HEADER VIRAL PROTEIN/IMMUNE SYSTEM 01-AUG-23 8TNG TITLE CRYO-EM STRUCTURE OF HIV-1 ENV BG505 DS-SOSIP IN COMPLEX WITH BROADLY TITLE 2 NEUTRALIZING LLAMA NANOBODY R27 TARGETING THE CD4-BINDING SITE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV-1 BG505 DS-SOSIP GP120; COMPND 3 CHAIN: A, C, E; COMPND 4 FRAGMENT: UNP RESIDUES 30-505; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIHIV-1 BG505 DS-SOSIP GP41N GP41; COMPND 8 CHAIN: B, D, F; COMPND 9 FRAGMENT: UNP RESIDUES 509-661; COMPND 10 SYNONYM: ENV POLYPROTEN; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: CD4-BINDING SITE TARGETING NANOBODY R27; COMPND 14 CHAIN: H, I, J; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F; SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PVRC8400; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 20 ORGANISM_COMMON: LLAMA; SOURCE 21 ORGANISM_TAXID: 9844; SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 23 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F; SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PVRC8400 KEYWDS HIV-1 ENVELOPE, ANTIBODY, NANOBODY, VHH, LLAMA, BG505 DS-SOSIP, KEYWDS 2 NEUTRALIZATION, IMMUNIZATION, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR T.ZHOU,P.D.KWONG,J.XU REVDAT 1 08-MAY-24 8TNG 0 JRNL AUTH J.XU,T.ZHOU JRNL TITL CRYO-EM STRUCTURE OF HIV-1 ENV BG505 DS-SOSIP IN COMPLEX JRNL TITL 2 WITH BROADLY NEUTRALIZING LLAMA NANOBODY R27 TARGETING THE JRNL TITL 3 CD4-BINDING SITE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.58 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, SERIALEM, CRYOSPARC, COOT, REMARK 3 CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7LPN REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : 82.900 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) : 3.580 REMARK 3 NUMBER OF PARTICLES : 315969 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 8TNG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-23. REMARK 100 THE DEPOSITION ID IS D_1000276250. 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 BETWEEN HIV-1 ENV BG505 REMARK 245 DS-SOSIP AND LLAMA NANOBODY R27 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 3.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 22500 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: NONAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, G, REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e 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 ASN A 186A REMARK 465 GLN A 186B REMARK 465 GLY A 186C REMARK 465 ASN A 186D REMARK 465 ARG A 186E REMARK 465 SER A 186F REMARK 465 ASN A 186G REMARK 465 ASN A 186H REMARK 465 SER A 186I REMARK 465 THR A 400 REMARK 465 SER A 401 REMARK 465 VAL A 402 REMARK 465 GLN A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 SER A 407 REMARK 465 THR A 408 REMARK 465 GLY A 409 REMARK 465 SER A 410 REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 REMARK 465 ARG A 509 REMARK 465 ARG A 510 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 ARG A 513 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 ASN C 186A REMARK 465 GLN C 186B REMARK 465 GLY C 186C REMARK 465 ASN C 186D REMARK 465 ARG C 186E REMARK 465 SER C 186F REMARK 465 ASN C 186G REMARK 465 ASN C 186H REMARK 465 SER C 186I REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 SER C 410 REMARK 465 VAL C 506 REMARK 465 GLY C 507 REMARK 465 ARG C 508 REMARK 465 ARG C 509 REMARK 465 ARG C 510 REMARK 465 ARG C 511 REMARK 465 ARG C 512 REMARK 465 ARG C 513 REMARK 465 ALA D 512 REMARK 465 VAL D 513 REMARK 465 GLY D 514 REMARK 465 ILE D 515 REMARK 465 GLY D 516 REMARK 465 ALA D 517 REMARK 465 VAL D 518 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 PRO D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 ASN E 186A REMARK 465 GLN E 186B REMARK 465 GLY E 186C REMARK 465 ASN E 186D REMARK 465 ARG E 186E REMARK 465 SER E 186F REMARK 465 ASN E 186G REMARK 465 ASN E 186H REMARK 465 SER E 186I 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 VAL E 506 REMARK 465 GLY E 507 REMARK 465 ARG E 508 REMARK 465 ARG E 509 REMARK 465 ARG E 510 REMARK 465 ARG E 511 REMARK 465 ARG E 512 REMARK 465 ARG E 513 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN J 1 N 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 OG SER H 52 OG SER H 57 2.09 REMARK 500 ND2 ASN E 301 O5 NAG E 605 2.11 REMARK 500 OG SER H 33 O LEU H 51 2.15 REMARK 500 O ASP B 632 OG SER B 636 2.17 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 A 201 CA - CB - SG ANGL. DEV. = 8.9 DEGREES REMARK 500 CYS A 433 CA - CB - SG ANGL. DEV. = 7.7 DEGREES REMARK 500 CYS C 296 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 CYS E 196 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 CYS E 296 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 CYS E 501 CA - CB - SG ANGL. DEV. = 11.3 DEGREES REMARK 500 CYS F 605 CA - CB - SG ANGL. DEV. = 6.6 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 ALA A 60 -61.70 61.72 REMARK 500 TYR A 61 -3.98 69.66 REMARK 500 LYS A 65 30.22 -99.16 REMARK 500 HIS A 66 162.47 63.46 REMARK 500 THR A 128 98.01 -68.88 REMARK 500 GLU A 153 -95.47 56.97 REMARK 500 PRO A 240 43.48 -84.86 REMARK 500 SER A 241 17.81 -146.90 REMARK 500 GLN A 258 2.26 59.94 REMARK 500 GLU A 268 -110.20 60.83 REMARK 500 THR A 278 -2.77 -143.40 REMARK 500 ASP A 321A 98.09 68.75 REMARK 500 ARG A 350 3.49 -66.35 REMARK 500 THR A 450 70.82 -107.09 REMARK 500 LEU A 452 146.26 -171.62 REMARK 500 THR A 461 -145.02 55.16 REMARK 500 THR A 465 43.65 -143.46 REMARK 500 LYS A 485 55.19 -97.14 REMARK 500 ARG A 500 54.78 -94.32 REMARK 500 SER B 534 49.53 -83.14 REMARK 500 CYS B 598 -160.60 -165.91 REMARK 500 SER B 599 11.52 82.67 REMARK 500 LYS B 601 -95.82 170.47 REMARK 500 ASN B 607 -157.79 -78.25 REMARK 500 VAL B 608 79.52 61.75 REMARK 500 ASN B 637 34.00 -142.35 REMARK 500 ALA C 60 -61.82 61.72 REMARK 500 TYR C 61 -3.97 69.48 REMARK 500 HIS C 66 163.28 61.63 REMARK 500 LEU C 122 104.50 -51.32 REMARK 500 THR C 135 88.77 -151.95 REMARK 500 GLU C 153 -96.48 54.38 REMARK 500 ASP C 167 -15.76 -142.68 REMARK 500 PHE C 210 33.72 -97.40 REMARK 500 LYS C 232 34.33 -99.84 REMARK 500 PRO C 240 43.64 -84.70 REMARK 500 SER C 241 17.50 -146.77 REMARK 500 CYS C 247 -179.88 -172.04 REMARK 500 LEU C 261 -161.72 -79.81 REMARK 500 ASN C 262 127.26 -34.76 REMARK 500 GLU C 268 -107.73 63.78 REMARK 500 THR C 278 -6.94 -143.69 REMARK 500 ASN C 300 140.21 71.23 REMARK 500 ASP C 321A 92.33 76.83 REMARK 500 LEU C 369 46.33 -80.09 REMARK 500 THR C 450 67.44 -104.54 REMARK 500 LEU C 452 146.55 -170.86 REMARK 500 LEU C 454 153.31 -49.28 REMARK 500 THR C 461 -147.06 54.64 REMARK 500 SER C 463 -175.77 -170.13 REMARK 500 REMARK 500 THIS ENTRY HAS 105 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 E 196 ASN E 197 144.73 REMARK 500 TYR E 384 CYS E 385 -149.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-41415 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-41416 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-41417 RELATED DB: EMDB DBREF 8TNG A 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 8TNG B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8TNG C 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 8TNG D 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8TNG E 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 8TNG F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8TNG H 1 113 PDB 8TNG 8TNG 1 113 DBREF 8TNG I 1 113 PDB 8TNG 8TNG 1 113 DBREF 8TNG J 1 113 PDB 8TNG 8TNG 1 113 SEQADV 8TNG CYS A 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 8TNG ASN A 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8TNG CYS A 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 8TNG CYS A 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8TNG ARG A 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG A 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG A 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG A 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG A 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG PRO B 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8TNG CYS B 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8TNG CYS C 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 8TNG ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8TNG CYS C 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 8TNG CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8TNG ARG C 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG C 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG C 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG C 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG C 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG PRO D 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8TNG CYS D 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8TNG CYS E 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 8TNG ASN E 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8TNG CYS E 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 8TNG CYS E 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8TNG ARG E 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG E 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG E 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG E 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG ARG E 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8TNG PRO F 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8TNG CYS F 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 A 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 A 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 A 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 A 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 A 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 A 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 A 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 A 481 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 A 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 A 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 A 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 A 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 A 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 A 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 A 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 A 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 A 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 A 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 A 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 A 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 A 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 A 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 A 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 A 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 A 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 A 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 A 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 A 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 A 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 A 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 A 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 C 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 C 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 C 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 C 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 C 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 C 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 C 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 C 481 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 C 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 C 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 C 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 C 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 C 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 C 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 C 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 C 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 C 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 C 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 C 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 C 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 C 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 C 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 C 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 C 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 C 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 C 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 C 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 C 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 C 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 C 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 C 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 D 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 E 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 E 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 E 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 E 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 E 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 E 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 E 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 E 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 E 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 E 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 E 481 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 E 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 E 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 E 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 E 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 E 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 E 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 E 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 E 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 E 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 E 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 E 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 E 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 E 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 E 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 E 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 E 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 E 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 E 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 E 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 E 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 E 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 E 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 E 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 H 121 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 121 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 H 121 PHE ASP LEU GLU ASN TYR SER ILE GLY TRP PHE ARG GLN SEQRES 4 H 121 ALA PRO GLY LYS ALA ARG GLU GLY VAL ALA CYS LEU SER SEQRES 5 H 121 LYS ASN SER GLY ILE GLY HIS SER VAL LYS GLY ARG PHE SEQRES 6 H 121 THR ILE SER ARG ASP GLY ASP SER ASN THR TRP PHE LEU SEQRES 7 H 121 GLN MET GLY ALA LEU GLU ALA GLU ASP THR ALA VAL TYR SEQRES 8 H 121 THR CYS ALA THR TYR ASN ARG ALA CYS ALA ASN TYR VAL SEQRES 9 H 121 THR ILE TRP PRO GLU PHE ARG GLY GLN GLY THR GLN VAL SEQRES 10 H 121 THR VAL SER SER SEQRES 1 I 121 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 I 121 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 I 121 PHE ASP LEU GLU ASN TYR SER ILE GLY TRP PHE ARG GLN SEQRES 4 I 121 ALA PRO GLY LYS ALA ARG GLU GLY VAL ALA CYS LEU SER SEQRES 5 I 121 LYS ASN SER GLY ILE GLY HIS SER VAL LYS GLY ARG PHE SEQRES 6 I 121 THR ILE SER ARG ASP GLY ASP SER ASN THR TRP PHE LEU SEQRES 7 I 121 GLN MET GLY ALA LEU GLU ALA GLU ASP THR ALA VAL TYR SEQRES 8 I 121 THR CYS ALA THR TYR ASN ARG ALA CYS ALA ASN TYR VAL SEQRES 9 I 121 THR ILE TRP PRO GLU PHE ARG GLY GLN GLY THR GLN VAL SEQRES 10 I 121 THR VAL SER SER SEQRES 1 J 121 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 J 121 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 J 121 PHE ASP LEU GLU ASN TYR SER ILE GLY TRP PHE ARG GLN SEQRES 4 J 121 ALA PRO GLY LYS ALA ARG GLU GLY VAL ALA CYS LEU SER SEQRES 5 J 121 LYS ASN SER GLY ILE GLY HIS SER VAL LYS GLY ARG PHE SEQRES 6 J 121 THR ILE SER ARG ASP GLY ASP SER ASN THR TRP PHE LEU SEQRES 7 J 121 GLN MET GLY ALA LEU GLU ALA GLU ASP THR ALA VAL TYR SEQRES 8 J 121 THR CYS ALA THR TYR ASN ARG ALA CYS ALA ASN TYR VAL SEQRES 9 J 121 THR ILE TRP PRO GLU PHE ARG GLY GLN GLY THR GLN VAL SEQRES 10 J 121 THR VAL SER SER HET NAG G 1 14 HET NAG G 2 14 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 NAG M 1 14 HET NAG M 2 14 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 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 BMA S 3 11 HET MAN S 4 11 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET MAN Z 4 11 HET NAG a 1 14 HET NAG a 2 14 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET NAG d 1 14 HET NAG d 2 14 HET NAG e 1 14 HET NAG e 2 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG A 609 14 HET NAG A 610 14 HET NAG B 701 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HET NAG C 606 14 HET NAG C 607 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 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 10 NAG 71(C8 H15 N O6) FORMUL 11 BMA 3(C6 H12 O6) FORMUL 19 MAN 2(C6 H12 O6) HELIX 1 AA1 ASN A 98 SER A 115 1 18 HELIX 2 AA2 THR A 139 ARG A 151 5 5 HELIX 3 AA3 LYS A 335 ARG A 350 1 16 HELIX 4 AA4 THR B 529 SER B 534 1 6 HELIX 5 AA5 THR B 536 ASN B 543 1 8 HELIX 6 AA6 GLY B 572 VAL B 580 1 9 HELIX 7 AA7 VAL B 580 TRP B 596 1 17 HELIX 8 AA8 ASN B 618 MET B 626 1 9 HELIX 9 AA9 THR B 627 ILE B 635 1 9 HELIX 10 AB1 TYR B 638 ASP B 664 1 27 HELIX 11 AB2 ASN C 98 SER C 115 1 18 HELIX 12 AB3 TYR C 177 LEU C 179 5 3 HELIX 13 AB4 LYS C 335 ARG C 350 1 16 HELIX 14 AB5 ASN C 377 GLU C 381 5 5 HELIX 15 AB6 THR D 529 SER D 534 1 6 HELIX 16 AB7 THR D 536 ARG D 542 1 7 HELIX 17 AB8 GLN D 577 TRP D 596 1 20 HELIX 18 AB9 LEU D 619 ASP D 624 1 6 HELIX 19 AC1 THR D 627 ILE D 635 1 9 HELIX 20 AC2 TYR D 638 ASP D 664 1 27 HELIX 21 AC3 ASN E 94 ASN E 98 5 5 HELIX 22 AC4 ASN E 99 LYS E 117 1 19 HELIX 23 AC5 THR E 139 ARG E 151 5 5 HELIX 24 AC6 LYS E 335 ARG E 350 1 16 HELIX 25 AC7 THR F 529 SER F 534 1 6 HELIX 26 AC8 GLY F 572 TRP F 596 1 25 HELIX 27 AC9 LEU F 619 ASP F 624 1 6 HELIX 28 AD1 THR F 627 ILE F 635 1 9 HELIX 29 AD2 ILE F 641 ASP F 664 1 24 SHEET 1 AA1 3 GLY A 495 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL A 38 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 LYS A 487 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 LYS A 227 -1 N ALA A 224 O VAL A 489 SHEET 4 AA2 5 SER A 243 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 GLU A 83 ILE A 84 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 PHE A 53 ALA A 55 0 SHEET 2 AA3 2 HIS A 216 CYS A 218 -1 O CYS A 218 N PHE A 53 SHEET 1 AA4 3 LEU A 129 GLN A 130 0 SHEET 2 AA4 3 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 3 AA4 3 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA5 3 THR A 132 ASN A 133 0 SHEET 2 AA5 3 LYS A 155 THR A 162 -1 O ASN A 156 N THR A 132 SHEET 3 AA5 3 LYS A 169 PHE A 176 -1 O SER A 174 N CYS A 157 SHEET 1 AA6 2 MET A 271 SER A 274 0 SHEET 2 AA6 2 ILE A 284 GLN A 287 -1 O GLN A 287 N MET A 271 SHEET 1 AA7 4 SER A 413 PRO A 417 0 SHEET 2 AA7 4 HIS A 330 SER A 334 -1 N VAL A 333 O ILE A 414 SHEET 3 AA7 4 GLN A 293 THR A 297 -1 N ASN A 295 O ASN A 332 SHEET 4 AA7 4 ARG A 444 ASN A 448 -1 O SER A 447 N ILE A 294 SHEET 1 AA8 2 THR A 303 ARG A 308 0 SHEET 2 AA8 2 ALA A 316 GLY A 321 -1 O PHE A 317 N ILE A 307 SHEET 1 AA9 4 SER A 393 TRP A 395 0 SHEET 2 AA9 4 ILE A 359 PHE A 361 -1 N ILE A 359 O TRP A 395 SHEET 3 AA9 4 THR A 467 PRO A 470 1 O PHE A 468 N ARG A 360 SHEET 4 AA9 4 LEU A 454 ARG A 456 -1 N THR A 455 O ARG A 469 SHEET 1 AB1 3 ASN A 377 CYS A 378 0 SHEET 2 AB1 3 GLU A 381 PHE A 383 -1 O GLU A 381 N CYS A 378 SHEET 3 AB1 3 ILE A 420 LYS A 421 -1 O LYS A 421 N PHE A 382 SHEET 1 AB2 2 ILE A 423 ILE A 424 0 SHEET 2 AB2 2 MET A 434 TYR A 435 -1 N MET A 434 O ILE A 424 SHEET 1 AB3 2 TRP C 35 TYR C 39 0 SHEET 2 AB3 2 GLY C 495 THR C 499 -1 O THR C 499 N TRP C 35 SHEET 1 AB4 5 TRP C 45 ASP C 47 0 SHEET 2 AB4 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AB4 5 PHE C 223 LYS C 227 -1 N ALA C 224 O VAL C 489 SHEET 4 AB4 5 SER C 243 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB4 5 GLU C 83 ILE C 84 -1 N ILE C 84 O THR C 244 SHEET 1 AB5 2 PHE C 53 ALA C 55 0 SHEET 2 AB5 2 HIS C 216 CYS C 218 -1 O CYS C 218 N PHE C 53 SHEET 1 AB6 2 GLU C 91 PHE C 93 0 SHEET 2 AB6 2 GLY C 237 CYS C 239 -1 O CYS C 239 N GLU C 91 SHEET 1 AB7 5 LYS C 169 PHE C 176 0 SHEET 2 AB7 5 LYS C 155 THR C 162 -1 N CYS C 157 O SER C 174 SHEET 3 AB7 5 LEU C 129 CYS C 131 -1 N GLN C 130 O SER C 158 SHEET 4 AB7 5 LYS C 189 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB7 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AB8 2 MET C 271 SER C 274 0 SHEET 2 AB8 2 ILE C 284 GLN C 287 -1 O GLN C 287 N MET C 271 SHEET 1 AB9 4 SER C 413 PRO C 417 0 SHEET 2 AB9 4 HIS C 330 SER C 334 -1 N CYS C 331 O LEU C 416 SHEET 3 AB9 4 GLN C 293 THR C 297 -1 N ASN C 295 O ASN C 332 SHEET 4 AB9 4 ARG C 444 ASN C 448 -1 O SER C 447 N ILE C 294 SHEET 1 AC1 2 ARG C 304 ARG C 308 0 SHEET 2 AC1 2 ALA C 316 THR C 320 -1 O PHE C 317 N ILE C 307 SHEET 1 AC2 4 SER C 393 TRP C 395 0 SHEET 2 AC2 4 ILE C 359 PHE C 361 -1 N ILE C 359 O TRP C 395 SHEET 3 AC2 4 THR C 467 PRO C 470 1 O PHE C 468 N ARG C 360 SHEET 4 AC2 4 LEU C 454 ARG C 456 -1 N THR C 455 O ARG C 469 SHEET 1 AC3 2 PHE C 382 PHE C 383 0 SHEET 2 AC3 2 ILE C 420 LYS C 421 -1 O LYS C 421 N PHE C 382 SHEET 1 AC4 3 GLY E 495 THR E 499 0 SHEET 2 AC4 3 TRP E 35 TYR E 39 -1 N TRP E 35 O THR E 499 SHEET 3 AC4 3 CYS F 604 PRO F 609 -1 O CYS F 604 N VAL E 38 SHEET 1 AC5 5 TRP E 45 ASP E 47 0 SHEET 2 AC5 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AC5 5 PHE E 223 LYS E 227 -1 N ALA E 224 O VAL E 489 SHEET 4 AC5 5 SER E 243 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC5 5 GLU E 83 ILE E 84 -1 N ILE E 84 O THR E 244 SHEET 1 AC6 2 PHE E 53 ALA E 55 0 SHEET 2 AC6 2 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AC7 5 VAL E 172 PHE E 176 0 SHEET 2 AC7 5 LYS E 155 PHE E 159 -1 N LYS E 155 O PHE E 176 SHEET 3 AC7 5 LEU E 129 THR E 132 -1 N GLN E 130 O SER E 158 SHEET 4 AC7 5 LYS E 189 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC7 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC8 2 MET E 271 SER E 274 0 SHEET 2 AC8 2 ILE E 284 GLN E 287 -1 O LEU E 285 N ARG E 273 SHEET 1 AC9 4 SER E 413 PRO E 417 0 SHEET 2 AC9 4 HIS E 330 SER E 334 -1 N CYS E 331 O LEU E 416 SHEET 3 AC9 4 ILE E 294 THR E 297 -1 N ASN E 295 O ASN E 332 SHEET 4 AC9 4 ARG E 444 SER E 447 -1 O CYS E 445 N CYS E 296 SHEET 1 AD1 2 ARG E 304 ARG E 308 0 SHEET 2 AD1 2 ALA E 316 THR E 320 -1 O PHE E 317 N ILE E 307 SHEET 1 AD2 4 SER E 393 TRP E 395 0 SHEET 2 AD2 4 ILE E 359 PHE E 361 -1 N ILE E 359 O TRP E 395 SHEET 3 AD2 4 THR E 467 PRO E 470 1 O PHE E 468 N ARG E 360 SHEET 4 AD2 4 LEU E 454 ARG E 456 -1 N THR E 455 O ARG E 469 SHEET 1 AD3 3 ASN E 377 CYS E 378 0 SHEET 2 AD3 3 GLU E 381 PHE E 383 -1 O GLU E 381 N CYS E 378 SHEET 3 AD3 3 ILE E 420 LYS E 421 -1 O LYS E 421 N PHE E 382 SHEET 1 AD4 4 LEU H 4 SER H 7 0 SHEET 2 AD4 4 SER H 21 ALA H 24 -1 O VAL H 23 N GLN H 5 SHEET 3 AD4 4 THR H 77 GLN H 81 -1 O TRP H 78 N CYS H 22 SHEET 4 AD4 4 THR H 68 SER H 70 -1 N THR H 68 O GLN H 81 SHEET 1 AD5 3 LEU H 11 VAL H 12 0 SHEET 2 AD5 3 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AD5 3 ALA H 88 TYR H 90 -1 N TYR H 90 O THR H 107 SHEET 1 AD6 3 ARG H 45 CYS H 50 0 SHEET 2 AD6 3 SER H 33 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 3 AD6 3 THR H 94 TYR H 95 -1 O TYR H 95 N SER H 33 SHEET 1 AD7 4 LEU I 4 SER I 7 0 SHEET 2 AD7 4 SER I 17 ALA I 24 -1 O VAL I 23 N GLN I 5 SHEET 3 AD7 4 THR I 77 GLY I 82A-1 O LEU I 80 N LEU I 20 SHEET 4 AD7 4 THR I 68 SER I 70 -1 N THR I 68 O GLN I 81 SHEET 1 AD8 3 GLY I 10 VAL I 12 0 SHEET 2 AD8 3 THR I 107 VAL I 111 1 O THR I 110 N VAL I 12 SHEET 3 AD8 3 ALA I 88 TYR I 90 -1 N TYR I 90 O THR I 107 SHEET 1 AD9 3 GLY I 47 CYS I 50 0 SHEET 2 AD9 3 SER I 33 PHE I 37 -1 N TRP I 36 O ALA I 49 SHEET 3 AD9 3 THR I 94 TYR I 95 -1 O TYR I 95 N SER I 33 SHEET 1 AE1 4 GLN J 5 SER J 7 0 SHEET 2 AE1 4 SER J 17 VAL J 23 -1 O VAL J 23 N GLN J 5 SHEET 3 AE1 4 THR J 77 GLY J 82A-1 O LEU J 80 N LEU J 20 SHEET 4 AE1 4 THR J 68 ARG J 71 -1 N THR J 68 O GLN J 81 SHEET 1 AE2 3 GLY J 10 VAL J 12 0 SHEET 2 AE2 3 THR J 107 VAL J 111 1 O THR J 110 N VAL J 12 SHEET 3 AE2 3 ALA J 88 TYR J 90 -1 N TYR J 90 O THR J 107 SHEET 1 AE3 3 ARG J 45 CYS J 50 0 SHEET 2 AE3 3 SER J 33 GLN J 39 -1 N ARG J 38 O GLU J 46 SHEET 3 AE3 3 THR J 94 TYR J 95 -1 O TYR J 95 N SER J 33 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.04 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 201 CYS A 433 1555 1555 2.04 SSBOND 6 CYS A 218 CYS A 247 1555 1555 2.04 SSBOND 7 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 8 CYS A 296 CYS A 331 1555 1555 2.04 SSBOND 9 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 10 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 11 CYS A 501 CYS B 605 1555 1555 2.02 SSBOND 12 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 13 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 14 CYS C 119 CYS C 205 1555 1555 2.04 SSBOND 15 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 16 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 17 CYS C 201 CYS C 433 1555 1555 2.03 SSBOND 18 CYS C 218 CYS C 247 1555 1555 2.04 SSBOND 19 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 20 CYS C 296 CYS C 331 1555 1555 2.04 SSBOND 21 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 22 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 23 CYS C 501 CYS D 605 1555 1555 2.03 SSBOND 24 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 25 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 26 CYS E 119 CYS E 205 1555 1555 2.04 SSBOND 27 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 28 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 29 CYS E 201 CYS E 433 1555 1555 2.03 SSBOND 30 CYS E 218 CYS E 247 1555 1555 2.04 SSBOND 31 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 32 CYS E 296 CYS E 331 1555 1555 2.04 SSBOND 33 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 34 CYS E 385 CYS E 418 1555 1555 2.05 SSBOND 35 CYS E 501 CYS F 605 1555 1555 2.04 SSBOND 36 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 37 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 38 CYS H 50 CYS H 99 1555 1555 2.03 SSBOND 39 CYS I 22 CYS I 92 1555 1555 2.04 SSBOND 40 CYS I 50 CYS I 99 1555 1555 2.03 SSBOND 41 CYS J 22 CYS J 92 1555 1555 2.04 SSBOND 42 CYS J 50 CYS J 99 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG A 601 1555 1555 1.45 LINK ND2 ASN A 133 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG G 1 1555 1555 1.43 LINK ND2 ASN A 160 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG A 610 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG L 1 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG M 1 1555 1555 1.45 LINK ND2 ASN A 301 C1 NAG A 609 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 608 1555 1555 1.45 LINK ND2 ASN A 363 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG A 606 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 607 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.45 LINK ND2 ASN C 88 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN C 133 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG C 606 1555 1555 1.45 LINK ND2 ASN C 234 C1 NAG C 602 1555 1555 1.45 LINK ND2 ASN C 262 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG C 607 1555 1555 1.46 LINK ND2 ASN C 332 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 604 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 1.45 LINK ND2 ASN E 156 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG E 609 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG b 1 1555 1555 1.43 LINK ND2 ASN E 301 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 608 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG E 606 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 607 1555 1555 1.45 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 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 R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.44 LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.45 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.44 LINK O3 BMA Z 3 C1 MAN Z 4 1555 1555 1.45 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.45 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