HEADER VIRAL PROTEIN/IMMUNE SYSTEM 28-JUL-22 8DVD TITLE CRYO-EM STRUCTURE OF SIVMAC239 SOS-2P ENV TRIMER IN COMPLEX WITH HUMAN TITLE 2 BNAB PGT145 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 8 CHAIN: E, F, G; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: PGT145 HEAVY; COMPND 12 CHAIN: H; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: PGT145 LIGHT; COMPND 16 CHAIN: L; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SIMIAN IMMUNODEFICIENCY VIRUS; SOURCE 3 ORGANISM_TAXID: 11723; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: SIMIAN IMMUNODEFICIENCY VIRUS; SOURCE 9 ORGANISM_TAXID: 11723; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 4; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS CD4, HIV-1, SOSIP, VACCINE, IMMUNE SYSTEM, SIV, VIRAL PROTEIN, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR J.GORMAN,P.D.KWONG JRNL AUTH J.GORMAN,P.D.KWONG JRNL TITL CRYO-EM STRUCTURES OF PREFUSION SIV ENVELOPE TRIMER JRNL REF NAT.STRUCT.MOL.BIOL. 2022 JRNL REFN ESSN 1545-9985 JRNL DOI 10.1038/S41594-022-00852-1 REMARK 2 REMARK 2 RESOLUTION. 4.12 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6TYB 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) : 4.120 REMARK 3 NUMBER OF PARTICLES : 61881 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 8DVD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000267398. 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 : SIVMAC239 SOS-2P IN COMPLEX REMARK 245 WITH PGT145 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 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) : 51.15 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: A, B, C, E, F, G, H, L, D, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, j, k, l, REMARK 350 AND CHAINS: m, n, o, p, q, r, s, t, u, v, REMARK 350 AND CHAINS: w, x, y, z, 0, 1, 2, 3, 4, REMARK 350 AND CHAINS: 5, 6, 7, 8, 9, AA, BA, CA, REMARK 350 AND CHAINS: DA, EA, FA, GA, HA, IA, JA, REMARK 350 AND CHAINS: KA, LA, MA, NA, OA, PA, QA, REMARK 350 AND CHAINS: RA REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 VAL A 558 REMARK 465 PRO A 559 REMARK 465 LYS A 560 REMARK 465 ARG A 561 REMARK 465 GLN A 562 REMARK 465 GLN A 563 REMARK 465 GLU A 564 REMARK 465 LEU A 565 REMARK 465 LEU A 566 REMARK 465 ARG A 567 REMARK 465 LEU A 568 REMARK 465 PRO A 569 REMARK 465 VAL A 570 REMARK 465 TRP A 571 REMARK 465 VAL B 558 REMARK 465 PRO B 559 REMARK 465 LYS B 560 REMARK 465 ARG B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 GLU B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 ARG B 567 REMARK 465 LEU B 568 REMARK 465 PRO B 569 REMARK 465 VAL B 570 REMARK 465 VAL C 558 REMARK 465 PRO C 559 REMARK 465 LYS C 560 REMARK 465 ARG C 561 REMARK 465 GLN C 562 REMARK 465 GLN C 563 REMARK 465 GLU C 564 REMARK 465 LEU C 565 REMARK 465 LEU C 566 REMARK 465 ARG C 567 REMARK 465 LEU C 568 REMARK 465 PRO C 569 REMARK 465 VAL C 570 REMARK 465 THR E 506 REMARK 465 GLY E 507 REMARK 465 GLY E 508 REMARK 465 THR E 509 REMARK 465 SER E 510 REMARK 465 ARG E 511 REMARK 465 THR F 506 REMARK 465 GLY F 507 REMARK 465 GLY F 508 REMARK 465 THR F 509 REMARK 465 SER F 510 REMARK 465 ARG F 511 REMARK 465 THR G 506 REMARK 465 GLY G 507 REMARK 465 GLY G 508 REMARK 465 THR G 509 REMARK 465 SER G 510 REMARK 465 ARG G 511 REMARK 465 ALA H 119 REMARK 465 SER H 120 REMARK 465 THR H 121 REMARK 465 LYS H 122 REMARK 465 GLY H 123 REMARK 465 PRO H 124 REMARK 465 SER H 125 REMARK 465 VAL H 126 REMARK 465 PHE H 127 REMARK 465 PRO H 128 REMARK 465 LEU H 129 REMARK 465 ALA H 130 REMARK 465 PRO H 131 REMARK 465 SER H 132 REMARK 465 SER H 133 REMARK 465 LYS H 134 REMARK 465 SER H 135 REMARK 465 THR H 136 REMARK 465 SER H 137 REMARK 465 GLY H 138 REMARK 465 GLY H 139 REMARK 465 THR H 140 REMARK 465 ALA H 141 REMARK 465 ALA H 142 REMARK 465 LEU H 143 REMARK 465 GLY H 144 REMARK 465 CYS H 145 REMARK 465 LEU H 146 REMARK 465 VAL H 147 REMARK 465 LYS H 148 REMARK 465 ASP H 149 REMARK 465 TYR H 150 REMARK 465 PHE H 151 REMARK 465 PRO H 152 REMARK 465 GLU H 153 REMARK 465 PRO H 154 REMARK 465 VAL H 155 REMARK 465 THR H 156 REMARK 465 VAL H 157 REMARK 465 SER H 158 REMARK 465 TRP H 159 REMARK 465 ASN H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 ALA H 163 REMARK 465 LEU H 164 REMARK 465 THR H 165 REMARK 465 SER H 166 REMARK 465 GLY H 167 REMARK 465 VAL H 168 REMARK 465 HIS H 169 REMARK 465 THR H 170 REMARK 465 PHE H 171 REMARK 465 PRO H 172 REMARK 465 ALA H 173 REMARK 465 VAL H 174 REMARK 465 LEU H 175 REMARK 465 GLN H 176 REMARK 465 SER H 177 REMARK 465 SER H 178 REMARK 465 GLY H 179 REMARK 465 LEU H 180 REMARK 465 TYR H 181 REMARK 465 SER H 182 REMARK 465 LEU H 183 REMARK 465 SER H 184 REMARK 465 SER H 185 REMARK 465 VAL H 186 REMARK 465 VAL H 187 REMARK 465 THR H 188 REMARK 465 VAL H 189 REMARK 465 PRO H 190 REMARK 465 SER H 191 REMARK 465 SER H 192 REMARK 465 SER H 193 REMARK 465 LEU H 194 REMARK 465 GLY H 195 REMARK 465 THR H 196 REMARK 465 GLN H 197 REMARK 465 THR H 198 REMARK 465 TYR H 199 REMARK 465 ILE H 200 REMARK 465 CYS H 201 REMARK 465 ASN H 202 REMARK 465 VAL H 203 REMARK 465 ASN H 204 REMARK 465 HIS H 205 REMARK 465 LYS H 206 REMARK 465 PRO H 207 REMARK 465 SER H 208 REMARK 465 ASN H 209 REMARK 465 THR H 210 REMARK 465 LYS H 211 REMARK 465 VAL H 212 REMARK 465 ASP H 213 REMARK 465 LYS H 214 REMARK 465 LYS H 215 REMARK 465 VAL H 216 REMARK 465 GLU H 217 REMARK 465 PRO H 218 REMARK 465 LYS H 219 REMARK 465 SER H 220 REMARK 465 CYS H 221 REMARK 465 ASP H 222 REMARK 465 GLU L 1 REMARK 465 ARG L 108 REMARK 465 THR L 109 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 ASP L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 LYS L 145 REMARK 465 VAL L 146 REMARK 465 GLN L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 SER L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 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 O3 NAGKA 1 O5 NAGKA 2 1.93 REMARK 500 O3 NAGNA 1 O5 NAGNA 2 2.05 REMARK 500 O3 NAG e 1 O5 NAG e 2 2.06 REMARK 500 O3 NAG 2 1 O5 NAG 2 2 2.06 REMARK 500 O3 NAG T 2 O5 BMA T 3 2.10 REMARK 500 OG1 THR B 606 O VAL G 36 2.11 REMARK 500 O THR G 253 OH TYR G 479 2.13 REMARK 500 O TRP E 460 O6 NAG j 1 2.13 REMARK 500 O3 NAGJA 2 O5 BMAJA 3 2.16 REMARK 500 O3 NAG o 2 O5 BMA o 3 2.16 REMARK 500 OH TYR E 290 OE1 GLU E 344 2.16 REMARK 500 O3 NAG z 1 O5 NAG z 2 2.18 REMARK 500 N LEU B 537 OE2 GLU C 654 2.19 REMARK 500 O3 NAG r 2 O2 BMA r 3 2.19 REMARK 500 O3 NAG k 2 O5 BMA k 3 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS G 205 CA - CB - SG ANGL. DEV. = 10.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN A 554 -4.03 69.32 REMARK 500 ASN A 575 -168.88 -79.01 REMARK 500 PRO A 611 -167.07 -71.24 REMARK 500 ASN A 612 126.75 -34.77 REMARK 500 GLN B 554 -4.58 69.38 REMARK 500 ASN B 575 -63.98 -92.84 REMARK 500 PRO B 611 -169.01 -71.25 REMARK 500 ASN B 612 124.85 -36.38 REMARK 500 THR C 538 -0.53 73.40 REMARK 500 GLN C 554 -3.11 68.92 REMARK 500 LEU C 576 32.21 -97.48 REMARK 500 PRO C 611 -167.79 -72.15 REMARK 500 ASN C 612 125.79 -35.38 REMARK 500 THR E 71 -8.63 74.68 REMARK 500 ASN E 88 53.31 -90.60 REMARK 500 THR E 144C -129.33 58.73 REMARK 500 THR E 144D -147.49 43.43 REMARK 500 ALA E 144N -99.02 54.75 REMARK 500 ASP E 149I -122.83 60.63 REMARK 500 THR E 149L -6.50 73.56 REMARK 500 ASN E 160 -62.49 -94.72 REMARK 500 MET E 161 70.19 56.90 REMARK 500 GLU E 203 -179.82 -66.27 REMARK 500 TYR E 209 -3.58 72.38 REMARK 500 TRP E 258 -8.21 73.52 REMARK 500 MET E 310 46.03 -80.41 REMARK 500 PHE E 333 -95.20 56.73 REMARK 500 ARG E 354 -162.17 58.97 REMARK 500 GLN E 405 -136.67 56.78 REMARK 500 LYS E 429 -69.05 -94.95 REMARK 500 VAL E 430 -60.13 -134.10 REMARK 500 LYS E 432 179.58 82.40 REMARK 500 GLN E 466 66.39 60.03 REMARK 500 TYR E 504 -159.99 60.35 REMARK 500 THR F 68 -41.18 -130.79 REMARK 500 THR F 71 -7.15 74.02 REMARK 500 GLN F 73 22.59 -143.54 REMARK 500 ASN F 88 52.49 -94.11 REMARK 500 THR F 144C -130.30 59.76 REMARK 500 THR F 144D -147.42 43.35 REMARK 500 ALA F 144N 68.61 61.78 REMARK 500 LYS F 144O 178.20 -59.93 REMARK 500 ASP F 149I -113.44 57.46 REMARK 500 THR F 149L -2.11 71.21 REMARK 500 GLN F 153 20.46 -145.46 REMARK 500 MET F 161 74.03 58.98 REMARK 500 SER F 199 144.67 -171.20 REMARK 500 MET F 237 108.71 -56.41 REMARK 500 TRP F 258 -7.97 73.91 REMARK 500 ASP F 279 -166.68 -162.44 REMARK 500 REMARK 500 THIS ENTRY HAS 86 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 CYS G 119 VAL G 120 -146.52 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 MAN F 601 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-27631 RELATED DB: EMDB REMARK 900 SAME CONSTRUCT WITH JACALIN REMARK 900 RELATED ID: 8DUA RELATED DB: PDB REMARK 900 ALTERNATE STRAIN REMARK 900 RELATED ID: EMD-27735 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF SIVMAC239 SOS-2P ENV TRIMER IN COMPLEX WITH REMARK 900 HUMAN BNAB PGT145 DBREF1 8DVD A 512 664 UNP A0A0C5JYT4_SIV DBREF2 8DVD A A0A0C5JYT4 401 548 DBREF1 8DVD B 512 664 UNP A0A0C5JYT4_SIV DBREF2 8DVD B A0A0C5JYT4 401 548 DBREF1 8DVD C 512 664 UNP A0A0C5JYT4_SIV DBREF2 8DVD C A0A0C5JYT4 401 548 DBREF1 8DVD E 33 511 UNP A0A4Y5TGK0_SIV DBREF2 8DVD E A0A4Y5TGK0 23 522 DBREF1 8DVD F 33 511 UNP A0A4Y5TGK0_SIV DBREF2 8DVD F A0A4Y5TGK0 23 522 DBREF1 8DVD G 33 511 UNP A0A4Y5TGK0_SIV DBREF2 8DVD G A0A4Y5TGK0 23 522 DBREF 8DVD H 1 222 PDB 8DVD 8DVD 1 222 DBREF 8DVD L 1 214 PDB 8DVD 8DVD 1 214 SEQADV 8DVD PRO A 559 UNP A0A0C5JYT VAL 447 CONFLICT SEQADV 8DVD PRO A 569 UNP A0A0C5JYT THR 457 CONFLICT SEQADV 8DVD CYS A 605 UNP A0A0C5JYT HIS 493 CONFLICT SEQADV 8DVD PRO B 559 UNP A0A0C5JYT VAL 447 CONFLICT SEQADV 8DVD PRO B 569 UNP A0A0C5JYT THR 457 CONFLICT SEQADV 8DVD CYS B 605 UNP A0A0C5JYT HIS 493 CONFLICT SEQADV 8DVD PRO C 559 UNP A0A0C5JYT VAL 447 CONFLICT SEQADV 8DVD PRO C 569 UNP A0A0C5JYT THR 457 CONFLICT SEQADV 8DVD CYS C 605 UNP A0A0C5JYT HIS 493 CONFLICT SEQADV 8DVD THR E 169 UNP A0A4Y5TGK LYS 180 CONFLICT SEQADV 8DVD CYS E 501 UNP A0A4Y5TGK VAL 512 CONFLICT SEQADV 8DVD THR F 169 UNP A0A4Y5TGK LYS 180 CONFLICT SEQADV 8DVD CYS F 501 UNP A0A4Y5TGK VAL 512 CONFLICT SEQADV 8DVD THR G 169 UNP A0A4Y5TGK LYS 180 CONFLICT SEQADV 8DVD CYS G 501 UNP A0A4Y5TGK VAL 512 CONFLICT SEQRES 1 A 148 GLY VAL PHE VAL LEU GLY PHE LEU GLY PHE LEU ALA THR SEQRES 2 A 148 ALA GLY SER ALA MET GLY ALA ALA SER LEU THR LEU THR SEQRES 3 A 148 ALA GLN SER ARG THR LEU LEU ALA GLY ILE VAL GLN GLN SEQRES 4 A 148 GLN GLN GLN LEU LEU ASP VAL PRO LYS ARG GLN GLN GLU SEQRES 5 A 148 LEU LEU ARG LEU PRO VAL TRP GLY THR LYS ASN LEU GLN SEQRES 6 A 148 THR ARG VAL THR ALA ILE GLU LYS TYR LEU LYS ASP GLN SEQRES 7 A 148 ALA GLN LEU ASN ALA TRP GLY CYS ALA PHE ARG GLN VAL SEQRES 8 A 148 CYS CYS THR THR VAL PRO TRP PRO ASN ALA SER LEU THR SEQRES 9 A 148 PRO LYS TRP ASN ASN GLU THR TRP GLN GLU TRP GLU ARG SEQRES 10 A 148 LYS VAL ASP PHE LEU GLU GLU ASN ILE THR ALA LEU LEU SEQRES 11 A 148 GLU GLU ALA GLN ILE GLN GLN GLU LYS ASN MET TYR GLU SEQRES 12 A 148 LEU GLN LYS LEU ASN SEQRES 1 B 148 GLY VAL PHE VAL LEU GLY PHE LEU GLY PHE LEU ALA THR SEQRES 2 B 148 ALA GLY SER ALA MET GLY ALA ALA SER LEU THR LEU THR SEQRES 3 B 148 ALA GLN SER ARG THR LEU LEU ALA GLY ILE VAL GLN GLN SEQRES 4 B 148 GLN GLN GLN LEU LEU ASP VAL PRO LYS ARG GLN GLN GLU SEQRES 5 B 148 LEU LEU ARG LEU PRO VAL TRP GLY THR LYS ASN LEU GLN SEQRES 6 B 148 THR ARG VAL THR ALA ILE GLU LYS TYR LEU LYS ASP GLN SEQRES 7 B 148 ALA GLN LEU ASN ALA TRP GLY CYS ALA PHE ARG GLN VAL SEQRES 8 B 148 CYS CYS THR THR VAL PRO TRP PRO ASN ALA SER LEU THR SEQRES 9 B 148 PRO LYS TRP ASN ASN GLU THR TRP GLN GLU TRP GLU ARG SEQRES 10 B 148 LYS VAL ASP PHE LEU GLU GLU ASN ILE THR ALA LEU LEU SEQRES 11 B 148 GLU GLU ALA GLN ILE GLN GLN GLU LYS ASN MET TYR GLU SEQRES 12 B 148 LEU GLN LYS LEU ASN SEQRES 1 C 148 GLY VAL PHE VAL LEU GLY PHE LEU GLY PHE LEU ALA THR SEQRES 2 C 148 ALA GLY SER ALA MET GLY ALA ALA SER LEU THR LEU THR SEQRES 3 C 148 ALA GLN SER ARG THR LEU LEU ALA GLY ILE VAL GLN GLN SEQRES 4 C 148 GLN GLN GLN LEU LEU ASP VAL PRO LYS ARG GLN GLN GLU SEQRES 5 C 148 LEU LEU ARG LEU PRO VAL TRP GLY THR LYS ASN LEU GLN SEQRES 6 C 148 THR ARG VAL THR ALA ILE GLU LYS TYR LEU LYS ASP GLN SEQRES 7 C 148 ALA GLN LEU ASN ALA TRP GLY CYS ALA PHE ARG GLN VAL SEQRES 8 C 148 CYS CYS THR THR VAL PRO TRP PRO ASN ALA SER LEU THR SEQRES 9 C 148 PRO LYS TRP ASN ASN GLU THR TRP GLN GLU TRP GLU ARG SEQRES 10 C 148 LYS VAL ASP PHE LEU GLU GLU ASN ILE THR ALA LEU LEU SEQRES 11 C 148 GLU GLU ALA GLN ILE GLN GLN GLU LYS ASN MET TYR GLU SEQRES 12 C 148 LEU GLN LYS LEU ASN SEQRES 1 E 500 THR LEU TYR VAL THR VAL PHE TYR GLY VAL PRO ALA TRP SEQRES 2 E 500 ARG ASN ALA THR ILE PRO LEU PHE CYS ALA THR LYS ASN SEQRES 3 E 500 ARG ASP THR TRP GLY THR THR GLN CYS LEU PRO ASP ASN SEQRES 4 E 500 GLY ASP TYR SER GLU VAL ALA LEU ASN VAL THR GLU SER SEQRES 5 E 500 PHE ASP ALA TRP ASN ASN THR VAL THR GLU GLN ALA ILE SEQRES 6 E 500 GLU ASP VAL TRP GLN LEU PHE GLU THR SER ILE LYS PRO SEQRES 7 E 500 CYS VAL LYS LEU SER PRO LEU CYS ILE THR MET ARG CYS SEQRES 8 E 500 ASN LYS SER GLU THR ASP ARG TRP GLY LEU THR LYS SER SEQRES 9 E 500 ILE THR THR THR ALA SER THR THR SER THR THR ALA SER SEQRES 10 E 500 ALA LYS VAL ASP MET VAL ASN GLU THR SER SER CYS ILE SEQRES 11 E 500 ALA GLN ASP ASN CYS THR GLY LEU GLU GLN GLU GLN MET SEQRES 12 E 500 ILE SER CYS LYS PHE ASN MET THR GLY LEU LYS ARG ASP SEQRES 13 E 500 LYS THR LYS GLU TYR ASN GLU THR TRP TYR SER ALA ASP SEQRES 14 E 500 LEU VAL CYS GLU GLN GLY ASN ASN THR GLY ASN GLU SER SEQRES 15 E 500 ARG CYS TYR MET ASN HIS CYS ASN THR SER VAL ILE GLN SEQRES 16 E 500 GLU SER CYS ASP LYS HIS TYR TRP ASP ALA ILE ARG PHE SEQRES 17 E 500 ARG TYR CYS ALA PRO PRO GLY TYR ALA LEU LEU ARG CYS SEQRES 18 E 500 ASN ASP THR ASN TYR SER GLY PHE MET PRO LYS CYS SER SEQRES 19 E 500 LYS VAL VAL VAL SER SER CYS THR ARG MET MET GLU THR SEQRES 20 E 500 GLN THR SER THR TRP PHE GLY PHE ASN GLY THR ARG ALA SEQRES 21 E 500 GLU ASN ARG THR TYR ILE TYR TRP HIS GLY ARG ASP ASN SEQRES 22 E 500 ARG THR ILE ILE SER LEU ASN LYS TYR TYR ASN LEU THR SEQRES 23 E 500 MET LYS CYS ARG ARG PRO GLY ASN LYS THR VAL LEU PRO SEQRES 24 E 500 VAL THR ILE MET SER GLY LEU VAL PHE HIS SER GLN PRO SEQRES 25 E 500 ILE ASN ASP ARG PRO LYS GLN ALA TRP CYS TRP PHE GLY SEQRES 26 E 500 GLY LYS TRP LYS ASP ALA ILE LYS GLU VAL LYS GLN THR SEQRES 27 E 500 ILE VAL LYS HIS PRO ARG TYR THR GLY THR ASN ASN THR SEQRES 28 E 500 ASP LYS ILE ASN LEU THR ALA PRO GLY GLY GLY ASP PRO SEQRES 29 E 500 GLU VAL THR PHE MET TRP THR ASN CYS ARG GLY GLU PHE SEQRES 30 E 500 LEU TYR CYS LYS MET ASN TRP PHE LEU ASN TRP VAL GLU SEQRES 31 E 500 ASP ARG ASN THR ALA ASN GLN LYS PRO LYS GLU GLN HIS SEQRES 32 E 500 LYS ARG ASN TYR VAL PRO CYS HIS ILE ARG GLN ILE ILE SEQRES 33 E 500 ASN THR TRP HIS LYS VAL GLY LYS ASN VAL TYR LEU PRO SEQRES 34 E 500 PRO ARG GLU GLY ASP LEU THR CYS ASN SER THR VAL THR SEQRES 35 E 500 SER LEU ILE ALA ASN ILE ASP TRP ILE ASP GLY ASN GLN SEQRES 36 E 500 THR ASN ILE THR MET SER ALA GLU VAL ALA GLU LEU TYR SEQRES 37 E 500 ARG LEU GLU LEU GLY ASP TYR LYS LEU VAL GLU ILE THR SEQRES 38 E 500 PRO ILE GLY LEU ALA PRO THR ASP CYS LYS ARG TYR THR SEQRES 39 E 500 THR GLY GLY THR SER ARG SEQRES 1 F 500 THR LEU TYR VAL THR VAL PHE TYR GLY VAL PRO ALA TRP SEQRES 2 F 500 ARG ASN ALA THR ILE PRO LEU PHE CYS ALA THR LYS ASN SEQRES 3 F 500 ARG ASP THR TRP GLY THR THR GLN CYS LEU PRO ASP ASN SEQRES 4 F 500 GLY ASP TYR SER GLU VAL ALA LEU ASN VAL THR GLU SER SEQRES 5 F 500 PHE ASP ALA TRP ASN ASN THR VAL THR GLU GLN ALA ILE SEQRES 6 F 500 GLU ASP VAL TRP GLN LEU PHE GLU THR SER ILE LYS PRO SEQRES 7 F 500 CYS VAL LYS LEU SER PRO LEU CYS ILE THR MET ARG CYS SEQRES 8 F 500 ASN LYS SER GLU THR ASP ARG TRP GLY LEU THR LYS SER SEQRES 9 F 500 ILE THR THR THR ALA SER THR THR SER THR THR ALA SER SEQRES 10 F 500 ALA LYS VAL ASP MET VAL ASN GLU THR SER SER CYS ILE SEQRES 11 F 500 ALA GLN ASP ASN CYS THR GLY LEU GLU GLN GLU GLN MET SEQRES 12 F 500 ILE SER CYS LYS PHE ASN MET THR GLY LEU LYS ARG ASP SEQRES 13 F 500 LYS THR LYS GLU TYR ASN GLU THR TRP TYR SER ALA ASP SEQRES 14 F 500 LEU VAL CYS GLU GLN GLY ASN ASN THR GLY ASN GLU SER SEQRES 15 F 500 ARG CYS TYR MET ASN HIS CYS ASN THR SER VAL ILE GLN SEQRES 16 F 500 GLU SER CYS ASP LYS HIS TYR TRP ASP ALA ILE ARG PHE SEQRES 17 F 500 ARG TYR CYS ALA PRO PRO GLY TYR ALA LEU LEU ARG CYS SEQRES 18 F 500 ASN ASP THR ASN TYR SER GLY PHE MET PRO LYS CYS SER SEQRES 19 F 500 LYS VAL VAL VAL SER SER CYS THR ARG MET MET GLU THR SEQRES 20 F 500 GLN THR SER THR TRP PHE GLY PHE ASN GLY THR ARG ALA SEQRES 21 F 500 GLU ASN ARG THR TYR ILE TYR TRP HIS GLY ARG ASP ASN SEQRES 22 F 500 ARG THR ILE ILE SER LEU ASN LYS TYR TYR ASN LEU THR SEQRES 23 F 500 MET LYS CYS ARG ARG PRO GLY ASN LYS THR VAL LEU PRO SEQRES 24 F 500 VAL THR ILE MET SER GLY LEU VAL PHE HIS SER GLN PRO SEQRES 25 F 500 ILE ASN ASP ARG PRO LYS GLN ALA TRP CYS TRP PHE GLY SEQRES 26 F 500 GLY LYS TRP LYS ASP ALA ILE LYS GLU VAL LYS GLN THR SEQRES 27 F 500 ILE VAL LYS HIS PRO ARG TYR THR GLY THR ASN ASN THR SEQRES 28 F 500 ASP LYS ILE ASN LEU THR ALA PRO GLY GLY GLY ASP PRO SEQRES 29 F 500 GLU VAL THR PHE MET TRP THR ASN CYS ARG GLY GLU PHE SEQRES 30 F 500 LEU TYR CYS LYS MET ASN TRP PHE LEU ASN TRP VAL GLU SEQRES 31 F 500 ASP ARG ASN THR ALA ASN GLN LYS PRO LYS GLU GLN HIS SEQRES 32 F 500 LYS ARG ASN TYR VAL PRO CYS HIS ILE ARG GLN ILE ILE SEQRES 33 F 500 ASN THR TRP HIS LYS VAL GLY LYS ASN VAL TYR LEU PRO SEQRES 34 F 500 PRO ARG GLU GLY ASP LEU THR CYS ASN SER THR VAL THR SEQRES 35 F 500 SER LEU ILE ALA ASN ILE ASP TRP ILE ASP GLY ASN GLN SEQRES 36 F 500 THR ASN ILE THR MET SER ALA GLU VAL ALA GLU LEU TYR SEQRES 37 F 500 ARG LEU GLU LEU GLY ASP TYR LYS LEU VAL GLU ILE THR SEQRES 38 F 500 PRO ILE GLY LEU ALA PRO THR ASP CYS LYS ARG TYR THR SEQRES 39 F 500 THR GLY GLY THR SER ARG SEQRES 1 G 500 THR LEU TYR VAL THR VAL PHE TYR GLY VAL PRO ALA TRP SEQRES 2 G 500 ARG ASN ALA THR ILE PRO LEU PHE CYS ALA THR LYS ASN SEQRES 3 G 500 ARG ASP THR TRP GLY THR THR GLN CYS LEU PRO ASP ASN SEQRES 4 G 500 GLY ASP TYR SER GLU VAL ALA LEU ASN VAL THR GLU SER SEQRES 5 G 500 PHE ASP ALA TRP ASN ASN THR VAL THR GLU GLN ALA ILE SEQRES 6 G 500 GLU ASP VAL TRP GLN LEU PHE GLU THR SER ILE LYS PRO SEQRES 7 G 500 CYS VAL LYS LEU SER PRO LEU CYS ILE THR MET ARG CYS SEQRES 8 G 500 ASN LYS SER GLU THR ASP ARG TRP GLY LEU THR LYS SER SEQRES 9 G 500 ILE THR THR THR ALA SER THR THR SER THR THR ALA SER SEQRES 10 G 500 ALA LYS VAL ASP MET VAL ASN GLU THR SER SER CYS ILE SEQRES 11 G 500 ALA GLN ASP ASN CYS THR GLY LEU GLU GLN GLU GLN MET SEQRES 12 G 500 ILE SER CYS LYS PHE ASN MET THR GLY LEU LYS ARG ASP SEQRES 13 G 500 LYS THR LYS GLU TYR ASN GLU THR TRP TYR SER ALA ASP SEQRES 14 G 500 LEU VAL CYS GLU GLN GLY ASN ASN THR GLY ASN GLU SER SEQRES 15 G 500 ARG CYS TYR MET ASN HIS CYS ASN THR SER VAL ILE GLN SEQRES 16 G 500 GLU SER CYS ASP LYS HIS TYR TRP ASP ALA ILE ARG PHE SEQRES 17 G 500 ARG TYR CYS ALA PRO PRO GLY TYR ALA LEU LEU ARG CYS SEQRES 18 G 500 ASN ASP THR ASN TYR SER GLY PHE MET PRO LYS CYS SER SEQRES 19 G 500 LYS VAL VAL VAL SER SER CYS THR ARG MET MET GLU THR SEQRES 20 G 500 GLN THR SER THR TRP PHE GLY PHE ASN GLY THR ARG ALA SEQRES 21 G 500 GLU ASN ARG THR TYR ILE TYR TRP HIS GLY ARG ASP ASN SEQRES 22 G 500 ARG THR ILE ILE SER LEU ASN LYS TYR TYR ASN LEU THR SEQRES 23 G 500 MET LYS CYS ARG ARG PRO GLY ASN LYS THR VAL LEU PRO SEQRES 24 G 500 VAL THR ILE MET SER GLY LEU VAL PHE HIS SER GLN PRO SEQRES 25 G 500 ILE ASN ASP ARG PRO LYS GLN ALA TRP CYS TRP PHE GLY SEQRES 26 G 500 GLY LYS TRP LYS ASP ALA ILE LYS GLU VAL LYS GLN THR SEQRES 27 G 500 ILE VAL LYS HIS PRO ARG TYR THR GLY THR ASN ASN THR SEQRES 28 G 500 ASP LYS ILE ASN LEU THR ALA PRO GLY GLY GLY ASP PRO SEQRES 29 G 500 GLU VAL THR PHE MET TRP THR ASN CYS ARG GLY GLU PHE SEQRES 30 G 500 LEU TYR CYS LYS MET ASN TRP PHE LEU ASN TRP VAL GLU SEQRES 31 G 500 ASP ARG ASN THR ALA ASN GLN LYS PRO LYS GLU GLN HIS SEQRES 32 G 500 LYS ARG ASN TYR VAL PRO CYS HIS ILE ARG GLN ILE ILE SEQRES 33 G 500 ASN THR TRP HIS LYS VAL GLY LYS ASN VAL TYR LEU PRO SEQRES 34 G 500 PRO ARG GLU GLY ASP LEU THR CYS ASN SER THR VAL THR SEQRES 35 G 500 SER LEU ILE ALA ASN ILE ASP TRP ILE ASP GLY ASN GLN SEQRES 36 G 500 THR ASN ILE THR MET SER ALA GLU VAL ALA GLU LEU TYR SEQRES 37 G 500 ARG LEU GLU LEU GLY ASP TYR LYS LEU VAL GLU ILE THR SEQRES 38 G 500 PRO ILE GLY LEU ALA PRO THR ASP CYS LYS ARG TYR THR SEQRES 39 G 500 THR GLY GLY THR SER ARG SEQRES 1 H 244 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 244 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 244 ASN SER PHE SER ASN HIS ASP VAL HIS TRP VAL ARG GLN SEQRES 4 H 244 ALA THR GLY GLN GLY LEU GLU TRP MET GLY TRP MET SER SEQRES 5 H 244 HIS GLU GLY ASP LYS THR GLY LEU ALA GLN LYS PHE GLN SEQRES 6 H 244 GLY ARG VAL THR ILE THR ARG ASP SER GLY ALA SER THR SEQRES 7 H 244 VAL TYR MET GLU LEU ARG GLY LEU THR ALA ASP ASP THR SEQRES 8 H 244 ALA ILE TYR TYR CYS LEU THR GLY SER LYS HIS ARG LEU SEQRES 9 H 244 ARG ASP TYR PHE LEU TYS ASN GLU TYS GLY PRO ASN TYR SEQRES 10 H 244 GLU GLU TRP GLY ASP TYR LEU ALA THR LEU ASP VAL TRP SEQRES 11 H 244 GLY HIS GLY THR ALA VAL THR VAL SER SER ALA SER THR SEQRES 12 H 244 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 13 H 244 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 14 H 244 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 15 H 244 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 16 H 244 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 17 H 244 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 18 H 244 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 19 H 244 ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 1 L 219 GLU VAL VAL ILE THR GLN SER PRO LEU PHE LEU PRO VAL SEQRES 2 L 219 THR PRO GLY GLU ALA ALA SER LEU SER CYS LYS CYS SER SEQRES 3 L 219 HIS SER LEU GLN HIS SER THR GLY ALA ASN TYR LEU ALA SEQRES 4 L 219 TRP TYR LEU GLN ARG PRO GLY GLN THR PRO ARG LEU LEU SEQRES 5 L 219 ILE HIS LEU ALA THR HIS 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 ILE SER ARG VAL GLU SER ASP ASP VAL GLY THR TYR SEQRES 8 L 219 TYR CYS MET GLN GLY LEU HIS SER PRO TRP 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 ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS 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 HET TYS H 100F 16 HET TYS H 100I 16 HET NAG E 601 14 HET MAN F 601 11 HET NAG F 602 14 HET NAG G 601 14 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET MAN D 4 11 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET MAN I 4 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 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 MAN M 4 11 HET MAN M 5 11 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET MAN O 4 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 NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET 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 NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET MAN W 4 11 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HET MAN X 4 11 HET MAN X 5 11 HET NAG Y 1 14 HET NAG Y 2 14 HET BMA Y 3 11 HET MAN Y 4 11 HET MAN Y 5 11 HET MAN Y 6 11 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET MAN a 4 11 HET MAN a 5 11 HET NAG b 1 14 HET NAG b 2 14 HET BMA b 3 11 HET NAG c 1 14 HET NAG c 2 14 HET BMA c 3 11 HET MAN c 4 11 HET MAN c 5 11 HET MAN c 6 11 HET MAN c 7 11 HET MAN c 8 11 HET NAG d 1 14 HET NAG d 2 14 HET BMA d 3 11 HET MAN d 4 11 HET NAG e 1 14 HET NAG e 2 14 HET BMA e 3 11 HET MAN e 4 11 HET MAN e 5 11 HET MAN e 6 11 HET MAN e 7 11 HET MAN e 8 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 MAN f 7 11 HET MAN f 8 11 HET NAG g 1 14 HET NAG g 2 14 HET BMA g 3 11 HET MAN g 4 11 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 BMA j 3 11 HET MAN j 4 11 HET MAN j 5 11 HET NAG k 1 14 HET NAG k 2 14 HET BMA k 3 11 HET NAG l 1 14 HET NAG l 2 14 HET BMA l 3 11 HET NAG m 1 14 HET NAG m 2 14 HET BMA m 3 11 HET MAN m 4 11 HET NAG n 1 14 HET NAG n 2 14 HET NAG o 1 14 HET NAG o 2 14 HET BMA o 3 11 HET MAN o 4 11 HET MAN o 5 11 HET NAG p 1 14 HET NAG p 2 14 HET NAG q 1 14 HET NAG q 2 14 HET BMA q 3 11 HET MAN q 4 11 HET NAG r 1 14 HET NAG r 2 14 HET BMA r 3 11 HET MAN r 4 11 HET NAG s 1 14 HET NAG s 2 14 HET BMA s 3 11 HET MAN s 4 11 HET MAN s 5 11 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 MAN t 6 11 HET NAG u 1 14 HET NAG u 2 14 HET BMA u 3 11 HET MAN u 4 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 MAN x 4 11 HET MAN x 5 11 HET MAN x 6 11 HET MAN x 7 11 HET NAG y 1 14 HET NAG y 2 14 HET BMA y 3 11 HET MAN y 4 11 HET NAG z 1 14 HET NAG z 2 14 HET BMA z 3 11 HET MAN z 4 11 HET MAN z 5 11 HET MAN z 6 11 HET MAN z 7 11 HET NAG 0 1 14 HET NAG 0 2 14 HET BMA 0 3 11 HET MAN 0 4 11 HET MAN 0 5 11 HET NAG 1 1 14 HET NAG 1 2 14 HET BMA 1 3 11 HET NAG 2 1 14 HET NAG 2 2 14 HET NAG 3 1 14 HET NAG 3 2 14 HET NAG 4 1 14 HET NAG 4 2 14 HET BMA 4 3 11 HET MAN 4 4 11 HET MAN 4 5 11 HET NAG 5 1 14 HET NAG 5 2 14 HET BMA 5 3 11 HET MAN 5 4 11 HET NAG 6 1 14 HET NAG 6 2 14 HET BMA 6 3 11 HET NAG 7 1 14 HET NAG 7 2 14 HET BMA 7 3 11 HET MAN 7 4 11 HET NAG 8 1 14 HET NAG 8 2 14 HET NAG 9 1 14 HET NAG 9 2 14 HET BMA 9 3 11 HET MAN 9 4 11 HET MAN 9 5 11 HET NAG AA 1 14 HET NAG AA 2 14 HET NAG BA 1 14 HET NAG BA 2 14 HET BMA BA 3 11 HET MAN BA 4 11 HET NAG CA 1 14 HET NAG CA 2 14 HET BMA CA 3 11 HET MAN CA 4 11 HET NAG DA 1 14 HET NAG DA 2 14 HET BMA DA 3 11 HET MAN DA 4 11 HET MAN DA 5 11 HET NAG EA 1 14 HET NAG EA 2 14 HET BMA EA 3 11 HET MAN EA 4 11 HET MAN EA 5 11 HET MAN EA 6 11 HET NAG FA 1 14 HET NAG FA 2 14 HET BMA FA 3 11 HET MAN FA 4 11 HET NAG GA 1 14 HET NAG GA 2 14 HET BMA GA 3 11 HET MAN GA 4 11 HET MAN GA 5 11 HET NAG HA 1 14 HET NAG HA 2 14 HET BMA HA 3 11 HET NAG IA 1 14 HET NAG IA 2 14 HET BMA IA 3 11 HET MAN IA 4 11 HET MAN IA 5 11 HET MAN IA 6 11 HET MAN IA 7 11 HET NAG JA 1 14 HET NAG JA 2 14 HET BMA JA 3 11 HET MAN JA 4 11 HET NAG KA 1 14 HET NAG KA 2 14 HET BMA KA 3 11 HET MAN KA 4 11 HET MAN KA 5 11 HET MAN KA 6 11 HET MAN KA 7 11 HET MAN KA 8 11 HET NAG LA 1 14 HET NAG LA 2 14 HET BMA LA 3 11 HET MAN LA 4 11 HET MAN LA 5 11 HET NAG MA 1 14 HET NAG MA 2 14 HET BMA MA 3 11 HET NAG NA 1 14 HET NAG NA 2 14 HET NAG OA 1 14 HET NAG OA 2 14 HET NAG PA 1 14 HET NAG PA 2 14 HET BMA PA 3 11 HET MAN PA 4 11 HET MAN PA 5 11 HET NAG QA 1 14 HET NAG QA 2 14 HET BMA QA 3 11 HET MAN QA 4 11 HET NAG RA 1 14 HET NAG RA 2 14 HET BMA RA 3 11 HETNAM TYS O-SULFO-L-TYROSINE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM MAN ALPHA-D-MANNOSE HETNAM BMA BETA-D-MANNOSE FORMUL 7 TYS 2(C9 H11 N O6 S) FORMUL 9 NAG 147(C8 H15 N O6) FORMUL 10 MAN 94(C6 H12 O6) FORMUL 13 BMA 61(C6 H12 O6) HELIX 1 AA1 GLY A 512 PHE A 522 1 10 HELIX 2 AA2 LEU A 523 SER A 528 5 6 HELIX 3 AA3 THR A 538 GLN A 553 1 16 HELIX 4 AA4 THR A 578 TRP A 596 1 19 HELIX 5 AA5 THR A 627 ASN A 664 1 38 HELIX 6 AA6 VAL B 513 GLY B 521 1 8 HELIX 7 AA7 PHE B 522 ALA B 526 5 5 HELIX 8 AA8 THR B 538 GLN B 553 1 16 HELIX 9 AA9 THR B 578 GLY B 597 1 20 HELIX 10 AB1 THR B 627 ASN B 664 1 38 HELIX 11 AB2 VAL C 513 GLY C 521 1 8 HELIX 12 AB3 PHE C 522 ALA C 526 5 5 HELIX 13 AB4 THR C 538 GLN C 553 1 16 HELIX 14 AB5 THR C 578 GLY C 597 1 20 HELIX 15 AB6 THR C 627 PHE C 637 1 11 HELIX 16 AB7 LEU C 638 ASN C 664 1 27 HELIX 17 AB8 ASN E 98 LYS E 117 1 20 HELIX 18 AB9 ASN E 132 TRP E 139 1 8 HELIX 19 AC1 SER E 149D ASP E 149I 1 6 HELIX 20 AC2 TYR E 177 ALA E 179 5 3 HELIX 21 AC3 TRP E 338 HIS E 352 1 15 HELIX 22 AC4 ASP E 368 PHE E 373 1 6 HELIX 23 AC5 MET E 387 ASP E 396 1 10 HELIX 24 AC6 LYS E 406 GLN E 410 5 5 HELIX 25 AC7 GLU E 474 GLU E 477 5 4 HELIX 26 AC8 LEU E 478 LEU E 483 1 6 HELIX 27 AC9 ASN F 98 ILE F 116 1 19 HELIX 28 AD1 LEU F 122 CYS F 126 5 5 HELIX 29 AD2 LYS F 133 TRP F 139 1 7 HELIX 30 AD3 SER F 149D ASP F 149I 1 6 HELIX 31 AD4 ASN F 287 ASN F 291 5 5 HELIX 32 AD5 TRP F 338 HIS F 352 1 15 HELIX 33 AD6 ASN F 355 ILE F 359 5 5 HELIX 34 AD7 ASP F 368 PHE F 373 1 6 HELIX 35 AD8 MET F 387 ASP F 396 1 10 HELIX 36 AD9 LYS F 406 GLN F 410 5 5 HELIX 37 AE1 ALA F 476 GLY F 484 1 9 HELIX 38 AE2 ASN G 98 LYS G 117 1 20 HELIX 39 AE3 LEU G 122 CYS G 126 5 5 HELIX 40 AE4 LYS G 133 TRP G 139 1 7 HELIX 41 AE5 SER G 149D ASP G 149I 1 6 HELIX 42 AE6 TYR G 177 ALA G 179 5 3 HELIX 43 AE7 TRP G 338 HIS G 352 1 15 HELIX 44 AE8 ASN G 355 ILE G 359 5 5 HELIX 45 AE9 ASP G 368 PHE G 373 1 6 HELIX 46 AF1 MET G 387 GLU G 395 1 9 HELIX 47 AF2 GLU G 474 ALA G 476 5 3 HELIX 48 AF3 GLU G 477 LEU G 483 1 7 HELIX 49 AF4 GLY H 26 ASN H 31 5 6 HELIX 50 AF5 SER H 73 ALA H 75 5 3 HELIX 51 AF6 THR H 83 THR H 87 5 5 HELIX 52 AF7 GLU L 79 VAL L 83 5 5 SHEET 1 AA1 3 VAL B 603 PRO B 609 0 SHEET 2 AA1 3 TYR G 35 TYR G 40 -1 O VAL G 36 N VAL B 608 SHEET 3 AA1 3 ILE G 494 THR G 499 -1 O THR G 499 N TYR G 35 SHEET 1 AA2 3 VAL C 603 PRO C 609 0 SHEET 2 AA2 3 TYR E 35 TYR E 40 -1 O VAL E 36 N VAL C 608 SHEET 3 AA2 3 ILE E 494 THR E 499 -1 O GLY E 495 N PHE E 39 SHEET 1 AA3 5 TRP E 45 ASN E 47 0 SHEET 2 AA3 5 TYR E 486 ILE E 491 -1 O GLU E 490 N ARG E 46 SHEET 3 AA3 5 TYR E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AA3 5 VAL E 242 SER E 245 -1 O VAL E 243 N ARG E 227 SHEET 5 AA3 5 VAL E 84 LEU E 86 -1 N LEU E 86 O VAL E 242 SHEET 1 AA4 3 CYS E 74 PRO E 76 0 SHEET 2 AA4 3 PHE E 53 THR E 56 1 N THR E 56 O LEU E 75 SHEET 3 AA4 3 PHE E 215 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AA5 3 ARG E 130 CYS E 131 0 SHEET 2 AA5 3 CYS E 157 PHE E 159 -1 O LYS E 158 N ARG E 130 SHEET 3 AA5 3 TYR E 172 GLU E 174 -1 O TYR E 172 N PHE E 159 SHEET 1 AA6 2 LEU E 181 CYS E 183 0 SHEET 2 AA6 2 CYS E 191 MET E 193 -1 O TYR E 192 N VAL E 182 SHEET 1 AA7 3 GLN E 202 GLU E 203 0 SHEET 2 AA7 3 VAL E 434 TYR E 435 1 O TYR E 435 N GLN E 202 SHEET 3 AA7 3 ILE E 423 ILE E 424 -1 N ILE E 424 O VAL E 434 SHEET 1 AA8 5 ILE E 271 TRP E 273 0 SHEET 2 AA8 5 ARG E 281 ILE E 284 -1 O ILE E 283 N TYR E 272 SHEET 3 AA8 5 LEU E 452 ASP E 457 -1 O LEU E 452 N ILE E 284 SHEET 4 AA8 5 ASN E 468 MET E 471 -1 O THR E 470 N ASN E 455 SHEET 5 AA8 5 ASN E 360 THR E 362 1 N ASN E 360 O ILE E 469 SHEET 1 AA9 6 THR E 376 CYS E 378 0 SHEET 2 AA9 6 GLU E 381 CYS E 385 -1 O LEU E 383 N THR E 376 SHEET 3 AA9 6 VAL E 416 HIS E 419 -1 O HIS E 419 N TYR E 384 SHEET 4 AA9 6 TRP E 330 CYS E 331 -1 N CYS E 331 O VAL E 416 SHEET 5 AA9 6 THR E 293 ARG E 298 -1 N ARG E 297 O TRP E 330 SHEET 6 AA9 6 LEU E 443 THR E 448 -1 O SER E 447 N MET E 294 SHEET 1 AB1 2 LEU E 305 THR E 308 0 SHEET 2 AB1 2 VAL E 314 SER E 317 -1 O PHE E 315 N VAL E 307 SHEET 1 AB2 2 PHE F 39 TYR F 40 0 SHEET 2 AB2 2 ILE F 494 GLY F 495 -1 O GLY F 495 N PHE F 39 SHEET 1 AB3 5 TRP F 45 ASN F 47 0 SHEET 2 AB3 5 TYR F 486 ILE F 491 -1 O GLU F 490 N ARG F 46 SHEET 3 AB3 5 TYR F 223 CYS F 228 -1 N LEU F 226 O LYS F 487 SHEET 4 AB3 5 VAL F 242 SER F 245 -1 O VAL F 243 N ARG F 227 SHEET 5 AB3 5 VAL F 84 LEU F 86 -1 N VAL F 84 O VAL F 244 SHEET 1 AB4 3 CYS F 74 PRO F 76 0 SHEET 2 AB4 3 PHE F 53 THR F 56 1 N THR F 56 O LEU F 75 SHEET 3 AB4 3 PHE F 215 CYS F 218 -1 O ARG F 216 N ALA F 55 SHEET 1 AB5 3 MET F 129 ASN F 132 0 SHEET 2 AB5 3 GLU F 188 MET F 193 -1 O SER F 189 N CYS F 131 SHEET 3 AB5 3 LEU F 181 VAL F 182 -1 N VAL F 182 O TYR F 192 SHEET 1 AB6 2 MET F 154 ILE F 155 0 SHEET 2 AB6 2 TRP F 176 TYR F 177 -1 O TRP F 176 N ILE F 155 SHEET 1 AB7 2 LYS F 158 PHE F 159 0 SHEET 2 AB7 2 TYR F 172 ASN F 173 -1 O TYR F 172 N PHE F 159 SHEET 1 AB8 3 GLN F 202 GLU F 203 0 SHEET 2 AB8 3 ASN F 433 TYR F 435 1 O TYR F 435 N GLN F 202 SHEET 3 AB8 3 ILE F 423 ASN F 425 -1 N ILE F 424 O VAL F 434 SHEET 1 AB9 4 GLY F 260 PHE F 261 0 SHEET 2 AB9 4 GLY F 441 ASP F 457 -1 O THR F 450 N GLY F 260 SHEET 3 AB9 4 ASN F 468 MET F 471 -1 O THR F 470 N ASN F 455 SHEET 4 AB9 4 ASN F 360 THR F 362 1 N ASN F 360 O ILE F 469 SHEET 1 AC1 8 ILE F 271 TRP F 273 0 SHEET 2 AC1 8 ARG F 281 ILE F 284 -1 O ILE F 283 N TYR F 272 SHEET 3 AC1 8 GLY F 441 ASP F 457 -1 O LEU F 452 N ILE F 284 SHEET 4 AC1 8 THR F 293 LYS F 302 -1 N CYS F 296 O CYS F 445 SHEET 5 AC1 8 TRP F 330 CYS F 331 -1 O TRP F 330 N ARG F 297 SHEET 6 AC1 8 VAL F 416 ILE F 420 -1 O VAL F 416 N CYS F 331 SHEET 7 AC1 8 GLU F 381 CYS F 385 -1 N TYR F 384 O HIS F 419 SHEET 8 AC1 8 MET F 374 CYS F 378 -1 N THR F 376 O LEU F 383 SHEET 1 AC2 5 TRP G 45 ASN G 47 0 SHEET 2 AC2 5 TYR G 486 ILE G 491 -1 O GLU G 490 N ARG G 46 SHEET 3 AC2 5 TYR G 223 CYS G 228 -1 N LEU G 226 O LYS G 487 SHEET 4 AC2 5 VAL G 242 SER G 245 -1 O VAL G 243 N ARG G 227 SHEET 5 AC2 5 VAL G 84 LEU G 86 -1 N LEU G 86 O VAL G 242 SHEET 1 AC3 2 PHE G 53 ALA G 55 0 SHEET 2 AC3 2 ARG G 216 CYS G 218 -1 O ARG G 216 N ALA G 55 SHEET 1 AC4 3 MET G 129 ASN G 132 0 SHEET 2 AC4 3 GLU G 188 MET G 193 -1 O SER G 189 N CYS G 131 SHEET 3 AC4 3 LEU G 181 CYS G 183 -1 N VAL G 182 O TYR G 192 SHEET 1 AC5 2 ILE G 155 PHE G 159 0 SHEET 2 AC5 2 TYR G 172 TRP G 176 -1 O TRP G 176 N ILE G 155 SHEET 1 AC6 3 GLN G 202 GLU G 203 0 SHEET 2 AC6 3 ASN G 433 TYR G 435 1 O TYR G 435 N GLN G 202 SHEET 3 AC6 3 ILE G 423 ASN G 425 -1 N ILE G 424 O VAL G 434 SHEET 1 AC7 9 SER G 256 THR G 257 0 SHEET 2 AC7 9 TRP G 375 CYS G 378 -1 O TRP G 375 N THR G 257 SHEET 3 AC7 9 GLU G 381 CYS G 385 -1 O LEU G 383 N THR G 376 SHEET 4 AC7 9 VAL G 416 ILE G 420 -1 O HIS G 419 N TYR G 384 SHEET 5 AC7 9 TRP G 330 CYS G 331 -1 N CYS G 331 O VAL G 416 SHEET 6 AC7 9 THR G 293 LYS G 302 -1 N ARG G 297 O TRP G 330 SHEET 7 AC7 9 GLY G 441 ASP G 457 -1 O CYS G 445 N CYS G 296 SHEET 8 AC7 9 THR G 282 SER G 285 -1 N ILE G 284 O LEU G 452 SHEET 9 AC7 9 ILE G 271 TRP G 273 -1 N TYR G 272 O ILE G 283 SHEET 1 AC8 4 GLY G 260 PHE G 261 0 SHEET 2 AC8 4 GLY G 441 ASP G 457 -1 O THR G 450 N GLY G 260 SHEET 3 AC8 4 ASN G 468 THR G 470 -1 O ASN G 468 N ASP G 457 SHEET 4 AC8 4 ASN G 360 THR G 362 1 N ASN G 360 O ILE G 469 SHEET 1 AC9 2 VAL G 307 THR G 308 0 SHEET 2 AC9 2 VAL G 314 PHE G 315 -1 O PHE G 315 N VAL G 307 SHEET 1 AD1 4 LEU H 4 GLN H 6 0 SHEET 2 AD1 4 VAL H 18 ALA H 24 -1 O LYS H 23 N VAL H 5 SHEET 3 AD1 4 THR H 77 LEU H 82 -1 O LEU H 82 N VAL H 18 SHEET 4 AD1 4 VAL H 65 ARG H 71 -1 N THR H 70 O TYR H 79 SHEET 1 AD2 6 GLU H 10 LYS H 12 0 SHEET 2 AD2 6 THR H 112 VAL H 116 1 O THR H 115 N LYS H 12 SHEET 3 AD2 6 ALA H 88 GLY H 95 -1 N TYR H 90 O THR H 112 SHEET 4 AD2 6 ASP H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AD2 6 LEU H 45 MET H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AD2 6 THR H 55 LEU H 57 -1 O GLY H 56 N TRP H 50 SHEET 1 AD3 2 LEU H 100 LEU H 100E 0 SHEET 2 AD3 2 TYR H 100M GLY H 100Q-1 O GLU H 100O N ASP H 100B SHEET 1 AD4 4 THR L 5 SER L 7 0 SHEET 2 AD4 4 ALA L 19 LYS L 24 -1 O LYS L 24 N THR L 5 SHEET 3 AD4 4 ASP L 70 ILE L 75 -1 O ILE L 75 N ALA L 19 SHEET 4 AD4 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AD5 6 PHE L 10 VAL L 13 0 SHEET 2 AD5 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AD5 6 GLY L 84 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD5 6 LEU L 33 GLN L 38 -1 N ALA L 34 O MET L 89 SHEET 5 AD5 6 ARG L 45 HIS L 49 -1 O ARG L 45 N LEU L 37 SHEET 6 AD5 6 HIS L 53 ARG L 54 -1 O HIS L 53 N HIS L 49 SSBOND 1 CYS A 598 CYS A 604 1555 1555 2.03 SSBOND 2 CYS A 605 CYS F 501 1555 1555 2.03 SSBOND 3 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 4 CYS B 605 CYS G 501 1555 1555 2.03 SSBOND 5 CYS C 598 CYS C 604 1555 1555 2.03 SSBOND 6 CYS C 605 CYS E 501 1555 1555 2.03 SSBOND 7 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 8 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 9 CYS E 126 CYS E 196 1555 1555 2.04 SSBOND 10 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 11 CYS E 149E CYS E 149K 1555 1555 2.03 SSBOND 12 CYS E 183 CYS E 191 1555 1555 2.03 SSBOND 13 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 14 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 15 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 16 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 17 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 18 CYS F 54 CYS F 74 1555 1555 2.04 SSBOND 19 CYS F 119 CYS F 205 1555 1555 2.03 SSBOND 20 CYS F 126 CYS F 196 1555 1555 2.04 SSBOND 21 CYS F 131 CYS F 157 1555 1555 2.03 SSBOND 22 CYS F 149E CYS F 149K 1555 1555 2.03 SSBOND 23 CYS F 183 CYS F 191 1555 1555 2.03 SSBOND 24 CYS F 218 CYS F 247 1555 1555 2.03 SSBOND 25 CYS F 228 CYS F 239 1555 1555 2.03 SSBOND 26 CYS F 296 CYS F 331 1555 1555 2.03 SSBOND 27 CYS F 378 CYS F 445 1555 1555 2.03 SSBOND 28 CYS F 385 CYS F 418 1555 1555 2.03 SSBOND 29 CYS G 54 CYS G 74 1555 1555 2.03 SSBOND 30 CYS G 119 CYS G 205 1555 1555 2.02 SSBOND 31 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 32 CYS G 131 CYS G 157 1555 1555 2.04 SSBOND 33 CYS G 149E CYS G 149K 1555 1555 2.03 SSBOND 34 CYS G 183 CYS G 191 1555 1555 2.03 SSBOND 35 CYS G 218 CYS G 247 1555 1555 2.03 SSBOND 36 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 37 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 38 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 39 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 40 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 41 CYS L 23 CYS L 88 1555 1555 2.04 LINK ND2 ASN A 612 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 625 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN A 641 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN B 612 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN B 625 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN B 641 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN C 612 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN C 625 C1 NAG P 1 1555 1555 1.45 LINK ND2 ASN C 641 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN E 47 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN E 97 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN E 132 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN E 149 C1 NAG b 1 1555 1555 1.45 LINK ND2 ASN E 149J C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG f 1 1555 1555 1.59 LINK ND2 ASN E 173 C1 NAG l 1 1555 1555 1.43 LINK ND2 ASN E 185B C1 NAG h 1 1555 1555 1.45 LINK ND2 ASN E 187 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN E 229 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN E 267A C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN E 280 C1 NAG j 1 1555 1555 1.44 LINK ND2 ASN E 291 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN E 354E C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN E 360 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN E 446 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN E 464 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 468 C1 NAG k 1 1555 1555 1.44 LINK ND2 ASN F 47 C1 NAG z 1 1555 1555 1.44 LINK ND2 ASN F 88 C1 NAG n 1 1555 1555 1.44 LINK ND2 ASN F 97 C1 NAG m 1 1555 1555 1.44 LINK ND2 ASN F 132 C1 NAG o 1 1555 1555 1.44 LINK ND2 ASN F 149 C1 NAG w 1 1555 1555 1.45 LINK ND2 ASN F 149J C1 NAG y 1 1555 1555 1.44 LINK ND2 ASN F 160 C1 NAG 0 1 1555 1555 1.45 LINK ND2 ASN F 173 C1 NAG 1 1 1555 1555 1.45 LINK ND2 ASN F 185B C1 NAG 2 1 1555 1555 1.46 LINK ND2 ASN F 187 C1 NAG p 1 1555 1555 1.44 LINK ND2 ASN F 197 C1 NAG q 1 1555 1555 1.44 LINK ND2 ASN F 229 C1 NAG r 1 1555 1555 1.44 LINK ND2 ASN F 262 C1 NAG x 1 1555 1555 1.44 LINK ND2 ASN F 267A C1 NAG u 1 1555 1555 1.44 LINK ND2 ASN F 280 C1 NAG 4 1 1555 1555 1.44 LINK ND2 ASN F 291 C1 NAG v 1 1555 1555 1.44 LINK ND2 ASN F 301 C1 NAG 5 1 1555 1555 1.44 LINK ND2 ASN F 354E C1 NAG 3 1 1555 1555 1.44 LINK ND2 ASN F 360 C1 NAG t 1 1555 1555 1.44 LINK ND2 ASN F 446 C1 NAG s 1 1555 1555 1.44 LINK ND2 ASN F 464 C1 NAG F 602 1555 1555 1.44 LINK ND2 ASN F 468 C1 NAG 6 1 1555 1555 1.44 LINK ND2 ASN G 47 C1 NAGKA 1 1555 1555 1.44 LINK ND2 ASN G 88 C1 NAG 8 1 1555 1555 1.44 LINK ND2 ASN G 97 C1 NAG 7 1 1555 1555 1.44 LINK ND2 ASN G 132 C1 NAG 9 1 1555 1555 1.44 LINK ND2 ASN G 149 C1 NAGHA 1 1555 1555 1.45 LINK ND2 ASN G 149J C1 NAGJA 1 1555 1555 1.45 LINK ND2 ASN G 160 C1 NAGLA 1 1555 1555 1.44 LINK ND2 ASN G 173 C1 NAGMA 1 1555 1555 1.45 LINK ND2 ASN G 185B C1 NAGNA 1 1555 1555 1.45 LINK ND2 ASN G 187 C1 NAGAA 1 1555 1555 1.44 LINK ND2 ASN G 197 C1 NAGBA 1 1555 1555 1.44 LINK ND2 ASN G 229 C1 NAGCA 1 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAGIA 1 1555 1555 1.44 LINK ND2 ASN G 267A C1 NAGFA 1 1555 1555 1.44 LINK ND2 ASN G 280 C1 NAGPA 1 1555 1555 1.44 LINK ND2 ASN G 291 C1 NAGGA 1 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAGRA 1 1555 1555 1.45 LINK ND2 ASN G 354E C1 NAGOA 1 1555 1555 1.44 LINK ND2 ASN G 360 C1 NAGEA 1 1555 1555 1.44 LINK ND2 ASN G 446 C1 NAGDA 1 1555 1555 1.44 LINK ND2 ASN G 464 C1 NAG G 601 1555 1555 1.44 LINK ND2 ASN G 468 C1 NAGQA 1 1555 1555 1.44 LINK C LEU H 100E N TYS H 100F 1555 1555 1.33 LINK C TYS H 100F N ASN H 100G 1555 1555 1.33 LINK C GLU H 100H N TYS H 100I 1555 1555 1.33 LINK C TYS H 100I N GLY H 100J 1555 1555 1.33 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 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.45 LINK O3 BMA K 3 C1 MAN K 4 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.44 LINK O3 BMA M 3 C1 MAN M 4 1555 1555 1.44 LINK O6 BMA M 3 C1 MAN M 5 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O3 BMA O 3 C1 MAN O 4 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 1.44 LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.44 LINK O6 BMA P 3 C1 MAN P 5 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.46 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.45 LINK O3 BMA T 3 C1 MAN T 4 1555 1555 1.44 LINK O6 BMA T 3 C1 MAN T 5 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.45 LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.45 LINK O3 BMA W 3 C1 MAN W 4 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44 LINK O3 BMA X 3 C1 MAN X 4 1555 1555 1.44 LINK O6 BMA X 3 C1 MAN X 5 1555 1555 1.45 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.45 LINK O3 BMA Y 3 C1 MAN Y 4 1555 1555 1.45 LINK O6 BMA Y 3 C1 MAN Y 6 1555 1555 1.44 LINK O2 MAN Y 4 C1 MAN Y 5 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.45 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.44 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.44 LINK O3 BMA a 3 C1 MAN a 4 1555 1555 1.44 LINK O6 BMA a 3 C1 MAN a 5 1555 1555 1.44 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG b 2 C1 BMA b 3 1555 1555 1.45 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.45 LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.44 LINK O3 BMA c 3 C1 MAN c 4 1555 1555 1.44 LINK O6 BMA c 3 C1 MAN c 7 1555 1555 1.44 LINK O2 MAN c 4 C1 MAN c 5 1555 1555 1.45 LINK O2 MAN c 5 C1 MAN c 6 1555 1555 1.44 LINK O6 MAN c 7 C1 MAN c 8 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.43 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.44 LINK O3 BMA d 3 C1 MAN d 4 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.45 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.44 LINK O3 BMA e 3 C1 MAN e 4 1555 1555 1.44 LINK O6 BMA e 3 C1 MAN e 6 1555 1555 1.44 LINK O2 MAN e 4 C1 MAN e 5 1555 1555 1.44 LINK O3 MAN e 6 C1 MAN e 7 1555 1555 1.44 LINK O6 MAN e 6 C1 MAN e 8 1555 1555 1.44 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.43 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.43 LINK O3 BMA f 3 C1 MAN f 4 1555 1555 1.42 LINK O6 BMA f 3 C1 MAN f 6 1555 1555 1.44 LINK O2 MAN f 4 C1 MAN f 5 1555 1555 1.43 LINK O3 MAN f 6 C1 MAN f 7 1555 1555 1.43 LINK O6 MAN f 6 C1 MAN f 8 1555 1555 1.43 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O4 NAG g 2 C1 BMA g 3 1555 1555 1.44 LINK O3 BMA g 3 C1 MAN g 4 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 1.44 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.45 LINK O3 BMA j 3 C1 MAN j 4 1555 1555 1.44 LINK O6 BMA j 3 C1 MAN j 5 1555 1555 1.45 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.44 LINK O4 NAG k 2 C1 BMA k 3 1555 1555 1.45 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.44 LINK O4 NAG l 2 C1 BMA l 3 1555 1555 1.45 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.44 LINK O4 NAG m 2 C1 BMA m 3 1555 1555 1.44 LINK O3 BMA m 3 C1 MAN m 4 1555 1555 1.44 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.44 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.44 LINK O4 NAG o 2 C1 BMA o 3 1555 1555 1.45 LINK O3 BMA o 3 C1 MAN o 4 1555 1555 1.44 LINK O6 BMA o 3 C1 MAN o 5 1555 1555 1.44 LINK O4 NAG p 1 C1 NAG p 2 1555 1555 1.44 LINK O4 NAG q 1 C1 NAG q 2 1555 1555 1.44 LINK O4 NAG q 2 C1 BMA q 3 1555 1555 1.45 LINK O3 BMA q 3 C1 MAN q 4 1555 1555 1.45 LINK O4 NAG r 1 C1 NAG r 2 1555 1555 1.44 LINK O4 NAG r 2 C1 BMA r 3 1555 1555 1.45 LINK O3 BMA r 3 C1 MAN r 4 1555 1555 1.44 LINK O4 NAG s 1 C1 NAG s 2 1555 1555 1.44 LINK O4 NAG s 2 C1 BMA s 3 1555 1555 1.44 LINK O3 BMA s 3 C1 MAN s 4 1555 1555 1.44 LINK O6 BMA s 3 C1 MAN s 5 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 1.44 LINK O6 BMA t 3 C1 MAN t 6 1555 1555 1.44 LINK O2 MAN t 4 C1 MAN t 5 1555 1555 1.44 LINK O4 NAG u 1 C1 NAG u 2 1555 1555 1.44 LINK O4 NAG u 2 C1 BMA u 3 1555 1555 1.44 LINK O6 BMA u 3 C1 MAN u 4 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 1.44 LINK O3 BMA v 3 C1 MAN v 4 1555 1555 1.44 LINK O6 BMA v 3 C1 MAN v 5 1555 1555 1.44 LINK O4 NAG w 1 C1 NAG w 2 1555 1555 1.44 LINK O4 NAG w 2 C1 BMA w 3 1555 1555 1.45 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 O3 BMA x 3 C1 MAN x 4 1555 1555 1.44 LINK O6 BMA x 3 C1 MAN x 6 1555 1555 1.44 LINK O2 MAN x 4 C1 MAN x 5 1555 1555 1.45 LINK O6 MAN x 6 C1 MAN x 7 1555 1555 1.44 LINK O4 NAG y 1 C1 NAG y 2 1555 1555 1.43 LINK O4 NAG y 2 C1 BMA y 3 1555 1555 1.44 LINK O3 BMA y 3 C1 MAN y 4 1555 1555 1.44 LINK O4 NAG z 1 C1 NAG z 2 1555 1555 1.44 LINK O4 NAG z 2 C1 BMA z 3 1555 1555 1.44 LINK O3 BMA z 3 C1 MAN z 4 1555 1555 1.44 LINK O6 BMA z 3 C1 MAN z 6 1555 1555 1.44 LINK O2 MAN z 4 C1 MAN z 5 1555 1555 1.44 LINK O3 MAN z 6 C1 MAN z 7 1555 1555 1.44 LINK O4 NAG 0 1 C1 NAG 0 2 1555 1555 1.44 LINK O4 NAG 0 2 C1 BMA 0 3 1555 1555 1.44 LINK O3 BMA 0 3 C1 MAN 0 4 1555 1555 1.44 LINK O6 BMA 0 3 C1 MAN 0 5 1555 1555 1.45 LINK O4 NAG 1 1 C1 NAG 1 2 1555 1555 1.43 LINK O4 NAG 1 2 C1 BMA 1 3 1555 1555 1.45 LINK O4 NAG 2 1 C1 NAG 2 2 1555 1555 1.44 LINK O4 NAG 3 1 C1 NAG 3 2 1555 1555 1.44 LINK O4 NAG 4 1 C1 NAG 4 2 1555 1555 1.44 LINK O4 NAG 4 2 C1 BMA 4 3 1555 1555 1.44 LINK O3 BMA 4 3 C1 MAN 4 4 1555 1555 1.44 LINK O6 BMA 4 3 C1 MAN 4 5 1555 1555 1.44 LINK O4 NAG 5 1 C1 NAG 5 2 1555 1555 1.44 LINK O4 NAG 5 2 C1 BMA 5 3 1555 1555 1.45 LINK O3 BMA 5 3 C1 MAN 5 4 1555 1555 1.44 LINK O4 NAG 6 1 C1 NAG 6 2 1555 1555 1.44 LINK O4 NAG 6 2 C1 BMA 6 3 1555 1555 1.44 LINK O4 NAG 7 1 C1 NAG 7 2 1555 1555 1.44 LINK O4 NAG 7 2 C1 BMA 7 3 1555 1555 1.45 LINK O3 BMA 7 3 C1 MAN 7 4 1555 1555 1.45 LINK O4 NAG 8 1 C1 NAG 8 2 1555 1555 1.44 LINK O4 NAG 9 1 C1 NAG 9 2 1555 1555 1.44 LINK O4 NAG 9 2 C1 BMA 9 3 1555 1555 1.45 LINK O3 BMA 9 3 C1 MAN 9 4 1555 1555 1.44 LINK O6 BMA 9 3 C1 MAN 9 5 1555 1555 1.44 LINK O4 NAGAA 1 C1 NAGAA 2 1555 1555 1.44 LINK O4 NAGBA 1 C1 NAGBA 2 1555 1555 1.44 LINK O4 NAGBA 2 C1 BMABA 3 1555 1555 1.45 LINK O3 BMABA 3 C1 MANBA 4 1555 1555 1.45 LINK O4 NAGCA 1 C1 NAGCA 2 1555 1555 1.44 LINK O4 NAGCA 2 C1 BMACA 3 1555 1555 1.45 LINK O3 BMACA 3 C1 MANCA 4 1555 1555 1.44 LINK O4 NAGDA 1 C1 NAGDA 2 1555 1555 1.44 LINK O4 NAGDA 2 C1 BMADA 3 1555 1555 1.44 LINK O3 BMADA 3 C1 MANDA 4 1555 1555 1.44 LINK O6 BMADA 3 C1 MANDA 5 1555 1555 1.44 LINK O4 NAGEA 1 C1 NAGEA 2 1555 1555 1.44 LINK O4 NAGEA 2 C1 BMAEA 3 1555 1555 1.44 LINK O3 BMAEA 3 C1 MANEA 4 1555 1555 1.44 LINK O6 BMAEA 3 C1 MANEA 6 1555 1555 1.44 LINK O2 MANEA 4 C1 MANEA 5 1555 1555 1.44 LINK O4 NAGFA 1 C1 NAGFA 2 1555 1555 1.44 LINK O4 NAGFA 2 C1 BMAFA 3 1555 1555 1.44 LINK O6 BMAFA 3 C1 MANFA 4 1555 1555 1.44 LINK O4 NAGGA 1 C1 NAGGA 2 1555 1555 1.44 LINK O4 NAGGA 2 C1 BMAGA 3 1555 1555 1.44 LINK O3 BMAGA 3 C1 MANGA 4 1555 1555 1.44 LINK O6 BMAGA 3 C1 MANGA 5 1555 1555 1.44 LINK O4 NAGHA 1 C1 NAGHA 2 1555 1555 1.44 LINK O4 NAGHA 2 C1 BMAHA 3 1555 1555 1.45 LINK O4 NAGIA 1 C1 NAGIA 2 1555 1555 1.45 LINK O4 NAGIA 2 C1 BMAIA 3 1555 1555 1.44 LINK O3 BMAIA 3 C1 MANIA 4 1555 1555 1.44 LINK O6 BMAIA 3 C1 MANIA 6 1555 1555 1.45 LINK O2 MANIA 4 C1 MANIA 5 1555 1555 1.44 LINK O6 MANIA 6 C1 MANIA 7 1555 1555 1.44 LINK O4 NAGJA 1 C1 NAGJA 2 1555 1555 1.45 LINK O4 NAGJA 2 C1 BMAJA 3 1555 1555 1.44 LINK O3 BMAJA 3 C1 MANJA 4 1555 1555 1.44 LINK O4 NAGKA 1 C1 NAGKA 2 1555 1555 1.45 LINK O4 NAGKA 2 C1 BMAKA 3 1555 1555 1.44 LINK O3 BMAKA 3 C1 MANKA 4 1555 1555 1.44 LINK O6 BMAKA 3 C1 MANKA 6 1555 1555 1.44 LINK O2 MANKA 4 C1 MANKA 5 1555 1555 1.44 LINK O3 MANKA 6 C1 MANKA 7 1555 1555 1.44 LINK O6 MANKA 6 C1 MANKA 8 1555 1555 1.44 LINK O4 NAGLA 1 C1 NAGLA 2 1555 1555 1.44 LINK O4 NAGLA 2 C1 BMALA 3 1555 1555 1.44 LINK O3 BMALA 3 C1 MANLA 4 1555 1555 1.44 LINK O6 BMALA 3 C1 MANLA 5 1555 1555 1.44 LINK O4 NAGMA 1 C1 NAGMA 2 1555 1555 1.43 LINK O4 NAGMA 2 C1 BMAMA 3 1555 1555 1.45 LINK O4 NAGNA 1 C1 NAGNA 2 1555 1555 1.44 LINK O4 NAGOA 1 C1 NAGOA 2 1555 1555 1.44 LINK O4 NAGPA 1 C1 NAGPA 2 1555 1555 1.44 LINK O4 NAGPA 2 C1 BMAPA 3 1555 1555 1.44 LINK O3 BMAPA 3 C1 MANPA 4 1555 1555 1.44 LINK O6 BMAPA 3 C1 MANPA 5 1555 1555 1.44 LINK O4 NAGQA 1 C1 NAGQA 2 1555 1555 1.44 LINK O4 NAGQA 2 C1 BMAQA 3 1555 1555 1.45 LINK O3 BMAQA 3 C1 MANQA 4 1555 1555 1.44 LINK O4 NAGRA 1 C1 NAGRA 2 1555 1555 1.44 LINK O4 NAGRA 2 C1 BMARA 3 1555 1555 1.45 CISPEP 1 SER L 7 PRO L 8 0 -4.55 CISPEP 2 SER L 94 PRO L 95 0 -0.10 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