 1555 1555 2.03 SSBOND 6 CYS G 218 CYS G 247 1555 1555 1.81 SSBOND 7 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 8 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 9 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 10 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 11 CYS G 501 CYS B 605 1555 1555 2.04 SSBOND 12 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 13 CYS E 54 CYS E 74 1555 1555 2.04 SSBOND 14 CYS E 119 CYS E 205 1555 1555 2.04 SSBOND 15 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 16 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 17 CYS E 201 CYS E 433 1555 1555 1.98 SSBOND 18 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 19 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 20 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 21 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 22 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 23 CYS E 501 CYS C 605 1555 1555 2.03 SSBOND 24 CYS F 54 CYS F 74 1555 1555 1.99 SSBOND 25 CYS F 119 CYS F 205 1555 1555 2.04 SSBOND 26 CYS F 126 CYS F 196 1555 1555 2.03 SSBOND 27 CYS F 131 CYS F 157 1555 1555 2.03 SSBOND 28 CYS F 201 CYS F 433 1555 1555 2.03 SSBOND 29 CYS F 218 CYS F 247 1555 1555 2.03 SSBOND 30 CYS F 228 CYS F 239 1555 1555 2.03 SSBOND 31 CYS F 296 CYS F 331 1555 1555 2.03 SSBOND 32 CYS F 378 CYS F 445 1555 1555 2.03 SSBOND 33 CYS F 385 CYS F 418 1555 1555 2.03 SSBOND 34 CYS F 501 CYS A 605 1555 1555 1.96 SSBOND 35 CYS C 598 CYS C 604 1555 1555 2.03 SSBOND 36 CYS A 598 CYS A 604 1555 1555 2.03 LINK C ALA H 100C N TYS H 100D 1555 1555 1.33 LINK C TYS H 100D N THR H 100E 1555 1555 1.33 LINK ND2 ASN G 88 C1 NAG J 1 1555 1555 1.45 LINK ND2 ASN G 133 C1 NAG G 601 1555 1555 1.44 LINK ND2 ASN G 156 C1 NAG K 1 1555 1555 1.45 LINK ND2 ASN G 160 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN G 197 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN G 234 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN G 262 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN G 276 C1 NAG G 602 1555 1555 1.46 LINK ND2 ASN G 295 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG G 603 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG G 604 1555 1555 1.44 LINK ND2 ASN G 339 C1 NAG G 605 1555 1555 1.44 LINK ND2 ASN G 355 C1 NAG G 606 1555 1555 1.44 LINK ND2 ASN G 363 C1 NAG G 607 1555 1555 1.43 LINK ND2 ASN G 386 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN G 392 C1 NAG G 608 1555 1555 1.45 LINK ND2 ASN G 448 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 133 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG E 603 1555 1555 1.42 LINK ND2 ASN E 234 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG E 606 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG E 608 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 609 1555 1555 1.44 LINK ND2 ASN E 355 C1 NAG E 610 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG E 611 1555 1555 1.45 LINK ND2 ASN E 386 C1 NAG E 612 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG E 613 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 614 1555 1555 1.44 LINK ND2 ASN F 88 C1 NAG F 601 1555 1555 1.44 LINK ND2 ASN F 133 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN F 156 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN F 160 C1 NAG I 1 1555 1555 1.42 LINK ND2 ASN F 197 C1 NAG F 602 1555 1555 1.44 LINK ND2 ASN F 234 C1 NAG F 603 1555 1555 1.44 LINK ND2 ASN F 262 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN F 276 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN F 295 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN F 301 C1 NAG F 604 1555 1555 1.44 LINK ND2 ASN F 332 C1 NAG F 605 1555 1555 1.44 LINK ND2 ASN F 339 C1 NAG F 606 1555 1555 1.44 LINK ND2 ASN F 355 C1 NAG F 607 1555 1555 1.45 LINK ND2 ASN F 363 C1 NAG F 608 1555 1555 1.44 LINK ND2 ASN F 386 C1 NAG F 609 1555 1555 1.44 LINK ND2 ASN F 392 C1 NAG F 610 1555 1555 1.44 LINK ND2 ASN F 448 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN C 611 C1 NAG C 701 1555 1555 1.44 LINK ND2 ASN C 618 C1 NAG C 702 1555 1555 1.44 LINK ND2 ASN A 611 C1 NAG A 701 1555 1555 1.42 LINK ND2 ASN A 618 C1 NAG A 702 1555 1555 1.47 LINK ND2 ASN A 637 C1 NAG A 703 1555 1555 1.47 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.39 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.39 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.39 LINK O6 BMA I 3 C1 MAN I 6 1555 1555 1.40 LINK O2 MAN I 4 C1 MAN I 5 1555 1555 1.39 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.39 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.39 LINK O3 BMA K 3 C1 MAN K 4 1555 1555 1.39 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.45 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG 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 5 1555 1555 1.45 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 U 1 C1 NAG U 2 1555 1555 1.45 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.45 LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.45 LINK O6 BMA V 3 C1 MAN V 5 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 CISPEP 1 THR L 7 PRO L 8 0 -0.72 CISPEP 2 THR L 94 PRO L 95 0 -0.56 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