HEADER IMMUNE SYSTEM 08-FEB-10 3LQA
TITLE CRYSTAL STRUCTURE OF CLADE C GP120 IN COMPLEX WITH SCD4 AND 21C FAB
CAVEAT 3LQA NAG G 2500 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4;
COMPND 3 CHAIN: C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ENVELOPE GLYCOPROTEIN GP160;
COMPND 7 CHAIN: G;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: HEAVY CHAIN OF ANTI HIV FAB FROM HUMAN 21C ANTIBODY;
COMPND 12 CHAIN: H;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: LIGHT CHAIN OF ANTI HIV FAB FROM HUMAN 21C ANTIBODY;
COMPND 16 CHAIN: L;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: CD4;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PACGP67B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HIV-1;
SOURCE 11 ORGANISM_TAXID: 11676;
SOURCE 12 GENE: ENV;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PACGP67B;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 21 MOL_ID: 4;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_TAXID: 9606;
SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS COMPLEX, POLY REACTIVITY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.DISKIN,P.M.MARCOVECCHIO,P.J.BJORKMAN
REVDAT 6 13-OCT-21 3LQA 1 SEQADV HETSYN
REVDAT 5 29-JUL-20 3LQA 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HETNAM LINK SITE
REVDAT 4 01-NOV-17 3LQA 1 REMARK
REVDAT 3 23-AUG-17 3LQA 1 SOURCE
REVDAT 2 26-MAY-10 3LQA 1 JRNL
REVDAT 1 07-APR-10 3LQA 0
JRNL AUTH R.DISKIN,P.M.MARCOVECCHIO,P.J.BJORKMAN
JRNL TITL STRUCTURE OF A CLADE C HIV-1 GP120 BOUND TO CD4 AND
JRNL TITL 2 CD4-INDUCED ANTIBODY REVEALS ANTI-CD4 POLYREACTIVITY.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 608 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20357769
JRNL DOI 10.1038/NSMB.1796
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 84.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 79.6
REMARK 3 NUMBER OF REFLECTIONS : 14967
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM 5%, REDUCED TO 0.5%
REMARK 3 FOR FINAL ROUNDS OF
REMARK 3 REFINEMENT. R VALUES WERE
REMARK 3 RECORDED BEFORE THE FINAL
REMARK 3 REFINEMENT ROUNDS.
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 40.000
REMARK 3 FREE R VALUE TEST SET COUNT : 83
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 6889
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 101.9
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42000
REMARK 3 B22 (A**2) : -1.10700
REMARK 3 B33 (A**2) : 1.52700
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) : NULL
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) : 0.024
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 75.54
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR:PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CNS_TOPPAR:DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : CNS_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CNS_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CNS_TOPPAR:CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057595.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : FLAT MIRROR, DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR, VERTICAL AND
REMARK 200 HORIZONTAL FOCUSSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14975
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 84.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 79.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.70500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE DIFFRACTION PATTERN FROM THE CRYSTALS WAS VERY
REMARK 200 ANISOTROPIC. THERE IS 80% COMPLETENESS TO 3.4A BECAUSE
REMARK 200 THE CRYSTALS DIFFRACTED TO ONLY 3.9A IN THE 'B' DIRECTION.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG MONOMETHYL ETHER 2000,
REMARK 280 5% (V/V) PEG 200, 0.2 M TRIMETHYLAMINE N-OXIDE, 0.1 M TRIS-HCL
REMARK 280 PH 8.5 , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 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 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.83500
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 75.83500
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 SMTRY1 5 1.000000 0.000000 0.000000 46.86500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 93.96500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.86500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 93.96500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.83500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.86500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 93.96500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.83500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.86500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 93.96500
REMARK 290 SMTRY3 8 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: C, G, H, L
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 LYS C 1
REMARK 465 LEU C 177
REMARK 465 ALA C 178
REMARK 465 PHE C 179
REMARK 465 GLN C 180
REMARK 465 LYS C 181
REMARK 465 ALA C 182
REMARK 465 ILE C 183
REMARK 465 ASP C 184
REMARK 465 GLY C 185
REMARK 465 ARG C 186
REMARK 465 HIS C 187
REMARK 465 HIS C 188
REMARK 465 HIS C 189
REMARK 465 HIS C 190
REMARK 465 HIS C 191
REMARK 465 HIS C 192
REMARK 465 GLU G 82
REMARK 465 ILE G 83
REMARK 465 VAL G 84
REMARK 465 LEU G 185
REMARK 465 CYS G 186
REMARK 465 VAL G 187
REMARK 465 GLY G 188
REMARK 465 ALA G 189
REMARK 465 GLY G 190
REMARK 465 ASN G 191
REMARK 465 CYS G 192
REMARK 465 ALA G 323
REMARK 465 THR G 392
REMARK 465 ASP G 393
REMARK 465 SER G 394
REMARK 465 THR G 395
REMARK 465 VAL G 396
REMARK 465 ASN G 397
REMARK 465 SER G 398
REMARK 465 THR G 399
REMARK 465 ASP G 400
REMARK 465 SER G 401
REMARK 465 THR G 402
REMARK 465 ALA G 403
REMARK 465 GLU G 404
REMARK 465 THR G 405
REMARK 465 GLY G 406
REMARK 465 ASN G 407
REMARK 465 SER G 408
REMARK 465 THR G 409
REMARK 465 ASN G 410
REMARK 465 THR G 411
REMARK 465 ASN G 412
REMARK 465 LYS G 494
REMARK 465 SER G 495
REMARK 465 GLY G 496
REMARK 465 HIS G 497
REMARK 465 HIS G 498
REMARK 465 HIS G 499
REMARK 465 HIS G 500
REMARK 465 HIS G 501
REMARK 465 HIS G 502
REMARK 465 LYS H 226
REMARK 465 SER H 227
REMARK 465 CYS H 228
REMARK 465 ASP H 229
REMARK 465 LYS H 230
REMARK 465 THR H 231
REMARK 465 GLN L 2
REMARK 465 GLU L 216
REMARK 465 CYS L 217
REMARK 465 SER L 218
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 C GLU H 160 CD PRO H 161 1.78
REMARK 500 O LEU C 51 O ASP C 53 2.05
REMARK 500 O ASN H 104 OG1 THR H 107 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN G 258 CA ASN G 258 CB 0.174
REMARK 500 ASN G 258 CB ASN G 258 CG 0.281
REMARK 500 ASN G 272 CB ASN G 272 CG 0.184
REMARK 500 ASN G 441 CB ASN G 441 CG 0.160
REMARK 500 VAL H 4 CB VAL H 4 CG2 -0.128
REMARK 500 TRP H 115 CB TRP H 115 CG -0.114
REMARK 500 TRP L 37 CB TRP L 37 CG -0.130
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 LYS C 35 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG C 59 CA - CB - CG ANGL. DEV. = -13.4 DEGREES
REMARK 500 GLN C 110 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 VAL C 146 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 ILE C 174 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 SER G 114 N - CA - C ANGL. DEV. = 18.7 DEGREES
REMARK 500 CYS G 201 CA - CB - SG ANGL. DEV. = 11.1 DEGREES
REMARK 500 PRO G 208 C - N - CA ANGL. DEV. = 17.4 DEGREES
REMARK 500 PRO G 208 C - N - CD ANGL. DEV. = -22.4 DEGREES
REMARK 500 TYR G 213 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 VAL G 251 N - CA - C ANGL. DEV. = -21.7 DEGREES
REMARK 500 GLU G 263 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500 ASN G 275 CA - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 ASN G 276 N - CA - CB ANGL. DEV. = -18.3 DEGREES
REMARK 500 VAL G 277 N - CA - C ANGL. DEV. = 17.5 DEGREES
REMARK 500 LYS G 278 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 LEU G 284 N - CA - C ANGL. DEV. = 16.3 DEGREES
REMARK 500 CYS G 292 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 LYS G 343 N - CA - C ANGL. DEV. = 17.5 DEGREES
REMARK 500 ASN G 380 N - CA - C ANGL. DEV. = -21.6 DEGREES
REMARK 500 HIS G 389 N - CA - C ANGL. DEV. = 23.4 DEGREES
REMARK 500 ASN G 390 N - CA - C ANGL. DEV. = 20.6 DEGREES
REMARK 500 CYS G 417 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 PRO G 437 C - N - CA ANGL. DEV. = 12.7 DEGREES
REMARK 500 PRO G 437 C - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500 PRO G 437 N - CA - C ANGL. DEV. = 16.1 DEGREES
REMARK 500 ASN G 441 CB - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 THR G 467 N - CA - C ANGL. DEV. = 22.9 DEGREES
REMARK 500 PRO G 472 C - N - CA ANGL. DEV. = -9.5 DEGREES
REMARK 500 ASP G 476 N - CA - C ANGL. DEV. = -18.3 DEGREES
REMARK 500 LEU H 29 CA - CB - CG ANGL. DEV. = 18.8 DEGREES
REMARK 500 LEU H 29 CB - CG - CD1 ANGL. DEV. = -11.7 DEGREES
REMARK 500 PRO H 41 C - N - CA ANGL. DEV. = -11.3 DEGREES
REMARK 500 ILE H 58 N - CA - C ANGL. DEV. = -40.5 DEGREES
REMARK 500 GLN H 65 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 GLN H 65 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG H 67 N - CA - C ANGL. DEV. = 19.6 DEGREES
REMARK 500 SER H 75 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 LEU H 105 CB - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 LEU H 105 CA - CB - CG ANGL. DEV. = 21.3 DEGREES
REMARK 500 LEU H 105 CB - CG - CD1 ANGL. DEV. = 13.1 DEGREES
REMARK 500 LEU H 105 CB - CG - CD2 ANGL. DEV. = -12.8 DEGREES
REMARK 500 TYR H 109 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 PRO H 159 C - N - CA ANGL. DEV. = 11.9 DEGREES
REMARK 500 PRO H 159 C - N - CD ANGL. DEV. = -39.8 DEGREES
REMARK 500 PRO H 159 CA - N - CD ANGL. DEV. = -9.3 DEGREES
REMARK 500 PRO H 161 C - N - CA ANGL. DEV. = 36.5 DEGREES
REMARK 500 PRO H 161 C - N - CD ANGL. DEV. = -50.8 DEGREES
REMARK 500 PRO H 214 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO L 8 C - N - CA ANGL. DEV. = -14.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 62 ANGLE DEVIATIONS.
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 PRO C 48 27.86 -67.11
REMARK 500 ASN C 52 -54.99 -14.58
REMARK 500 GLU C 87 50.02 39.96
REMARK 500 PRO C 122 129.59 -38.81
REMARK 500 PRO G 208 69.51 1.81
REMARK 500 PRO G 216 -139.62 -55.83
REMARK 500 GLN G 254 -14.10 39.98
REMARK 500 ASN G 386 18.64 -140.06
REMARK 500 ASN G 460 -128.18 120.02
REMARK 500 THR G 462 31.27 29.91
REMARK 500 PRO G 472 -173.76 -61.17
REMARK 500 PRO H 53 -0.56 -57.34
REMARK 500 THR H 107 -38.01 54.01
REMARK 500 PRO H 159 107.39 44.84
REMARK 500 PRO H 161 106.75 169.32
REMARK 500 ASN L 29 -79.81 -92.70
REMARK 500 PRO L 42 97.86 -39.35
REMARK 500 ASP L 53 -60.74 69.89
REMARK 500 ALA L 86 -169.85 170.02
REMARK 500 LEU L 97 -160.01 50.01
REMARK 500 THR L 99 -19.99 -40.00
REMARK 500 PRO L 170 147.95 -33.86
REMARK 500 PRO L 188 -7.37 -59.21
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 SER L 98 THR L 99 -148.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR H 94 0.07 SIDE CHAIN
REMARK 500 TYR H 102 0.12 SIDE CHAIN
REMARK 500 TYR H 110 0.08 SIDE CHAIN
REMARK 500 TYR H 114 0.09 SIDE CHAIN
REMARK 500 TYR L 34 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER L 98 -10.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LMJ RELATED DB: PDB
REMARK 900 21C FAB UNBOUND
DBREF 3LQA C 1 182 UNP P01730 CD4_HUMAN 26 207
DBREF 3LQA G 82 293 UNP Q1PHM6 Q1PHM6_9HIV1 82 232
DBREF 3LQA G 325 494 UNP Q1PHM6 Q1PHM6_9HIV1 325 494
DBREF 3LQA H 1 231 PDB 3LQA 3LQA 1 231
DBREF 3LQA L 2 218 PDB 3LQA 3LQA 2 218
SEQADV 3LQA ILE C 183 UNP P01730 EXPRESSION TAG
SEQADV 3LQA ASP C 184 UNP P01730 EXPRESSION TAG
SEQADV 3LQA GLY C 185 UNP P01730 EXPRESSION TAG
SEQADV 3LQA ARG C 186 UNP P01730 EXPRESSION TAG
SEQADV 3LQA HIS C 187 UNP P01730 EXPRESSION TAG
SEQADV 3LQA HIS C 188 UNP P01730 EXPRESSION TAG
SEQADV 3LQA HIS C 189 UNP P01730 EXPRESSION TAG
SEQADV 3LQA HIS C 190 UNP P01730 EXPRESSION TAG
SEQADV 3LQA HIS C 191 UNP P01730 EXPRESSION TAG
SEQADV 3LQA HIS C 192 UNP P01730 EXPRESSION TAG
SEQADV 3LQA GLY G 294 UNP Q1PHM6 LINKER
SEQADV 3LQA ALA G 323 UNP Q1PHM6 LINKER
SEQADV 3LQA GLY G 324 UNP Q1PHM6 LINKER
SEQADV 3LQA ILE G 89 UNP Q1PHM6 THR 89 ENGINEERED MUTATION
SEQADV 3LQA ASP G 226 UNP Q1PHM6 ASN 226 ENGINEERED MUTATION
SEQADV 3LQA ILE G 232 UNP Q1PHM6 THR 232 ENGINEERED MUTATION
SEQADV 3LQA THR G 285 UNP Q1PHM6 ASN 285 ENGINEERED MUTATION
SEQADV 3LQA ASN G 329 UNP Q1PHM6 SER 329 ENGINEERED MUTATION
SEQADV 3LQA ILE G 388 UNP Q1PHM6 THR 388 ENGINEERED MUTATION
SEQADV 3LQA ASP G 447 UNP Q1PHM6 ASN 447 ENGINEERED MUTATION
SEQADV 3LQA SER G 495 UNP Q1PHM6 EXPRESSION TAG
SEQADV 3LQA GLY G 496 UNP Q1PHM6 EXPRESSION TAG
SEQADV 3LQA HIS G 497 UNP Q1PHM6 EXPRESSION TAG
SEQADV 3LQA HIS G 498 UNP Q1PHM6 EXPRESSION TAG
SEQADV 3LQA HIS G 499 UNP Q1PHM6 EXPRESSION TAG
SEQADV 3LQA HIS G 500 UNP Q1PHM6 EXPRESSION TAG
SEQADV 3LQA HIS G 501 UNP Q1PHM6 EXPRESSION TAG
SEQADV 3LQA HIS G 502 UNP Q1PHM6 EXPRESSION TAG
SEQRES 1 C 192 LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU
SEQRES 2 C 192 LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE
SEQRES 3 C 192 HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN
SEQRES 4 C 192 GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN
SEQRES 5 C 192 ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY
SEQRES 6 C 192 ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP
SEQRES 7 C 192 SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU
SEQRES 8 C 192 GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SER
SEQRES 9 C 192 ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU THR
SEQRES 10 C 192 LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN CYS
SEQRES 11 C 192 ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS THR
SEQRES 12 C 192 LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY THR
SEQRES 13 C 192 TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL GLU
SEQRES 14 C 192 PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS ALA
SEQRES 15 C 192 ILE ASP GLY ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 G 332 GLU ILE VAL LEU GLU ASN VAL ILE GLU ASN PHE ASN MET
SEQRES 2 G 332 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLN ASP ILE
SEQRES 3 G 332 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS
SEQRES 4 G 332 LEU THR PRO LEU CYS VAL GLY ALA GLY ASN CYS ASN THR
SEQRES 5 G 332 SER THR ILE ALA GLN ALA CYS PRO LYS VAL SER PHE ASP
SEQRES 6 G 332 PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY TYR ALA
SEQRES 7 G 332 ILE LEU LYS CYS ASN ASP LYS THR PHE ASN GLY ILE GLY
SEQRES 8 G 332 PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR HIS GLY
SEQRES 9 G 332 ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY
SEQRES 10 G 332 SER LEU ALA GLU GLU GLU VAL VAL ILE ARG SER GLU ASN
SEQRES 11 G 332 ILE SER ASN ASN VAL LYS THR ILE ILE VAL HIS LEU THR
SEQRES 12 G 332 GLU SER VAL ASN ILE THR CYS ILE GLY ALA GLY HIS CYS
SEQRES 13 G 332 ASN ILE ASN GLU LYS ALA TRP ASN GLU THR LEU LYS LYS
SEQRES 14 G 332 VAL VAL GLU LYS LEU VAL LYS TYR PHE PRO ASN LYS THR
SEQRES 15 G 332 ILE GLU PHE ALA PRO PRO VAL GLY GLY ASP LEU GLU ILE
SEQRES 16 G 332 THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR
SEQRES 17 G 332 CYS ASN THR THR LYS LEU PHE ASN SER ILE HIS ASN SER
SEQRES 18 G 332 THR ASP SER THR VAL ASN SER THR ASP SER THR ALA GLU
SEQRES 19 G 332 THR GLY ASN SER THR ASN THR ASN ILE THR LEU PRO CYS
SEQRES 20 G 332 ARG ILE ARG GLN ILE ILE ASN MET TRP GLN GLU VAL GLY
SEQRES 21 G 332 ARG ALA MET TYR ALA PRO PRO SER LYS GLY ASN ILE THR
SEQRES 22 G 332 CYS ILE SER ASP ILE THR GLY LEU LEU LEU THR ARG ASP
SEQRES 23 G 332 GLY GLY GLU ASN LYS THR GLU ASN ASN ASP THR GLU ILE
SEQRES 24 G 332 PHE ARG PRO GLY GLY GLY ASP MET LYS ASP ASN TRP ARG
SEQRES 25 G 332 SER GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE LYS SER
SEQRES 26 G 332 GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 H 231 GLN VAL GLN VAL VAL GLN SER GLY ALA GLU VAL ARG LYS
SEQRES 2 H 231 PRO GLY ALA SER VAL LYS VAL SER CYS LYS VAL SER GLY
SEQRES 3 H 231 PHE THR LEU THR GLY LEU SER ILE HIS TRP VAL ARG GLN
SEQRES 4 H 231 ALA PRO GLY LYS GLY LEU GLU TRP MET GLY GLY PHE GLY
SEQRES 5 H 231 PRO GLU GLU ASN GLU ILE ILE TYR ALA GLN LYS PHE GLN
SEQRES 6 H 231 GLY ARG VAL SER MET THR GLU ASP THR SER THR ASN THR
SEQRES 7 H 231 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 H 231 ALA VAL TYR TYR CYS ALA THR GLY GLY ASN TYR TYR ASN
SEQRES 9 H 231 LEU TRP THR GLY TYR TYR PRO LEU ALA TYR TRP GLY GLN
SEQRES 10 H 231 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY
SEQRES 11 H 231 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR
SEQRES 12 H 231 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP
SEQRES 13 H 231 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY
SEQRES 14 H 231 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU
SEQRES 15 H 231 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR
SEQRES 16 H 231 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS
SEQRES 17 H 231 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS
SEQRES 18 H 231 LYS VAL GLU PRO LYS SER CYS ASP LYS THR
SEQRES 1 L 217 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER ALA ALA
SEQRES 2 L 217 PRO GLY GLN LYS VAL THR ILE SER CYS SER GLY SER SER
SEQRES 3 L 217 SER ASN ILE GLY LYS ASN TYR VAL SER TRP TYR GLN GLN
SEQRES 4 L 217 LEU PRO GLY ALA ALA PRO LYS LEU LEU ILE PHE ASP ASP
SEQRES 5 L 217 THR GLN ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY
SEQRES 6 L 217 SER LYS SER GLY THR SER ALA THR LEU ALA ILE THR GLY
SEQRES 7 L 217 LEU GLN THR GLY ASP GLU ALA ASP TYR TYR CYS GLY THR
SEQRES 8 L 217 TRP ASP SER SER LEU SER THR GLY GLN LEU PHE GLY GLY
SEQRES 9 L 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA
SEQRES 10 L 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU
SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP
SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP
SEQRES 13 L 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO
SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR
SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER
SEQRES 16 L 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU
SEQRES 17 L 217 LYS THR MET ALA HIS ALA GLU CYS SER
MODRES 3LQA ASN G 272 ASN GLYCOSYLATION SITE
MODRES 3LQA ASN G 380 ASN GLYCOSYLATION SITE
MODRES 3LQA ASN G 441 ASN GLYCOSYLATION SITE
MODRES 3LQA ASN G 258 ASN GLYCOSYLATION SITE
HET NAG G1000 14
HET NAG G1500 14
HET NAG G2000 14
HET NAG G2500 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
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
FORMUL 5 NAG 4(C8 H15 N O6)
HELIX 1 1 ARG C 59 ASP C 63 5 5
HELIX 2 2 ASN G 97 LEU G 115 1 19
HELIX 3 3 ASN G 329 PHE G 348 1 20
HELIX 4 4 ASP G 362 THR G 367 1 6
HELIX 5 5 ASP G 476 TYR G 486 1 11
HELIX 6 6 GLN H 62 GLN H 65 5 4
HELIX 7 7 SER H 168 ALA H 170 5 3
HELIX 8 8 SER H 198 GLN H 204 1 7
HELIX 9 9 SER L 127 ALA L 133 1 7
HELIX 10 10 THR L 187 HIS L 194 1 8
SHEET 1 A 6 VAL C 3 LYS C 7 0
SHEET 2 A 6 GLN C 89 THR C 101 1 O GLN C 94 N VAL C 4
SHEET 3 A 6 ASP C 80 VAL C 86 -1 N ASP C 80 O LEU C 95
SHEET 4 A 6 PHE C 26 LYS C 29 -1 N LYS C 29 O ILE C 83
SHEET 5 A 6 LYS C 35 GLN C 40 -1 O LEU C 37 N TRP C 28
SHEET 6 A 6 PHE C 43 LYS C 46 -1 O PHE C 43 N GLN C 40
SHEET 1 B 4 VAL C 3 LYS C 7 0
SHEET 2 B 4 GLN C 89 THR C 101 1 O GLN C 94 N VAL C 4
SHEET 3 B 4 LEU C 114 GLU C 119 -1 O GLU C 119 N GLY C 99
SHEET 4 B 4 THR C 143 VAL C 146 -1 O LEU C 144 N LEU C 116
SHEET 1 C 3 VAL C 12 LEU C 14 0
SHEET 2 C 3 LEU C 69 ILE C 71 -1 O LEU C 69 N LEU C 14
SHEET 3 C 3 ALA C 55 ASP C 56 -1 N ASP C 56 O ILE C 70
SHEET 1 D 4 ASN C 137 ILE C 138 0
SHEET 2 D 4 VAL C 128 ARG C 131 -1 N CYS C 130 O ILE C 138
SHEET 3 D 4 TRP C 157 GLN C 163 -1 O THR C 160 N GLN C 129
SHEET 4 D 4 LYS C 166 ILE C 172 -1 O PHE C 170 N CYS C 159
SHEET 1 E 2 GLU G 90 ASN G 93 0
SHEET 2 E 2 ILE G 232 CYS G 235 -1 O CYS G 235 N GLU G 90
SHEET 1 F 4 ILE G 197 ALA G 198 0
SHEET 2 F 4 VAL G 119 LYS G 120 -1 N LYS G 120 O ILE G 197
SHEET 3 F 4 ARG G 431 MET G 433 -1 O MET G 433 N VAL G 119
SHEET 4 F 4 ILE G 422 ASN G 424 -1 N ILE G 423 O ALA G 432
SHEET 1 G 3 VAL G 238 VAL G 241 0
SHEET 2 G 3 ALA G 220 CYS G 224 -1 N ILE G 221 O VAL G 241
SHEET 3 G 3 LYS G 489 VAL G 491 -1 O VAL G 491 N ALA G 220
SHEET 1 H 5 LEU G 255 LEU G 257 0
SHEET 2 H 5 THR G 443 LEU G 451 -1 O GLY G 450 N LEU G 256
SHEET 3 H 5 HIS G 283 ILE G 293 -1 N VAL G 288 O ILE G 448
SHEET 4 H 5 HIS G 325 ILE G 328 -1 O ASN G 327 N THR G 291
SHEET 5 H 5 THR G 414 LEU G 415 -1 O LEU G 415 N CYS G 326
SHEET 1 I 4 ILE G 388 HIS G 389 0
SHEET 2 I 4 THR G 352 PHE G 355 -1 N ILE G 353 O HIS G 389
SHEET 3 I 4 THR G 467 PRO G 472 1 O PHE G 470 N GLU G 354
SHEET 4 I 4 LEU G 453 ARG G 455 -1 N THR G 454 O ARG G 471
SHEET 1 J 3 PHE G 370 ASN G 371 0
SHEET 2 J 3 PHE G 376 CYS G 379 -1 O PHE G 377 N PHE G 370
SHEET 3 J 3 CYS G 417 ARG G 420 -1 O ARG G 418 N TYR G 378
SHEET 1 K 2 GLN H 3 GLN H 6 0
SHEET 2 K 2 CYS H 22 SER H 25 -1 O SER H 25 N GLN H 3
SHEET 1 L 6 GLU H 10 ARG H 12 0
SHEET 2 L 6 THR H 119 VAL H 123 1 O THR H 122 N ARG H 12
SHEET 3 L 6 ALA H 92 THR H 98 -1 N TYR H 94 O THR H 119
SHEET 4 L 6 ILE H 34 GLN H 39 -1 N GLN H 39 O VAL H 93
SHEET 5 L 6 LEU H 45 PHE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 L 6 ILE H 58 TYR H 60 -1 O ILE H 59 N GLY H 50
SHEET 1 M 4 GLU H 10 ARG H 12 0
SHEET 2 M 4 THR H 119 VAL H 123 1 O THR H 122 N ARG H 12
SHEET 3 M 4 ALA H 92 THR H 98 -1 N TYR H 94 O THR H 119
SHEET 4 M 4 TYR H 114 TRP H 115 -1 O TYR H 114 N THR H 98
SHEET 1 N 3 VAL H 18 VAL H 20 0
SHEET 2 N 3 THR H 78 LEU H 83 -1 O MET H 81 N VAL H 20
SHEET 3 N 3 VAL H 68 ASP H 73 -1 N SER H 69 O GLU H 82
SHEET 1 O 4 SER H 132 LEU H 136 0
SHEET 2 O 4 THR H 147 TYR H 157 -1 O GLY H 151 N LEU H 136
SHEET 3 O 4 TYR H 188 PRO H 197 -1 O VAL H 196 N ALA H 148
SHEET 4 O 4 VAL H 175 THR H 177 -1 N HIS H 176 O VAL H 193
SHEET 1 P 4 SER H 132 LEU H 136 0
SHEET 2 P 4 THR H 147 TYR H 157 -1 O GLY H 151 N LEU H 136
SHEET 3 P 4 TYR H 188 PRO H 197 -1 O VAL H 196 N ALA H 148
SHEET 4 P 4 VAL H 181 LEU H 182 -1 N VAL H 181 O SER H 189
SHEET 1 Q 3 THR H 163 TRP H 166 0
SHEET 2 Q 3 TYR H 206 HIS H 212 -1 O ASN H 209 N SER H 165
SHEET 3 Q 3 THR H 217 VAL H 223 -1 O VAL H 219 N VAL H 210
SHEET 1 R 5 SER L 10 ALA L 13 0
SHEET 2 R 5 THR L 107 VAL L 111 1 O THR L 110 N VAL L 11
SHEET 3 R 5 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 109
SHEET 4 R 5 VAL L 35 GLN L 40 -1 N SER L 36 O GLY L 91
SHEET 5 R 5 LYS L 47 ILE L 50 -1 O LYS L 47 N GLN L 39
SHEET 1 S 4 SER L 10 ALA L 13 0
SHEET 2 S 4 THR L 107 VAL L 111 1 O THR L 110 N VAL L 11
SHEET 3 S 4 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 109
SHEET 4 S 4 GLY L 100 PHE L 103 -1 O LEU L 102 N THR L 92
SHEET 1 T 3 VAL L 19 SER L 24 0
SHEET 2 T 3 SER L 72 ILE L 77 -1 O ALA L 73 N CYS L 23
SHEET 3 T 3 PHE L 64 SER L 69 -1 N SER L 65 O ALA L 76
SHEET 1 U 4 SER L 120 PHE L 124 0
SHEET 2 U 4 THR L 137 PHE L 145 -1 O VAL L 139 N PHE L 124
SHEET 3 U 4 TYR L 178 SER L 185 -1 O LEU L 184 N LEU L 138
SHEET 4 U 4 VAL L 165 THR L 167 -1 N GLU L 166 O TYR L 183
SHEET 1 V 4 SER L 159 VAL L 161 0
SHEET 2 V 4 THR L 151 ALA L 156 -1 N TRP L 154 O VAL L 161
SHEET 3 V 4 TYR L 197 HIS L 203 -1 O SER L 198 N LYS L 155
SHEET 4 V 4 SER L 206 MET L 212 -1 O MET L 212 N TYR L 197
SSBOND 1 CYS C 16 CYS C 84 1555 1555 2.01
SSBOND 2 CYS C 130 CYS C 159 1555 1555 2.05
SSBOND 3 CYS G 118 CYS G 201 1555 1555 2.04
SSBOND 4 CYS G 214 CYS G 243 1555 1555 2.03
SSBOND 5 CYS G 224 CYS G 235 1555 1555 2.05
SSBOND 6 CYS G 292 CYS G 326 1555 1555 2.02
SSBOND 7 CYS G 372 CYS G 444 1555 1555 2.03
SSBOND 8 CYS G 379 CYS G 417 1555 1555 2.03
SSBOND 9 CYS H 22 CYS H 96 1555 1555 2.06
SSBOND 10 CYS H 152 CYS H 208 1555 1555 2.01
SSBOND 11 CYS L 23 CYS L 90 1555 1555 2.04
SSBOND 12 CYS L 140 CYS L 199 1555 1555 2.02
LINK ND2 ASN G 258 C1 NAG G1000 1555 1555 1.57
LINK ND2 ASN G 272 C1 NAG G1500 1555 1555 1.52
LINK ND2 ASN G 380 C1 NAG G2000 1555 1555 1.53
LINK ND2 ASN G 441 C1 NAG G2500 1555 1555 1.56
CISPEP 1 TYR L 146 PRO L 147 0 -0.17
CRYST1 93.730 187.930 151.670 90.00 90.00 90.00 C 2 2 21 8
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 0.010669 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006593 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
