HEADER VIRAL PROTEIN/RECEPTOR/IMMUNE SYSTEM 15-JUN-98 1GC1
TITLE HIV-1 GP120 CORE COMPLEXED WITH CD4 AND A NEUTRALIZING HUMAN ANTIBODY
CAVEAT 1GC1 NAG A 1 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENVELOPE PROTEIN GP120;
COMPND 3 CHAIN: G;
COMPND 4 FRAGMENT: CORE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CD4;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: D1D2, N-TERMINAL TWO DOMAIN FRAGMENT;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ANTIBODY 17B;
COMPND 15 CHAIN: L;
COMPND 16 FRAGMENT: ANTIGEN-BINDING FRAGMENT, FAB;
COMPND 17 ENGINEERED: YES;
COMPND 18 OTHER_DETAILS: MONOCLONAL ANTIBODY 17B BINDS TO A CD4-INDUCED SITE ON
COMPND 19 GP120;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: ANTIBODY 17B;
COMPND 22 CHAIN: H;
COMPND 23 FRAGMENT: ANTIGEN-BINDING FRAGMENT, FAB;
COMPND 24 ENGINEERED: YES;
COMPND 25 OTHER_DETAILS: MONOCLONAL ANTIBODY 17B BINDS TO A CD4-INDUCED SITE ON
COMPND 26 GP120
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: CLADE B;
SOURCE 5 VARIANT: HXBC2;
SOURCE 6 ORGAN: OVARY;
SOURCE 7 GENE: ENV;
SOURCE 8 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 11 OTHER_DETAILS: SECRETED FROM DROSOPHILA SCHNEIDER 2 LINES UNDER
SOURCE 12 CONTROL OF AN INDUCIBLE METALLOTHIONEIN PROMOTER;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: CHO;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 26 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 28 OTHER_DETAILS: EPSTEIN-BARR VIRUS IMMORTALIZED B-CELL CLONE FUSED
SOURCE 29 WITH A MURINE B-CELL FUSION PARTNER;
SOURCE 30 MOL_ID: 4;
SOURCE 31 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 32 ORGANISM_COMMON: HUMAN;
SOURCE 33 ORGANISM_TAXID: 9606;
SOURCE 34 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 35 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;
SOURCE 36 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 37 OTHER_DETAILS: EPSTEIN-BARR VIRUS IMMORTALIZED B-CELL CLONE FUSED
SOURCE 38 WITH A MURINE B-CELL FUSION PARTNER
KEYWDS COMPLEX (HIV ENVELOPE PROTEIN-CD4-FAB), HIV-1 EXTERIOR ENVELOPE
KEYWDS 2 GP120, T-CELL SURFACE GLYCOPROTEIN CD4, ANTIGEN-BINDING FRAGMENT OF
KEYWDS 3 HUMAN IMMUNOGLOBULIN 17B, GLYCOSYLATED PROTEIN, VIRAL PROTEIN-
KEYWDS 4 RECEPTOR-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.D.KWONG,R.WYATT,J.ROBINSON,R.W.SWEET,J.SODROSKI,W.A.HENDRICKSON
REVDAT 8 09-AUG-23 1GC1 1 REMARK HETSYN SHEET
REVDAT 7 29-JUL-20 1GC1 1 CAVEAT COMPND REMARK HET
REVDAT 7 2 1 HETNAM FORMUL LINK SITE
REVDAT 7 3 1 ATOM
REVDAT 6 28-JUN-17 1GC1 1 SOURCE DBREF SEQADV
REVDAT 5 18-SEP-13 1GC1 1 REMARK
REVDAT 4 13-JUL-11 1GC1 1 VERSN
REVDAT 3 24-FEB-09 1GC1 1 VERSN
REVDAT 2 19-AUG-98 1GC1 1 SSBOND SOURCE COMPND REMARK
REVDAT 2 2 1 DBREF SEQADV
REVDAT 1 08-JUL-98 1GC1 0
JRNL AUTH P.D.KWONG,R.WYATT,J.ROBINSON,R.W.SWEET,J.SODROSKI,
JRNL AUTH 2 W.A.HENDRICKSON
JRNL TITL STRUCTURE OF AN HIV GP120 ENVELOPE GLYCOPROTEIN IN COMPLEX
JRNL TITL 2 WITH THE CD4 RECEPTOR AND A NEUTRALIZING HUMAN ANTIBODY.
JRNL REF NATURE V. 393 648 1998
JRNL REFN ISSN 0028-0836
JRNL PMID 9641677
JRNL DOI 10.1038/31405
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 74.9
REMARK 3 NUMBER OF REFLECTIONS : 28620
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.302
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1430
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.58
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 42.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1518
REMARK 3 BIN R VALUE (WORKING SET) : 0.2876
REMARK 3 BIN FREE R VALUE : 0.3878
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 92
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7080
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 194
REMARK 3 SOLVENT ATOMS : 603
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.590
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.330 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.310 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.970 ; 1.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.010 ; 2.000
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARAM3_MOD.CHO
REMARK 3 PARAMETER FILE 2 : PARAMCSDX.MISC
REMARK 3 PARAMETER FILE 3 : PARAMCSDX_MOD.PRO
REMARK 3 PARAMETER FILE 4 : PARAM19.SOL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH3.CHO
REMARK 3 TOPOLOGY FILE 3 : TOPHCSDX.MISC
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GC1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173511.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : AUG-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4-7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00614
REMARK 200 MONOCHROMATOR : SILICON CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37724
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.56
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.24700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.170
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT +
REMARK 200 MULTIPLE ISOMORPHOUS REPLACEMENT + DENSITY MODIFICATION
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: PDB ENTRIES 1HIL, 1CDH AND 3CD4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION CRYSTALLIZATION: 0.5
REMARK 280 UL OF PROTEIN (~10MG/ML IN 350 MM NACL, 5 MM TRISCL PH 7.0) +
REMARK 280 0.4 UL OF 0.1 M NACITRATE, 0.02 M NAHEPES, 10% ISOPROPANOL, 10.5%
REMARK 280 MONOMETHYL-PEG 5000, 0.0075% SEAPREP AGAROSE, PH 6.4 OVER A
REMARK 280 RESERVOIR OF 0.35 M NACL, 0.1 M NACITRATE, 0.02 M NAHEPES, 10%
REMARK 280 ISOPROPANOL, 10.5% MONOMETHYL-PEG 5000, PH 6.4, VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 98.35000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 98.35000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, C, L, H, A, B, 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 GLY G 79
REMARK 465 ALA G 80
REMARK 465 ARG G 81
REMARK 465 SER G 82
REMARK 465 GLU G 83
REMARK 465 VAL G 84
REMARK 465 VAL G 85
REMARK 465 LEU G 86
REMARK 465 VAL G 87
REMARK 465 ASN G 88
REMARK 465 VAL G 89
REMARK 465 ASN G 397
REMARK 465 SER G 398
REMARK 465 THR G 399
REMARK 465 TRP G 400
REMARK 465 SER G 401
REMARK 465 THR G 402
REMARK 465 LYS G 403
REMARK 465 GLY G 404
REMARK 465 SER G 405
REMARK 465 ASN G 406
REMARK 465 ASN G 407
REMARK 465 THR G 408
REMARK 465 GLU G 409
REMARK 465 ALA C 182
REMARK 465 SER C 183
REMARK 465 ASN C 184
REMARK 465 THR C 185
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 GLU G 91 76.15 47.23
REMARK 500 MET G 95 -176.54 -170.82
REMARK 500 TRP G 96 44.87 -73.90
REMARK 500 LYS G 97 -88.25 -113.33
REMARK 500 ASN G 98 -145.72 -157.78
REMARK 500 ASP G 99 -60.49 153.82
REMARK 500 SER G 115 -83.88 -98.52
REMARK 500 PRO G 118 -135.06 -111.75
REMARK 500 LYS G 121 102.89 -162.14
REMARK 500 CYS G 126 173.41 -49.33
REMARK 500 VAL G 127 -57.71 -139.75
REMARK 500 THR G 198 88.24 -170.78
REMARK 500 CYS G 205 108.89 -49.41
REMARK 500 ALA G 221 -141.41 53.64
REMARK 500 ASN G 230 107.17 -59.27
REMARK 500 THR G 240 -75.00 -77.29
REMARK 500 THR G 248 -87.07 -59.15
REMARK 500 HIS G 249 -176.32 -172.37
REMARK 500 GLN G 258 -13.50 46.79
REMARK 500 GLU G 268 -79.08 -109.48
REMARK 500 ALA G 299 12.52 -63.77
REMARK 500 SER G 347 30.06 -75.24
REMARK 500 LYS G 348 8.80 -176.57
REMARK 500 ARG G 350 -52.47 8.70
REMARK 500 GLN G 352 71.61 90.83
REMARK 500 ASN G 356 145.60 167.39
REMARK 500 LYS G 357 177.23 178.18
REMARK 500 ASP G 368 152.05 -41.16
REMARK 500 PHE G 391 73.68 -118.97
REMARK 500 ASN G 392 83.08 -164.28
REMARK 500 ASN G 460 35.75 -143.01
REMARK 500 ASN G 462 3.66 57.76
REMARK 500 SER C 19 81.30 -52.65
REMARK 500 GLN C 20 28.96 48.51
REMARK 500 LYS C 22 -151.39 -121.30
REMARK 500 SER C 23 92.70 -50.77
REMARK 500 SER C 31 -4.28 -56.90
REMARK 500 GLN C 40 79.82 -153.99
REMARK 500 SER C 57 -163.20 -126.73
REMARK 500 GLU C 87 85.29 -66.98
REMARK 500 ASP C 88 77.34 55.48
REMARK 500 GLN C 89 88.29 -172.18
REMARK 500 LYS C 90 68.77 -67.68
REMARK 500 SER C 104 26.55 -68.51
REMARK 500 ASP C 105 -125.25 52.61
REMARK 500 THR C 106 -57.14 -151.28
REMARK 500 HIS C 107 82.73 -68.03
REMARK 500 LYS C 142 -77.58 175.86
REMARK 500 GLN C 165 10.29 59.61
REMARK 500 SER L 7 -71.62 -54.27
REMARK 500
REMARK 500 THIS ENTRY HAS 89 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH G 1157
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: O
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: WATER HOH 1000 (ZERO OCCUPANCY) MARKS THE
REMARK 800 LOCATION OF THE CENTRAL UNMODELLED DENSITY IN THE "PHE 43"
REMARK 800 CAVITY.
DBREF 1GC1 G 83 127 UNP P04578 ENV_HV1H2 83 127
DBREF 1GC1 G 195 297 UNP P04578 ENV_HV1H2 195 297
DBREF 1GC1 G 330 492 UNP P04578 ENV_HV1H2 330 492
DBREF 1GC1 C 1 185 UNP P01730 CD4_HUMAN 26 210
DBREF 1GC1 L 1 213 PDB 1GC1 1GC1 1 213
DBREF 1GC1 H 1 229 PDB 1GC1 1GC1 1 229
SEQADV 1GC1 GLY G 79 UNP P04578 EXPRESSION TAG
SEQADV 1GC1 ALA G 80 UNP P04578 EXPRESSION TAG
SEQADV 1GC1 ARG G 81 UNP P04578 EXPRESSION TAG
SEQADV 1GC1 SER G 82 UNP P04578 EXPRESSION TAG
SEQADV 1GC1 GLY G 128 UNP P04578 LINKER
SEQADV 1GC1 ALA G 129 UNP P04578 LINKER
SEQADV 1GC1 GLY G 194 UNP P04578 LINKER
SEQADV 1GC1 GLY G 298 UNP P04578 LINKER
SEQADV 1GC1 ALA G 299 UNP P04578 LINKER
SEQADV 1GC1 GLY G 329 UNP P04578 LINKER
SEQADV 1GC1 LYS G 403 UNP P04578 GLU 403 CONFLICT
SEQADV 1GC1 ASN C 184 UNP P01730 SER 209 ENGINEERED MUTATION
SEQADV 1GC1 THR C 185 UNP P01730 ILE 210 ENGINEERED MUTATION
SEQRES 1 G 321 GLY ALA ARG SER GLU VAL VAL LEU VAL ASN VAL THR GLU
SEQRES 2 G 321 ASN PHE ASN MET TRP LYS ASN ASP MET VAL GLU GLN MET
SEQRES 3 G 321 HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU LYS
SEQRES 4 G 321 PRO CYS VAL LYS LEU THR PRO LEU CYS VAL GLY ALA GLY
SEQRES 5 G 321 SER CYS ASN THR SER VAL ILE THR GLN ALA CYS PRO LYS
SEQRES 6 G 321 VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO
SEQRES 7 G 321 ALA GLY PHE ALA ILE LEU LYS CYS ASN ASN LYS THR PHE
SEQRES 8 G 321 ASN GLY THR GLY PRO CYS THR ASN VAL SER THR VAL GLN
SEQRES 9 G 321 CYS THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU
SEQRES 10 G 321 LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE
SEQRES 11 G 321 ARG SER VAL ASN PHE THR ASP ASN ALA LYS THR ILE ILE
SEQRES 12 G 321 VAL GLN LEU ASN THR SER VAL GLU ILE ASN CYS THR GLY
SEQRES 13 G 321 ALA GLY HIS CYS ASN ILE SER ARG ALA LYS TRP ASN ASN
SEQRES 14 G 321 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN PHE
SEQRES 15 G 321 GLY ASN ASN LYS THR ILE ILE PHE LYS GLN SER SER GLY
SEQRES 16 G 321 GLY ASP PRO GLU ILE VAL THR HIS SER PHE ASN CYS GLY
SEQRES 17 G 321 GLY GLU PHE PHE TYR CYS ASN SER THR GLN LEU PHE ASN
SEQRES 18 G 321 SER THR TRP PHE ASN SER THR TRP SER THR LYS GLY SER
SEQRES 19 G 321 ASN ASN THR GLU GLY SER ASP THR ILE THR LEU PRO CYS
SEQRES 20 G 321 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN LYS VAL GLY
SEQRES 21 G 321 LYS ALA MET TYR ALA PRO PRO ILE SER GLY GLN ILE ARG
SEQRES 22 G 321 CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP
SEQRES 23 G 321 GLY GLY ASN SER ASN ASN GLU SER GLU ILE PHE ARG PRO
SEQRES 24 G 321 GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU
SEQRES 25 G 321 TYR LYS TYR LYS VAL VAL LYS ILE GLU
SEQRES 1 C 185 LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU
SEQRES 2 C 185 LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE
SEQRES 3 C 185 HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN
SEQRES 4 C 185 GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN
SEQRES 5 C 185 ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY
SEQRES 6 C 185 ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP
SEQRES 7 C 185 SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU
SEQRES 8 C 185 GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SER
SEQRES 9 C 185 ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU THR
SEQRES 10 C 185 LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN CYS
SEQRES 11 C 185 ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS THR
SEQRES 12 C 185 LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY THR
SEQRES 13 C 185 TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL GLU
SEQRES 14 C 185 PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS ALA
SEQRES 15 C 185 SER ASN THR
SEQRES 1 L 213 GLU LEU GLU LEU THR GLN SER PRO ALA THR LEU SER VAL
SEQRES 2 L 213 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER
SEQRES 3 L 213 GLU SER VAL SER SER ASP LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 L 213 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER
SEQRES 5 L 213 THR ARG ALA THR GLY VAL PRO ALA ARG PHE SER GLY SER
SEQRES 6 L 213 GLY SER GLY ALA GLU PHE THR LEU THR ILE SER SER LEU
SEQRES 7 L 213 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR
SEQRES 8 L 213 ASN ASN TRP PRO PRO ARG TYR THR PHE GLY GLN GLY THR
SEQRES 9 L 213 ARG LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL
SEQRES 10 L 213 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY
SEQRES 11 L 213 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO
SEQRES 12 L 213 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU
SEQRES 13 L 213 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP
SEQRES 14 L 213 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR
SEQRES 15 L 213 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA
SEQRES 16 L 213 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR
SEQRES 17 L 213 LYS SER PHE ASN ARG
SEQRES 1 H 229 GLN VAL GLN LEU LEU GLU SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 229 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 H 229 ASP THR PHE ILE ARG TYR SER PHE THR TRP VAL ARG GLN
SEQRES 4 H 229 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ARG ILE ILE
SEQRES 5 H 229 THR ILE LEU ASP VAL ALA HIS TYR ALA PRO HIS LEU GLN
SEQRES 6 H 229 GLY ARG VAL THR ILE THR ALA ASP LYS SER THR SER THR
SEQRES 7 H 229 VAL TYR LEU GLU LEU ARG ASN LEU ARG SER ASP ASP THR
SEQRES 8 H 229 ALA VAL TYR PHE CYS ALA GLY VAL TYR GLU GLY GLU ALA
SEQRES 9 H 229 ASP GLU GLY GLU TYR ASP ASN ASN GLY PHE LEU LYS HIS
SEQRES 10 H 229 TRP GLY GLN GLY THR LEU VAL THR VAL THR SER ALA SER
SEQRES 11 H 229 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER
SEQRES 12 H 229 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU
SEQRES 13 H 229 VAL LYS ASP TYR PHE PRO GLN PRO VAL THR VAL SER TRP
SEQRES 14 H 229 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO
SEQRES 15 H 229 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER
SEQRES 16 H 229 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR
SEQRES 17 H 229 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS
SEQRES 18 H 229 VAL ASP LYS LYS VAL GLU PRO LYS
MODRES 1GC1 ASN G 197 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 234 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 262 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 276 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 289 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 295 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 332 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 339 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 386 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 392 ASN GLYCOSYLATION SITE
MODRES 1GC1 ASN G 448 ASN GLYCOSYLATION SITE
HET NAG A 1 14
HET FUC A 2 10
HET NAG B 1 14
HET FUC B 2 10
HET NAG D 1 14
HET FUC D 2 10
HET NAG E 1 14
HET FUC E 2 10
HET NAG G 697 14
HET NAG G 762 14
HET NAG G 776 14
HET NAG G 789 14
HET NAG G 832 14
HET NAG G 839 14
HET NAG G 886 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 5 NAG 11(C8 H15 N O6)
FORMUL 5 FUC 4(C6 H12 O5)
FORMUL 16 HOH *603(H2 O)
HELIX 1 GA1 MET G 100 LEU G 116 1 17
HELIX 2 GA2 ARG G 335 SER G 347 1 13
HELIX 3 GA3 ASP G 368 THR G 373 1 6
HELIX 4 GA4 THR G 388 PHE G 391 5SLIGHTLY NON-STANDARD 4
HELIX 5 GA5 MET G 475 TYR G 484 1 10
HELIX 6 CA1 ARG C 58 GLY C 65 5IRREGULAR 8
HELIX 7 CA2 LYS C 75 SER C 79 5 5
HELIX 8 CA3 GLU C 150 SER C 154 5 5
HELIX 9 LA1 SER L 123 GLY L 130 1 8
HELIX 10 LA2 LYS L 185 GLU L 189 1 5
HELIX 11 HA1 THR H 28 ILE H 30 5 3
HELIX 12 HA2 ARG H 87 THR H 91 5 5
HELIX 13 HA3 SER H 171 ALA H 173 5 3
SHEET 1 A 2 ASN G 92 ASN G 94 0
SHEET 2 A 2 GLY G 237 CYS G 239 -1
SHEET 1 B 4 SER G 199 ILE G 201 0
SHEET 2 B 4 CYS G 119 THR G 123 -1
SHEET 3 B 4 VAL G 430 TYR G 435 -1
SHEET 4 B 4 GLN G 422 MET G 426 -1
SHEET 1 C 2 PRO G 214 ALA G 219 0
SHEET 2 C 2 GLN G 246 ILE G 251 -1
SHEET 1 D 3 ASN G 241 VAL G 245 0
SHEET 2 D 3 GLY G 222 ASN G 229 -1
SHEET 3 D 3 LYS G 485 ILE G 491 -1
SHEET 1 E 7 LEU G 261 GLY G 263 0
SHEET 2 E 7 ILE G 443 ILE G 449 1
SHEET 3 E 7 VAL G 292 GLY G 298 -1
SHEET 4 E 7 GLY G 329 SER G 334 -1
SHEET 5 E 7 ASP G 412 LYS G 421 -1
SHEET 6 E 7 GLU G 381 ASN G 386 -1
SHEET 7 E 7 HIS G 374 CYS G 378 -1
SHEET 1 F 6 VAL G 271 ARG G 273 0
SHEET 2 F 6 ILE G 284 LEU G 288 -1
SHEET 3 F 6 THR G 450 ASP G 457 -1
SHEET 4 F 6 GLU G 464 GLY G 471 -1
SHEET 5 F 6 THR G 358 LYS G 362 1
SHEET 6 F 6 SER G 393 TRP G 395 -1
SHEET 1 G 7 LYS C 2 LYS C 7 0
SHEET 2 G 7 GLN C 89 PHE C 98 1 N GLN C 94 O LYS C 2
SHEET 3 G 7 ASP C 80 VAL C 86 -1 N VAL C 86 O GLN C 89
SHEET 4 G 7 HIS C 27 LYS C 29 -1 N LYS C 29 O ILE C 83
SHEET 5 G 7 LYS C 35 GLN C 40 -1 N LEU C 37 O TRP C 28
SHEET 6 G 7 PHE C 43 LYS C 46 -1 N THR C 45 O GLY C 38
SHEET 7 G 7 GLY G 366 GLY G 367 -1 N GLY G 367 O LEU C 44
SHEET 1 H 2 VAL C 12 LEU C 14 0
SHEET 2 H 2 LEU C 69 ILE C 71 -1 N ILE C 71 O VAL C 12
SHEET 1 I 3 GLY C 99 ALA C 102 0
SHEET 2 I 3 LEU C 114 GLU C 119 -1 N GLU C 119 O GLY C 99
SHEET 3 I 3 THR C 143 VAL C 146 -1 N VAL C 146 O LEU C 114
SHEET 1 J 2 HIS C 107 LEU C 109 0
SHEET 2 J 2 VAL C 175 LEU C 177 1 N VAL C 175 O LEU C 108
SHEET 1 K 4 ASN C 137 GLY C 140 0
SHEET 2 K 4 SER C 127 ARG C 131 -1 N CYS C 130 O ILE C 138
SHEET 3 K 4 GLY C 155 GLN C 163 -1 N LEU C 162 O SER C 127
SHEET 4 K 4 LYS C 166 ILE C 174 -1 N ILE C 174 O GLY C 155
SHEET 1 L 4 LEU L 4 GLN L 6 0
SHEET 2 L 4 ALA L 19 ALA L 25 -1 N ARG L 24 O THR L 5
SHEET 3 L 4 GLU L 70 ILE L 75 -1 N ILE L 75 O ALA L 19
SHEET 4 L 4 PHE L 62 SER L 67 -1 N SER L 67 O GLU L 70
SHEET 1 M 5 THR L 10 VAL L 13 0
SHEET 2 M 5 THR L 104 ILE L 108 1 N ARG L 105 O LEU L 11
SHEET 3 M 5 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 104
SHEET 4 M 5 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85
SHEET 5 M 5 ARG L 45 ILE L 48 -1 N ILE L 48 O TRP L 35
SHEET 1 N 4 SER L 116 PHE L 120 0
SHEET 2 N 4 THR L 131 ASN L 139 -1 N ASN L 139 O SER L 116
SHEET 3 N 4 LEU L 177 SER L 184 -1 N LEU L 183 O ALA L 132
SHEET 4 N 4 SER L 161 VAL L 165 -1 N SER L 164 O SER L 178
SHEET 1 O 3 LYS L 147 TRP L 150 0
SHEET 2 O 3 VAL L 193 THR L 199 -1 N THR L 199 O LYS L 147
SHEET 3 O 3 VAL L 207 ASN L 212 -1 N PHE L 211 O TYR L 194
SHEET 1 P 4 GLN H 3 GLU H 6 0
SHEET 2 P 4 VAL H 18 SER H 25 -1 N SER H 25 O GLN H 3
SHEET 3 P 4 THR H 78 LEU H 83 -1 N LEU H 83 O VAL H 18
SHEET 4 P 4 VAL H 68 ASP H 73 -1 N ASP H 73 O THR H 78
SHEET 1 Q 6 GLU H 10 LYS H 12 0
SHEET 2 Q 6 THR H 122 VAL H 126 1 N THR H 125 O GLU H 10
SHEET 3 Q 6 ALA H 92 TYR H 100 -1 N TYR H 94 O THR H 122
SHEET 4 Q 6 TYR H 32 GLN H 39 -1 N GLN H 39 O VAL H 93
SHEET 5 Q 6 LEU H 45 ILE H 52 -1 N ILE H 51 O PHE H 34
SHEET 6 Q 6 VAL H 57 TYR H 60 -1 N HIS H 59 O ARG H 50
SHEET 1 R 4 SER H 135 LEU H 139 0
SHEET 2 R 4 THR H 150 TYR H 160 -1 N LYS H 158 O SER H 135
SHEET 3 R 4 TYR H 191 PRO H 200 -1 N VAL H 199 O ALA H 151
SHEET 4 R 4 VAL H 178 THR H 180 -1 N HIS H 179 O VAL H 196
SHEET 1 S 3 VAL H 165 TRP H 169 0
SHEET 2 S 3 ILE H 210 HIS H 215 -1 N ASN H 214 O THR H 166
SHEET 3 S 3 THR H 220 LYS H 225 -1 N LYS H 224 O CYS H 211
SSBOND 1 CYS G 119 CYS G 205 1555 1555 2.04
SSBOND 2 CYS G 126 CYS G 196 1555 1555 2.04
SSBOND 3 CYS G 218 CYS G 247 1555 1555 2.03
SSBOND 4 CYS G 228 CYS G 239 1555 1555 2.03
SSBOND 5 CYS G 296 CYS G 331 1555 1555 2.03
SSBOND 6 CYS G 331 CYS G 385 1555 1555 2.74
SSBOND 7 CYS G 378 CYS G 445 1555 1555 2.03
SSBOND 8 CYS G 385 CYS G 418 1555 1555 2.03
SSBOND 9 CYS C 16 CYS C 84 1555 1555 2.03
SSBOND 10 CYS C 130 CYS C 159 1555 1555 2.03
SSBOND 11 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 12 CYS L 136 CYS L 196 1555 1555 2.02
SSBOND 13 CYS H 22 CYS H 96 1555 1555 2.02
SSBOND 14 CYS H 155 CYS H 211 1555 1555 2.02
LINK ND2 ASN G 197 C1 NAG G 697 1555 1555 1.46
LINK ND2 ASN G 234 C1 NAG A 1 1555 1555 1.46
LINK ND2 ASN G 262 C1 NAG G 762 1555 1555 1.46
LINK ND2 ASN G 276 C1 NAG G 776 1555 1555 1.45
LINK ND2 ASN G 289 C1 NAG G 789 1555 1555 1.45
LINK ND2 ASN G 295 C1 NAG B 1 1555 1555 1.46
LINK ND2 ASN G 332 C1 NAG G 832 1555 1555 1.45
LINK ND2 ASN G 339 C1 NAG G 839 1555 1555 1.45
LINK ND2 ASN G 386 C1 NAG G 886 1555 1555 1.45
LINK ND2 ASN G 392 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN G 448 C1 NAG E 1 1555 1555 1.46
LINK O6 NAG A 1 C1 FUC A 2 1555 1555 1.40
LINK O6 NAG B 1 C1 FUC B 2 1555 1555 1.40
LINK O6 NAG D 1 C1 FUC D 2 1555 1555 1.41
LINK O6 NAG E 1 C1 FUC E 2 1555 1555 1.41
CISPEP 1 TRP L 94 PRO L 95 0 -1.61
SITE 1 O 1 HOH G1157
CRYST1 71.640 88.130 196.700 90.00 90.00 90.00 P 2 2 21 4
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 0.013959 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005084 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
