HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-JUN-07 2QAD
TITLE STRUCTURE OF TYROSINE-SULFATED 412D ANTIBODY COMPLEXED WITH HIV-1 YU2
TITLE 2 GP120 AND CD4
CAVEAT 2QAD NAG A 862 HAS WRONG CHIRALITY AT ATOM C1 NAG A 894 HAS WRONG
CAVEAT 2 2QAD CHIRALITY AT ATOM C1 NAG E 862 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 2QAD C1 NAG E 963 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160;
COMPND 3 CHAIN: A, E;
COMPND 4 FRAGMENT: CORE WITH V3;
COMPND 5 SYNONYM: ENV POLYPROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4;
COMPND 9 CHAIN: B, F;
COMPND 10 FRAGMENT: D1D2, IG-LIKE V-TYPE AND IG-LIKE C2-TYPE 1 DOMAINS;
COMPND 11 SYNONYM: T-CELL SURFACE ANTIGEN T4/LEU-3;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ANTI-HIV-1 ANTIBODY 412D LIGHT CHAIN;
COMPND 15 CHAIN: C, G;
COMPND 16 FRAGMENT: FAB, ANTIGEN-BINDING FRAGMENT;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: ANTI-HIV-1 ANTIBODY 412D HEAVY CHAIN;
COMPND 20 CHAIN: D, H;
COMPND 21 FRAGMENT: FAB, ANTIGEN-BINDING FRAGMENT;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: YU2;
SOURCE 5 GENE: ENV;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: EMBRYONIC CELL LINE 293;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: CMVR;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: CD4;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 EXPRESSION_SYSTEM: HUMAN HERPESVIRUS 4;
SOURCE 24 EXPRESSION_SYSTEM_COMMON: EPSTEIN-BARR VIRUS;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 10376;
SOURCE 26 EXPRESSION_SYSTEM_STRAIN: EPSTEIN-BARR VIRUS;
SOURCE 27 MOL_ID: 4;
SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 29 ORGANISM_COMMON: HUMAN;
SOURCE 30 ORGANISM_TAXID: 9606;
SOURCE 31 EXPRESSION_SYSTEM: HUMAN HERPESVIRUS 4;
SOURCE 32 EXPRESSION_SYSTEM_COMMON: EPSTEIN-BARR VIRUS;
SOURCE 33 EXPRESSION_SYSTEM_TAXID: 10376;
SOURCE 34 EXPRESSION_SYSTEM_STRAIN: EPSTEIN-BARR VIRUS
KEYWDS VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-C.HUANG,M.TANG,J.ROBINSON,R.WYATT,P.D.KWONG
REVDAT 11 15-NOV-23 2QAD 1 REMARK
REVDAT 10 30-AUG-23 2QAD 1 HETSYN
REVDAT 9 29-JUL-20 2QAD 1 CAVEAT COMPND REMARK HETNAM
REVDAT 9 2 1 LINK SITE
REVDAT 8 24-JUL-19 2QAD 1 REMARK LINK
REVDAT 7 18-OCT-17 2QAD 1 REMARK
REVDAT 6 16-AUG-17 2QAD 1 SOURCE REMARK
REVDAT 5 29-APR-15 2QAD 1 HETSYN
REVDAT 4 13-JUL-11 2QAD 1 VERSN
REVDAT 3 24-FEB-09 2QAD 1 VERSN
REVDAT 2 09-OCT-07 2QAD 1 JRNL
REVDAT 1 25-SEP-07 2QAD 0
JRNL AUTH C.-C.HUANG,S.N.LAM,P.ACHARYA,M.TANG,S.-H.XIANG,S.S.HUSSAN,
JRNL AUTH 2 R.L.STANFIELD,J.ROBINSON,J.SODROSKI,I.A.WILSON,R.WYATT,
JRNL AUTH 3 C.A.BEWLEY,P.D.KWONG
JRNL TITL STRUCTURES OF THE CCR5 N TERMINUS AND OF A TYROSINE-SULFATED
JRNL TITL 2 ANTIBODY WITH HIV-1 GP120 AND CD4
JRNL REF SCIENCE V. 317 1930 2007
JRNL REFN ISSN 0036-8075
JRNL PMID 17901336
JRNL DOI 10.1126/SCIENCE.1145373
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 66.7
REMARK 3 NUMBER OF REFLECTIONS : 25600
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1329
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 156.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -46.38600
REMARK 3 B22 (A**2) : 16.91000
REMARK 3 B33 (A**2) : 29.47500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -20.02100
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TLS REFINEMENT WAS PERFORMED WITH
REMARK 3 PHENIX. THE ANISOTROPIC B-FACTOR IN ANISOU RECORDS IS THE TOTAL
REMARK 3 B-FACTOR (B_TLS + B_INDIVIDUAL). THE ISOTROPIC EQUIVALENT B-
REMARK 3 FACTOR IN ATOM RECORDS IS THE MEAN OF THE TRACE OF THE ANISOU
REMARK 3 MATRIX DIVIDED BY 10000 AND MULTIPLIED BY 8*PI^2 AND REPRESENTS
REMARK 3 THE ISOTROPIC EQUIVALENT OF THE TOTAL B-FACTOR (B_TLS + B_
REMARK 3 INDIVIDUAL). TO OBTAIN THE INDIVIDUAL B-FACTORS, ONE NEEDS TO
REMARK 3 COMPUTE THE TLS COMPONENT (B_TLS) USING THE TLS RECORDS IN THE
REMARK 3 PDB FILE HEADER AND THEN SUBTRACT IT FROM THE TOTAL B-FACTORS
REMARK 3 (ON THE ANISOU RECORDS).
REMARK 4
REMARK 4 2QAD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1000043349.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SI (220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25816
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 67.8
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.13300
REMARK 200 R SYM (I) : 0.13300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 16.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.53700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: YU2CORE/CD4 D1D2 FROM PDB ENTRY 1RZK AND 412D FAB
REMARK 200 FROM PDB ENTRY 1RZG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17-19% POLYETHYLENE GLYCOL (PEG) 1500,
REMARK 280 0.1 M NA CACODYLATE PH 6.5, 0.2 M NA MALONATE, PH 5.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 26.51050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 300 REMARK: THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF TWO GP120/CD4/412D COMPLEXES. CHAIN A, B, C, AND
REMARK 300 D FORM ONE COMPLEX, AND CHAIN E, F, G, AND H FORM THE OTHER.
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: A, B, C, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25710 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 89
REMARK 465 LYS A 398
REMARK 465 LEU A 399
REMARK 465 PHE B 179
REMARK 465 GLN B 180
REMARK 465 LYS B 181
REMARK 465 CYS C 214
REMARK 465 VAL E 89
REMARK 465 THR E 404
REMARK 465 ARG E 405
REMARK 465 LYS E 406
REMARK 465 LEU E 407
REMARK 465 ASN E 408
REMARK 465 ASN E 409
REMARK 465 THR E 410
REMARK 465 GLY E 411
REMARK 465 ARG E 412
REMARK 465 GLN F 180
REMARK 465 LYS F 181
REMARK 465 CYS G 214
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 ARG A 397 O CB
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 ND2 ASN E 332 C2 NAG E 832 2.05
REMARK 500 ND2 ASN A 289 C2 NAG A 789 2.10
REMARK 500 ND2 ASN E 301 C2 NAG E 801 2.18
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 PRO A 214 C - N - CA ANGL. DEV. = 9.2 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 LYS A 97 51.10 -109.02
REMARK 500 ASP A 113 31.85 -75.52
REMARK 500 GLN A 114 -17.68 -149.24
REMARK 500 LEU A 116 73.82 -175.82
REMARK 500 VAL A 120 123.58 -177.30
REMARK 500 PRO A 212 106.11 -52.93
REMARK 500 PRO A 214 146.76 -37.94
REMARK 500 ASN A 229 66.94 -108.37
REMARK 500 PRO A 238 129.93 -38.16
REMARK 500 ASN A 241 59.19 -97.18
REMARK 500 GLN A 258 -34.52 63.08
REMARK 500 GLU A 268 -108.63 -90.26
REMARK 500 THR A 297 136.05 -170.64
REMARK 500 ASN A 300 33.06 -95.39
REMARK 500 ILE A 326 5.16 -68.15
REMARK 500 ALA A 329 -160.70 -126.45
REMARK 500 GLU A 351 42.97 -90.99
REMARK 500 GLN A 352 -35.80 -156.11
REMARK 500 PRO A 363 171.77 -53.65
REMARK 500 HIS A 374 97.59 -53.94
REMARK 500 PHE A 376 169.67 174.19
REMARK 500 ASN A 386 86.88 -56.04
REMARK 500 SER A 387 39.12 -86.06
REMARK 500 PHE A 391 46.87 -104.43
REMARK 500 ASP A 395 -42.41 74.09
REMARK 500 THR A 402 -93.95 -81.83
REMARK 500 ARG A 412 -147.92 -119.50
REMARK 500 ASP A 457 100.10 -162.37
REMARK 500 ASP A 461 104.94 65.08
REMARK 500 THR A 462 57.07 -95.47
REMARK 500 ASN A 463 -61.54 74.51
REMARK 500 ILE A 491 69.42 -104.36
REMARK 500 SER B 19 -80.31 -54.40
REMARK 500 ASN B 30 -155.89 -93.11
REMARK 500 ASP B 56 -155.23 -166.26
REMARK 500 SER B 57 145.19 176.05
REMARK 500 PHE B 67 74.01 -113.39
REMARK 500 LYS B 75 -145.52 -85.51
REMARK 500 SER B 79 109.58 -51.36
REMARK 500 ASP B 88 -44.73 76.65
REMARK 500 ASN B 103 31.14 -95.47
REMARK 500 PRO B 122 85.67 -69.39
REMARK 500 GLN B 129 79.87 -157.49
REMARK 500 ARG B 131 117.63 -160.00
REMARK 500 LYS B 136 97.00 -67.63
REMARK 500 SER B 147 -99.84 -67.56
REMARK 500 GLN B 163 108.93 -176.90
REMARK 500 ASN B 164 49.92 71.85
REMARK 500 GLN B 165 17.12 58.18
REMARK 500 SER C 30 -136.22 63.22
REMARK 500
REMARK 500 THIS ENTRY HAS 199 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2QAD A 89 121 UNP P35961 ENV_HV1Y2 88 120
DBREF 2QAD A 199 492 UNP P35961 ENV_HV1Y2 195 479
DBREF 2QAD B 1 181 UNP P01730 CD4_HUMAN 26 206
DBREF 2QAD E 89 121 UNP P35961 ENV_HV1Y2 88 120
DBREF 2QAD E 199 492 UNP P35961 ENV_HV1Y2 195 479
DBREF 2QAD F 1 181 UNP P01730 CD4_HUMAN 26 206
DBREF 2QAD C 1 214 UNP Q6GMX8 Q6GMX8_HUMAN 23 236
DBREF 2QAD D 36 214 UNP A4F255 A4F255_HUMAN 33 228
DBREF 2QAD G 1 214 UNP Q6GMX8 Q6GMX8_HUMAN 23 236
DBREF 2QAD H 36 214 UNP A4F255 A4F255_HUMAN 33 228
SEQRES 1 A 322 VAL THR GLU ASN PHE ASN MET TRP LYS ASN ASN MET VAL
SEQRES 2 A 322 GLU GLN MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN
SEQRES 3 A 322 SER LEU LYS PRO CYS VAL LYS LEU THR GLY GLY SER VAL
SEQRES 4 A 322 ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE
SEQRES 5 A 322 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU
SEQRES 6 A 322 LYS CYS ASN ASP LYS LYS PHE ASN GLY THR GLY PRO CYS
SEQRES 7 A 322 THR ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE ARG
SEQRES 8 A 322 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU
SEQRES 9 A 322 ALA GLU GLU GLU ILE VAL ILE ARG SER GLU ASN PHE THR
SEQRES 10 A 322 ASN ASN ALA LYS THR ILE ILE VAL GLN LEU ASN GLU SER
SEQRES 11 A 322 VAL VAL ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG
SEQRES 12 A 322 LYS SER ILE ASN ILE GLY PRO GLY ARG ALA LEU TYR THR
SEQRES 13 A 322 THR GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS
SEQRES 14 A 322 ASN LEU SER LYS THR GLN TRP GLU ASN THR LEU GLU GLN
SEQRES 15 A 322 ILE ALA ILE LYS LEU LYS GLU GLN PHE GLY ASN ASN LYS
SEQRES 16 A 322 THR ILE ILE PHE ASN PRO SER SER GLY GLY ASP PRO GLU
SEQRES 17 A 322 ILE VAL THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE
SEQRES 18 A 322 TYR CYS ASN SER THR GLN LEU PHE THR TRP ASN ASP THR
SEQRES 19 A 322 ARG LYS LEU ASN ASN THR GLY ARG ASN ILE THR LEU PRO
SEQRES 20 A 322 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL
SEQRES 21 A 322 GLY LYS ALA MET TYR ALA PRO PRO ILE ARG GLY GLN ILE
SEQRES 22 A 322 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG
SEQRES 23 A 322 ASP GLY GLY LYS ASP THR ASN GLY THR GLU ILE PHE ARG
SEQRES 24 A 322 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU
SEQRES 25 A 322 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU
SEQRES 1 B 181 LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU
SEQRES 2 B 181 LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE
SEQRES 3 B 181 HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN
SEQRES 4 B 181 GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN
SEQRES 5 B 181 ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY
SEQRES 6 B 181 ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP
SEQRES 7 B 181 SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU
SEQRES 8 B 181 GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SER
SEQRES 9 B 181 ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU THR
SEQRES 10 B 181 LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN CYS
SEQRES 11 B 181 ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS THR
SEQRES 12 B 181 LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY THR
SEQRES 13 B 181 TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL GLU
SEQRES 14 B 181 PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS
SEQRES 1 C 214 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA
SEQRES 2 C 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 C 214 GLN SER ILE SER ASN TRP LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 C 214 PRO GLY ARG ALA PRO LYS LEU LEU MET TYR LYS ALA SER
SEQRES 5 C 214 SER LEU LYS SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 C 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU
SEQRES 7 C 214 GLN SER ASP ASP PHE ALA THR TYR TYR CYS GLN GLN HIS
SEQRES 8 C 214 ASP SER SER PRO TYR THR PHE GLY GLN GLY THR LYS LEU
SEQRES 9 C 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 C 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 C 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 C 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 C 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 C 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 C 214 LYS ALA ASP TYR GLU LYS HIS LYS LEU TYR ALA CYS GLU
SEQRES 16 C 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 C 214 PHE ASN ARG GLY GLU CYS
SEQRES 1 D 231 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 D 231 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 D 231 GLY THR PHE SER ASN TYR ALA ILE ASN TRP VAL ARG GLN
SEQRES 4 D 231 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 D 231 PRO ILE PHE ASN ILE ALA HIS TYR ALA GLN ARG PHE GLN
SEQRES 6 D 231 GLY ARG VAL SER ILE THR ALA ASP GLU SER THR SER THR
SEQRES 7 D 231 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 D 231 ALA VAL PHE TYR CYS ALA SER PRO TYR PRO ASN ASP TYS
SEQRES 9 D 231 ASN ASP TYS ALA PRO GLU GLU GLY MET SER TRP TYR PHE
SEQRES 10 D 231 ASP LEU TRP GLY ARG GLY THR LEU VAL THR VAL SER PRO
SEQRES 11 D 231 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO
SEQRES 12 D 231 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY
SEQRES 13 D 231 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 14 D 231 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR
SEQRES 15 D 231 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU
SEQRES 16 D 231 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR
SEQRES 17 D 231 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN
SEQRES 18 D 231 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 1 E 322 VAL THR GLU ASN PHE ASN MET TRP LYS ASN ASN MET VAL
SEQRES 2 E 322 GLU GLN MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN
SEQRES 3 E 322 SER LEU LYS PRO CYS VAL LYS LEU THR GLY GLY SER VAL
SEQRES 4 E 322 ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE
SEQRES 5 E 322 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU
SEQRES 6 E 322 LYS CYS ASN ASP LYS LYS PHE ASN GLY THR GLY PRO CYS
SEQRES 7 E 322 THR ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE ARG
SEQRES 8 E 322 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU
SEQRES 9 E 322 ALA GLU GLU GLU ILE VAL ILE ARG SER GLU ASN PHE THR
SEQRES 10 E 322 ASN ASN ALA LYS THR ILE ILE VAL GLN LEU ASN GLU SER
SEQRES 11 E 322 VAL VAL ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG
SEQRES 12 E 322 LYS SER ILE ASN ILE GLY PRO GLY ARG ALA LEU TYR THR
SEQRES 13 E 322 THR GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS
SEQRES 14 E 322 ASN LEU SER LYS THR GLN TRP GLU ASN THR LEU GLU GLN
SEQRES 15 E 322 ILE ALA ILE LYS LEU LYS GLU GLN PHE GLY ASN ASN LYS
SEQRES 16 E 322 THR ILE ILE PHE ASN PRO SER SER GLY GLY ASP PRO GLU
SEQRES 17 E 322 ILE VAL THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE
SEQRES 18 E 322 TYR CYS ASN SER THR GLN LEU PHE THR TRP ASN ASP THR
SEQRES 19 E 322 ARG LYS LEU ASN ASN THR GLY ARG ASN ILE THR LEU PRO
SEQRES 20 E 322 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL
SEQRES 21 E 322 GLY LYS ALA MET TYR ALA PRO PRO ILE ARG GLY GLN ILE
SEQRES 22 E 322 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG
SEQRES 23 E 322 ASP GLY GLY LYS ASP THR ASN GLY THR GLU ILE PHE ARG
SEQRES 24 E 322 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU
SEQRES 25 E 322 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU
SEQRES 1 F 181 LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU
SEQRES 2 F 181 LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE
SEQRES 3 F 181 HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN
SEQRES 4 F 181 GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN
SEQRES 5 F 181 ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY
SEQRES 6 F 181 ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP
SEQRES 7 F 181 SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU
SEQRES 8 F 181 GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SER
SEQRES 9 F 181 ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU THR
SEQRES 10 F 181 LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN CYS
SEQRES 11 F 181 ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS THR
SEQRES 12 F 181 LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY THR
SEQRES 13 F 181 TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL GLU
SEQRES 14 F 181 PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS
SEQRES 1 G 214 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA
SEQRES 2 G 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 G 214 GLN SER ILE SER ASN TRP LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 G 214 PRO GLY ARG ALA PRO LYS LEU LEU MET TYR LYS ALA SER
SEQRES 5 G 214 SER LEU LYS SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 G 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU
SEQRES 7 G 214 GLN SER ASP ASP PHE ALA THR TYR TYR CYS GLN GLN HIS
SEQRES 8 G 214 ASP SER SER PRO TYR THR PHE GLY GLN GLY THR LYS LEU
SEQRES 9 G 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 G 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 G 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 G 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 G 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 G 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 G 214 LYS ALA ASP TYR GLU LYS HIS LYS LEU TYR ALA CYS GLU
SEQRES 16 G 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 G 214 PHE ASN ARG GLY GLU CYS
SEQRES 1 H 231 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 231 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 H 231 GLY THR PHE SER ASN TYR ALA ILE ASN TRP VAL ARG GLN
SEQRES 4 H 231 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 H 231 PRO ILE PHE ASN ILE ALA HIS TYR ALA GLN ARG PHE GLN
SEQRES 6 H 231 GLY ARG VAL SER ILE THR ALA ASP GLU SER THR SER THR
SEQRES 7 H 231 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 H 231 ALA VAL PHE TYR CYS ALA SER PRO TYR PRO ASN ASP TYS
SEQRES 9 H 231 ASN ASP TYS ALA PRO GLU GLU GLY MET SER TRP TYR PHE
SEQRES 10 H 231 ASP LEU TRP GLY ARG GLY THR LEU VAL THR VAL SER PRO
SEQRES 11 H 231 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO
SEQRES 12 H 231 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY
SEQRES 13 H 231 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 14 H 231 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR
SEQRES 15 H 231 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU
SEQRES 16 H 231 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR
SEQRES 17 H 231 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN
SEQRES 18 H 231 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS
MODRES 2QAD ASN A 234 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 241 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 262 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 276 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 289 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 295 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 301 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 332 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 356 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 362 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 386 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 394 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 400 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 413 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 448 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN A 463 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 234 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 241 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 262 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 276 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 289 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 295 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 301 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 332 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 356 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 362 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 386 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 394 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 413 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 448 ASN GLYCOSYLATION SITE
MODRES 2QAD ASN E 463 ASN GLYCOSYLATION SITE
MODRES 2QAD TYS D 100 TYR O-SULFO-L-TYROSINE
MODRES 2QAD TYS D 100C TYR O-SULFO-L-TYROSINE
MODRES 2QAD TYS H 100 TYR O-SULFO-L-TYROSINE
MODRES 2QAD TYS H 100C TYR O-SULFO-L-TYROSINE
HET TYS D 100 16
HET TYS D 100C 16
HET TYS H 100 16
HET TYS H 100C 16
HET NAG A 734 14
HET NAG A 741 14
HET NAG A 762 14
HET NAG A 776 14
HET NAG A 789 14
HET NAG A 795 14
HET NAG A 801 14
HET NAG A 832 14
HET NAG A 856 14
HET NAG A 862 14
HET NAG A 886 14
HET NAG A 894 14
HET NAG A 900 14
HET NAG A 913 14
HET NAG A 948 14
HET NAG A 963 14
HET MLA A 3 7
HET EDO A 8 4
HET MLA B 186 7
HET EDO C 215 4
HET EDO C 216 4
HET EDO D 215 4
HET NAG E 734 14
HET NAG E 741 14
HET NAG E 762 14
HET NAG E 776 14
HET NAG E 789 14
HET NAG E 795 14
HET NAG E 801 14
HET NAG E 832 14
HET NAG E 856 14
HET NAG E 862 14
HET NAG E 886 14
HET NAG E 894 14
HET NAG E 913 14
HET NAG E 948 14
HET NAG E 963 14
HET EDO E 7 4
HET EDO E 10 4
HET MLA F 186 7
HET EDO F 187 4
HET MLA H 215 7
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MLA MALONIC ACID
HETNAM EDO 1,2-ETHANEDIOL
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 MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METHANEDICARBOXYLIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 TYS 4(C9 H11 N O6 S)
FORMUL 9 NAG 31(C8 H15 N O6)
FORMUL 25 MLA 4(C3 H4 O4)
FORMUL 26 EDO 7(C2 H6 O2)
HELIX 1 1 ASN A 99 ASP A 113 1 15
HELIX 2 2 LYS A 335 GLY A 354 1 20
HELIX 3 3 ASP A 368 THR A 373 1 6
HELIX 4 4 ASP A 474 SER A 481 1 8
HELIX 5 5 ARG B 58 GLY B 65 5 8
HELIX 6 6 GLU B 150 SER B 154 5 5
HELIX 7 7 SER C 121 LYS C 126 1 6
HELIX 8 8 LYS C 183 LYS C 188 1 6
HELIX 9 9 THR D 28 TYR D 32 5 5
HELIX 10 10 GLN D 61 GLN D 64 5 4
HELIX 11 11 ARG D 83 THR D 87 5 5
HELIX 12 12 HIS D 200 ASN D 204 5 5
HELIX 13 13 ASN E 99 ASP E 113 1 15
HELIX 14 14 SER E 334 GLY E 354 1 21
HELIX 15 15 ASP E 368 THR E 373 1 6
HELIX 16 16 ASP E 474 SER E 481 1 8
HELIX 17 17 ARG F 58 GLY F 65 5 8
HELIX 18 18 GLU F 150 SER F 154 5 5
HELIX 19 19 SER G 121 LYS G 126 1 6
HELIX 20 20 LYS G 183 LYS G 188 1 6
HELIX 21 21 THR H 28 TYR H 32 5 5
HELIX 22 22 GLN H 61 GLN H 64 5 4
HELIX 23 23 ARG H 83 THR H 87 5 5
HELIX 24 24 HIS H 200 ASN H 204 5 5
SHEET 1 A 4 VAL A 200 THR A 202 0
SHEET 2 A 4 VAL A 120 LEU A 122 -1 N LYS A 121 O ILE A 201
SHEET 3 A 4 LYS A 432 MET A 434 -1 O LYS A 432 N LEU A 122
SHEET 4 A 4 ILE A 423 ASN A 425 -1 N ILE A 424 O ALA A 433
SHEET 1 B 2 ILE A 215 TYR A 217 0
SHEET 2 B 2 ILE E 307 ILE E 309 1 O ILE E 309 N HIS A 216
SHEET 1 C 3 VAL A 242 VAL A 245 0
SHEET 2 C 3 PHE A 223 CYS A 228 -1 N LYS A 227 O SER A 243
SHEET 3 C 3 TYR A 486 LYS A 490 -1 O VAL A 489 N ALA A 224
SHEET 1 D 5 LEU A 259 LEU A 261 0
SHEET 2 D 5 ILE A 443 ARG A 456 -1 O GLY A 451 N LEU A 260
SHEET 3 D 5 ILE A 284 ARG A 298 -1 N VAL A 292 O ILE A 449
SHEET 4 D 5 GLU A 466 PRO A 470 0
SHEET 5 D 5 ILE A 359 PHE A 361 1 N ILE A 360 O PHE A 468
SHEET 1 E 5 VAL A 271 SER A 274 0
SHEET 2 E 5 ILE A 284 ARG A 298 -1 O ILE A 285 N ARG A 273
SHEET 3 E 5 ILE A 443 ARG A 456 -1 O ILE A 449 N VAL A 292
SHEET 4 E 5 GLN A 328 SER A 334 0
SHEET 5 E 5 ASN A 413 ARG A 419 -1 O ILE A 414 N LEU A 333
SHEET 1 F 2 THR A 303 ARG A 304 0
SHEET 2 F 2 GLU A 322 ILE A 322A-1 O GLU A 322 N ARG A 304
SHEET 1 G 2 ILE A 307 ILE A 309 0
SHEET 2 G 2 ILE E 215 TYR E 217 1 O HIS E 216 N ILE A 309
SHEET 1 H 2 HIS A 374 CYS A 378 0
SHEET 2 H 2 GLU A 381 CYS A 385 -1 O PHE A 383 N PHE A 376
SHEET 1 I 3 LYS B 2 LYS B 7 0
SHEET 2 I 3 GLU B 92 ALA B 102 1 O LEU B 96 N GLY B 6
SHEET 3 I 3 THR B 81 ILE B 83 -1 N TYR B 82 O VAL B 93
SHEET 1 J 4 LYS B 2 LYS B 7 0
SHEET 2 J 4 GLU B 92 ALA B 102 1 O LEU B 96 N GLY B 6
SHEET 3 J 4 LEU B 114 GLU B 119 -1 O GLU B 119 N GLY B 99
SHEET 4 J 4 THR B 143 VAL B 146 -1 O LEU B 144 N LEU B 116
SHEET 1 K 2 VAL B 12 LEU B 14 0
SHEET 2 K 2 LEU B 69 ILE B 71 -1 O ILE B 71 N VAL B 12
SHEET 1 L 2 HIS B 27 LYS B 29 0
SHEET 2 L 2 LYS B 35 GLY B 38 -1 O ILE B 36 N TRP B 28
SHEET 1 M 3 HIS B 107 LEU B 108 0
SHEET 2 M 3 ILE B 172 VAL B 176 1 N VAL B 175 O LEU B 108
SHEET 3 M 3 GLY B 155 TRP B 157 -1 N GLY B 155 O ILE B 174
SHEET 1 N 2 GLN B 129 CYS B 130 0
SHEET 2 N 2 ILE B 138 GLN B 139 -1 O ILE B 138 N CYS B 130
SHEET 1 O 2 THR B 160 LEU B 162 0
SHEET 2 O 2 LYS B 167 GLU B 169 -1 O VAL B 168 N VAL B 161
SHEET 1 P 4 THR C 5 SER C 7 0
SHEET 2 P 4 VAL C 19 ARG C 24 -1 O ARG C 24 N THR C 5
SHEET 3 P 4 GLU C 70 ILE C 75 -1 O LEU C 73 N ILE C 21
SHEET 4 P 4 PHE C 62 SER C 67 -1 N SER C 63 O THR C 74
SHEET 1 Q 6 THR C 10 ALA C 13 0
SHEET 2 Q 6 THR C 102 ILE C 106 1 N GLU C 105 O LEU C 11
SHEET 3 Q 6 THR C 85 GLN C 89 -1 N TYR C 86 O THR C 102
SHEET 4 Q 6 ALA C 34 GLN C 38 -1 N TYR C 36 O TYR C 87
SHEET 5 Q 6 LYS C 45 TYR C 49 -1 O LYS C 45 N GLN C 37
SHEET 6 Q 6 SER C 53 LEU C 54 -1 O SER C 53 N TYR C 49
SHEET 1 R 3 VAL C 115 PHE C 118 0
SHEET 2 R 3 VAL C 133 PHE C 139 -1 O VAL C 133 N PHE C 118
SHEET 3 R 3 TYR C 173 LEU C 175 -1 O LEU C 175 N LEU C 136
SHEET 1 S 2 THR C 129 ALA C 130 0
SHEET 2 S 2 LEU C 181 SER C 182 -1 O LEU C 181 N ALA C 130
SHEET 1 T 2 LEU D 4 GLN D 6 0
SHEET 2 T 2 CYS D 22 ALA D 24 -1 O LYS D 23 N VAL D 5
SHEET 1 U 6 GLU D 10 LYS D 12 0
SHEET 2 U 6 LEU D 108 VAL D 111 1 O THR D 110 N LYS D 12
SHEET 3 U 6 ALA D 88 ALA D 93 -1 N ALA D 88 O VAL D 109
SHEET 4 U 6 ASN D 35 GLN D 39 -1 N VAL D 37 O TYR D 91
SHEET 5 U 6 LEU D 45 ILE D 51 -1 O GLU D 46 N ARG D 38
SHEET 6 U 6 ALA D 57 TYR D 59 -1 O HIS D 58 N GLY D 50
SHEET 1 V 3 VAL D 18 VAL D 20 0
SHEET 2 V 3 THR D 77 LEU D 82 -1 O LEU D 82 N VAL D 18
SHEET 3 V 3 VAL D 67 ASP D 72 -1 N ASP D 72 O THR D 77
SHEET 1 W 3 LEU D 138 CYS D 140 0
SHEET 2 W 3 SER D 180 VAL D 182 -1 O VAL D 182 N LEU D 138
SHEET 3 W 3 HIS D 164 THR D 165 -1 N HIS D 164 O VAL D 181
SHEET 1 X 2 VAL D 152 TRP D 154 0
SHEET 2 X 2 CYS D 196 VAL D 198 -1 O ASN D 197 N SER D 153
SHEET 1 Y 2 VAL D 169 LEU D 170 0
SHEET 2 Y 2 TYR D 176 SER D 177 -1 O SER D 177 N VAL D 169
SHEET 1 Z 4 VAL E 200 THR E 202 0
SHEET 2 Z 4 VAL E 120 LEU E 122 -1 N LYS E 121 O ILE E 201
SHEET 3 Z 4 LYS E 432 MET E 434 -1 O LYS E 432 N LEU E 122
SHEET 4 Z 4 ILE E 423 ASN E 425 -1 N ILE E 424 O ALA E 433
SHEET 1 AA 3 VAL E 242 VAL E 245 0
SHEET 2 AA 3 PHE E 223 CYS E 228 -1 N LYS E 227 O SER E 243
SHEET 3 AA 3 TYR E 486 LYS E 490 -1 O VAL E 489 N ALA E 224
SHEET 1 AB 5 LEU E 259 LEU E 261 0
SHEET 2 AB 5 ILE E 443 ARG E 456 -1 O GLY E 451 N LEU E 260
SHEET 3 AB 5 ILE E 284 ARG E 298 -1 N VAL E 292 O ILE E 449
SHEET 4 AB 5 GLU E 466 PRO E 470 0
SHEET 5 AB 5 ILE E 359 PHE E 361 1 N ILE E 360 O PHE E 468
SHEET 1 AC 5 VAL E 271 SER E 274 0
SHEET 2 AC 5 ILE E 284 ARG E 298 -1 O ILE E 285 N ARG E 273
SHEET 3 AC 5 ILE E 443 ARG E 456 -1 O ILE E 449 N VAL E 292
SHEET 4 AC 5 GLN E 328 LEU E 333 0
SHEET 5 AC 5 ILE E 414 ARG E 419 -1 O ILE E 414 N LEU E 333
SHEET 1 AD 2 THR E 303 ARG E 304 0
SHEET 2 AD 2 GLU E 322 ILE E 322A-1 O GLU E 322 N ARG E 304
SHEET 1 AE 2 HIS E 374 CYS E 378 0
SHEET 2 AE 2 GLU E 381 CYS E 385 -1 O PHE E 383 N PHE E 376
SHEET 1 AF 3 LYS F 2 LYS F 7 0
SHEET 2 AF 3 GLU F 92 ALA F 102 1 O LEU F 96 N GLY F 6
SHEET 3 AF 3 THR F 81 ILE F 83 -1 N TYR F 82 O VAL F 93
SHEET 1 AG 4 LYS F 2 LYS F 7 0
SHEET 2 AG 4 GLU F 92 ALA F 102 1 O LEU F 96 N GLY F 6
SHEET 3 AG 4 LEU F 114 GLU F 119 -1 O GLU F 119 N GLY F 99
SHEET 4 AG 4 THR F 143 VAL F 146 -1 O LEU F 144 N LEU F 116
SHEET 1 AH 2 VAL F 12 LEU F 14 0
SHEET 2 AH 2 LEU F 69 ILE F 71 -1 O ILE F 71 N VAL F 12
SHEET 1 AI 2 HIS F 27 LYS F 29 0
SHEET 2 AI 2 LYS F 35 GLY F 38 -1 O ILE F 36 N TRP F 28
SHEET 1 AJ 3 HIS F 107 LEU F 108 0
SHEET 2 AJ 3 ILE F 172 VAL F 176 1 N VAL F 175 O LEU F 108
SHEET 3 AJ 3 GLY F 155 TRP F 157 -1 N GLY F 155 O ILE F 174
SHEET 1 AK 2 GLN F 129 CYS F 130 0
SHEET 2 AK 2 ILE F 138 GLN F 139 -1 O ILE F 138 N CYS F 130
SHEET 1 AL 2 THR F 160 LEU F 162 0
SHEET 2 AL 2 LYS F 167 GLU F 169 -1 O VAL F 168 N VAL F 161
SHEET 1 AM 4 THR G 5 SER G 7 0
SHEET 2 AM 4 VAL G 19 ARG G 24 -1 O ARG G 24 N THR G 5
SHEET 3 AM 4 GLU G 70 ILE G 75 -1 O LEU G 73 N ILE G 21
SHEET 4 AM 4 PHE G 62 SER G 67 -1 N SER G 63 O THR G 74
SHEET 1 AN 6 THR G 10 ALA G 13 0
SHEET 2 AN 6 THR G 102 ILE G 106 1 N GLU G 105 O LEU G 11
SHEET 3 AN 6 THR G 85 GLN G 89 -1 N TYR G 86 O THR G 102
SHEET 4 AN 6 ALA G 34 GLN G 38 -1 N TYR G 36 O TYR G 87
SHEET 5 AN 6 LYS G 45 TYR G 49 -1 O LYS G 45 N GLN G 37
SHEET 6 AN 6 SER G 53 LEU G 54 -1 O SER G 53 N TYR G 49
SHEET 1 AO 3 VAL G 115 PHE G 118 0
SHEET 2 AO 3 VAL G 133 PHE G 139 -1 O VAL G 133 N PHE G 118
SHEET 3 AO 3 TYR G 173 LEU G 175 -1 O LEU G 175 N LEU G 136
SHEET 1 AP 2 THR G 129 ALA G 130 0
SHEET 2 AP 2 LEU G 181 SER G 182 -1 O LEU G 181 N ALA G 130
SHEET 1 AQ 2 LEU H 4 GLN H 6 0
SHEET 2 AQ 2 CYS H 22 ALA H 24 -1 O LYS H 23 N VAL H 5
SHEET 1 AR 6 GLU H 10 LYS H 12 0
SHEET 2 AR 6 LEU H 108 VAL H 111 1 O THR H 110 N LYS H 12
SHEET 3 AR 6 ALA H 88 ALA H 93 -1 N ALA H 88 O VAL H 109
SHEET 4 AR 6 ASN H 35 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 AR 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 AR 6 ALA H 57 TYR H 59 -1 O HIS H 58 N GLY H 50
SHEET 1 AS 3 VAL H 18 VAL H 20 0
SHEET 2 AS 3 THR H 77 LEU H 82 -1 O LEU H 82 N VAL H 18
SHEET 3 AS 3 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77
SHEET 1 AT 3 LEU H 138 CYS H 140 0
SHEET 2 AT 3 SER H 180 VAL H 182 -1 O VAL H 182 N LEU H 138
SHEET 3 AT 3 HIS H 164 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 AU 2 VAL H 152 TRP H 154 0
SHEET 2 AU 2 CYS H 196 VAL H 198 -1 O ASN H 197 N SER H 153
SHEET 1 AV 2 VAL H 169 LEU H 170 0
SHEET 2 AV 2 TYR H 176 SER H 177 -1 O SER H 177 N VAL H 169
SSBOND 1 CYS A 119 CYS A 205 1555 1555 2.03
SSBOND 2 CYS A 218 CYS A 247 1555 1555 2.04
SSBOND 3 CYS A 228 CYS A 239 1555 1555 2.04
SSBOND 4 CYS A 296 CYS A 331 1555 1555 2.03
SSBOND 5 CYS A 378 CYS A 445 1555 1555 2.03
SSBOND 6 CYS A 385 CYS A 418 1555 1555 2.03
SSBOND 7 CYS B 16 CYS B 84 1555 1555 2.04
SSBOND 8 CYS B 130 CYS B 159 1555 1555 2.04
SSBOND 9 CYS C 23 CYS C 88 1555 1555 2.04
SSBOND 10 CYS C 134 CYS C 194 1555 1555 2.03
SSBOND 11 CYS D 22 CYS D 92 1555 1555 2.04
SSBOND 12 CYS D 140 CYS D 196 1555 1555 2.03
SSBOND 13 CYS E 119 CYS E 205 1555 1555 2.03
SSBOND 14 CYS E 218 CYS E 247 1555 1555 2.04
SSBOND 15 CYS E 228 CYS E 239 1555 1555 2.04
SSBOND 16 CYS E 296 CYS E 331 1555 1555 2.03
SSBOND 17 CYS E 378 CYS E 445 1555 1555 2.04
SSBOND 18 CYS E 385 CYS E 418 1555 1555 2.03
SSBOND 19 CYS F 16 CYS F 84 1555 1555 2.04
SSBOND 20 CYS F 130 CYS F 159 1555 1555 2.04
SSBOND 21 CYS G 23 CYS G 88 1555 1555 2.04
SSBOND 22 CYS G 134 CYS G 194 1555 1555 2.04
SSBOND 23 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 24 CYS H 140 CYS H 196 1555 1555 2.03
LINK ND2 ASN A 234 C1 NAG A 734 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG A 741 1555 1555 1.45
LINK ND2 ASN A 262 C1 NAG A 762 1555 1555 1.44
LINK ND2 ASN A 276 C1 NAG A 776 1555 1555 1.44
LINK ND2 ASN A 289 C1 NAG A 789 1555 1555 1.44
LINK ND2 ASN A 295 C1 NAG A 795 1555 1555 1.44
LINK ND2 ASN A 301 C1 NAG A 801 1555 1555 1.43
LINK ND2 ASN A 332 C1 NAG A 832 1555 1555 1.44
LINK ND2 ASN A 356 C1 NAG A 856 1555 1555 1.44
LINK ND2 ASN A 362 C1 NAG A 862 1555 1555 1.46
LINK ND2 ASN A 386 C1 NAG A 886 1555 1555 1.44
LINK ND2 ASN A 394 C1 NAG A 894 1555 1555 1.44
LINK ND2 ASN A 400 C1 NAG A 900 1555 1555 1.44
LINK ND2 ASN A 413 C1 NAG A 913 1555 1555 1.45
LINK ND2 ASN A 448 C1 NAG A 948 1555 1555 1.44
LINK ND2 ASN A 463 C1 NAG A 963 1555 1555 1.44
LINK C ASP D 99 N TYS D 100 1555 1555 1.33
LINK C ASP D 100B N TYS D 100C 1555 1555 1.33
LINK N ALA D 100D C TYS D 100C 1555 1555 1.33
LINK N ASN D 100A C TYS D 100 1555 1555 1.33
LINK ND2 ASN E 234 C1 NAG E 734 1555 1555 1.44
LINK ND2 ASN E 241 C1 NAG E 741 1555 1555 1.44
LINK ND2 ASN E 262 C1 NAG E 762 1555 1555 1.44
LINK ND2 ASN E 276 C1 NAG E 776 1555 1555 1.45
LINK ND2 ASN E 289 C1 NAG E 789 1555 1555 1.44
LINK ND2 ASN E 295 C1 NAG E 795 1555 1555 1.44
LINK ND2 ASN E 301 C1 NAG E 801 1555 1555 1.44
LINK ND2 ASN E 332 C1 NAG E 832 1555 1555 1.43
LINK ND2 ASN E 356 C1 NAG E 856 1555 1555 1.44
LINK ND2 ASN E 362 C1 NAG E 862 1555 1555 1.45
LINK ND2 ASN E 386 C1 NAG E 886 1555 1555 1.43
LINK ND2 ASN E 394 C1 NAG E 894 1555 1555 1.45
LINK ND2 ASN E 413 C1 NAG E 913 1555 1555 1.45
LINK ND2 ASN E 448 C1 NAG E 948 1555 1555 1.44
LINK ND2 ASN E 463 C1 NAG E 963 1555 1555 1.44
LINK C ASP H 99 N TYS H 100 1555 1555 1.33
LINK N ALA H 100D C TYS H 100C 1555 1555 1.33
LINK C ASP H 100B N TYS H 100C 1555 1555 1.33
LINK N ASN H 100A C TYS H 100 1555 1555 1.33
CISPEP 1 SER C 7 PRO C 8 0 -4.11
CISPEP 2 SER C 94 PRO C 95 0 -2.38
CISPEP 3 TYR C 140 PRO C 141 0 1.74
CISPEP 4 PHE D 146 PRO D 147 0 -3.80
CISPEP 5 GLU D 148 PRO D 149 0 -1.76
CISPEP 6 SER G 7 PRO G 8 0 -4.44
CISPEP 7 SER G 94 PRO G 95 0 -2.40
CISPEP 8 TYR G 140 PRO G 141 0 0.79
CISPEP 9 PHE H 146 PRO H 147 0 -3.53
CISPEP 10 GLU H 148 PRO H 149 0 -3.26
CRYST1 109.600 53.021 225.326 90.00 104.64 90.00 P 1 21 1 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 0.009124 0.000000 0.002383 0.00000
SCALE2 0.000000 0.018860 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004587 0.00000
(ATOM LINES ARE NOT SHOWN.)
END