HEADER VIRAL PROTEIN 13-APR-06 2GOL
TITLE XRAY STRUCTURE OF GAG278
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MATRIX PROTEIN P17 (MA);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-131;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CAPSID PROTEIN P24 (CA);
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 132-277);
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: ISOLATE NEW YORK-5;
SOURCE 5 GENE: GAG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 10 ORGANISM_TAXID: 11676;
SOURCE 11 STRAIN: ISOLATE NEW YORK-5;
SOURCE 12 GENE: GAG;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS VIRAL MATURATION, IMMATURE, GAG, HIV-1, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.N.KELLY
REVDAT 3 14-FEB-24 2GOL 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2GOL 1 VERSN
REVDAT 1 26-SEP-06 2GOL 0
JRNL AUTH B.N.KELLY,B.R.HOWARD,H.WANG,H.ROBINSON,W.I.SUNDQUIST,
JRNL AUTH 2 C.P.HILL
JRNL TITL IMPLICATIONS FOR VIRAL CAPSID ASSEMBLY FROM CRYSTAL
JRNL TITL 2 STRUCTURES OF HIV-1 GAG 1-278 AND CAN 133-278.
JRNL REF BIOCHEMISTRY V. 45 11257 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16981686
JRNL DOI 10.1021/BI060927X
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 32633
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 + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1703
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1834
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2922
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 274
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.79000
REMARK 3 B22 (A**2) : -1.79000
REMARK 3 B33 (A**2) : 3.58000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.187
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.185
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.134
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.262
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3009 ; 0.025 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4084 ; 2.105 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 369 ;14.682 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 133 ;38.091 ;24.586
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 534 ;18.771 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;21.400 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 451 ; 0.179 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2254 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1513 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2097 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 228 ; 0.208 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 100 ; 0.243 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 31 ; 0.240 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1928 ; 1.596 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3011 ; 2.585 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1262 ; 3.555 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1073 ; 5.441 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2GOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037367.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-04; 07-JAN-04
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X25; X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000; 0.97791
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34399
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 8000, 0.2 M (NH4)2SO4, 0.1 M
REMARK 280 SODIUM CACODYLATE, PH 6.7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 56.71350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.51350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.51350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.35675
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.51350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.51350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 85.07025
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.51350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.51350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 28.35675
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.51350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.51350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 85.07025
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.71350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE:
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). THE BIOLOGICAL MOLECULE IS
REMARK 300 ONE MATRIX PROTEIN CONNECTED TO ONE CAPSID PROTEIN.
REMARK 300 SINCE THERE IS NO ELECTRON DENSITY FOR THE LINKER BETWEEN
REMARK 300 THE MA DOMAIN AND EITHER CA DOMAIN THE AUTHORS ARE UNABLE
REMARK 300 TO DETERMINE WHICH CA SHOULD CONNECT TO MA.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 ALA A 3
REMARK 465 ARG A 4
REMARK 465 ALA A 5
REMARK 465 GLN A 108
REMARK 465 ASN A 109
REMARK 465 LYS A 110
REMARK 465 SER A 111
REMARK 465 LYS A 112
REMARK 465 LYS A 113
REMARK 465 LYS A 114
REMARK 465 ALA A 115
REMARK 465 GLN A 116
REMARK 465 GLN A 117
REMARK 465 ALA A 118
REMARK 465 ALA A 119
REMARK 465 ALA A 120
REMARK 465 ASP A 121
REMARK 465 THR A 122
REMARK 465 GLY A 123
REMARK 465 ASN A 124
REMARK 465 ASN A 125
REMARK 465 SER A 126
REMARK 465 GLN A 127
REMARK 465 VAL A 128
REMARK 465 SER A 129
REMARK 465 GLN A 130
REMARK 465 ASN A 131
REMARK 465 TYR A 132
REMARK 465 PRO B 133
REMARK 465 ILE B 134
REMARK 465 VAL B 135
REMARK 465 GLN B 136
REMARK 465 ASN B 137
REMARK 465 LEU B 138
REMARK 465 GLN B 139
REMARK 465 GLY B 140
REMARK 465 GLN B 141
REMARK 465 MET B 142
REMARK 465 VAL B 143
REMARK 465 PRO D 133
REMARK 465 ILE D 134
REMARK 465 VAL D 135
REMARK 465 GLN D 136
REMARK 465 ASN D 137
REMARK 465 LEU D 138
REMARK 465 GLN D 139
REMARK 465 GLY D 140
REMARK 465 GLN D 141
REMARK 465 MET D 142
REMARK 465 VAL D 143
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 O HOH B 356 O HOH B 378 1.77
REMARK 500 OE1 GLU A 73 O HOH A 173 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 187 O HOH B 357 7555 1.96
REMARK 500 O HOH D 363 O HOH D 363 7555 2.15
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 THR B 186 N THR B 186 CA 0.123
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 ASP A 14 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 76 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 THR B 204 N - CA - C ANGL. DEV. = 26.4 DEGREES
REMARK 500 ARG B 232 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP D 213 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 PRO D 225 N - CA - C ANGL. DEV. = -16.1 DEGREES
REMARK 500 GLY D 226 N - CA - C ANGL. DEV. = -15.2 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 THR A 70 -164.80 -70.23
REMARK 500 PHE B 164 34.47 70.98
REMARK 500 THR B 204 -82.91 -15.75
REMARK 500 ILE B 205 -73.68 -3.18
REMARK 500 PRO B 222 142.64 -15.62
REMARK 500 PRO B 225 75.37 -11.07
REMARK 500 GLN B 227 46.01 -68.03
REMARK 500 MET B 228 122.20 83.68
REMARK 500 ARG B 229 154.12 -48.59
REMARK 500 HIS B 252 150.96 -47.90
REMARK 500 ALA D 146 24.03 -66.74
REMARK 500 ILE D 147 101.09 50.99
REMARK 500 ALA D 163 87.72 5.49
REMARK 500 TYR D 277 40.16 -100.90
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 GLU B 203 THR B 204 135.05
REMARK 500 THR B 204 ILE B 205 133.32
REMARK 500 PRO D 225 GLY D 226 -39.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GON RELATED DB: PDB
DBREF 2GOL A 2 132 UNP P12497 POL_HV1N5 1 131
DBREF 2GOL B 133 278 UNP P12497 POL_HV1N5 132 277
DBREF 2GOL D 133 278 UNP P12497 POL_HV1N5 132 277
SEQADV 2GOL HIS A 0 UNP P12497 CLONING ARTIFACT
SEQADV 2GOL MET A 1 UNP P12497 CLONING ARTIFACT
SEQRES 1 A 133 HIS MET GLY ALA ARG ALA SER VAL LEU SER GLY GLY GLU
SEQRES 2 A 133 LEU ASP LYS TRP GLU LYS ILE ARG LEU ARG PRO GLY GLY
SEQRES 3 A 133 LYS LYS GLN TYR LYS LEU LYS HIS ILE VAL TRP ALA SER
SEQRES 4 A 133 ARG GLU LEU GLU ARG PHE ALA VAL ASN PRO GLY LEU LEU
SEQRES 5 A 133 GLU THR SER GLU GLY CYS ARG GLN ILE LEU GLY GLN LEU
SEQRES 6 A 133 GLN PRO SER LEU GLN THR GLY SER GLU GLU LEU ARG SER
SEQRES 7 A 133 LEU TYR ASN THR ILE ALA VAL LEU TYR CYS VAL HIS GLN
SEQRES 8 A 133 ARG ILE ASP VAL LYS ASP THR LYS GLU ALA LEU ASP LYS
SEQRES 9 A 133 ILE GLU GLU GLU GLN ASN LYS SER LYS LYS LYS ALA GLN
SEQRES 10 A 133 GLN ALA ALA ALA ASP THR GLY ASN ASN SER GLN VAL SER
SEQRES 11 A 133 GLN ASN TYR
SEQRES 1 B 146 PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN
SEQRES 2 B 146 ALA ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL
SEQRES 3 B 146 VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET
SEQRES 4 B 146 PHE SER ALA LEU SER GLU GLY ALA THR PRO GLN ASP LEU
SEQRES 5 B 146 ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA
SEQRES 6 B 146 MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA
SEQRES 7 B 146 GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE
SEQRES 8 B 146 ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE
SEQRES 9 B 146 ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP
SEQRES 10 B 146 MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR
SEQRES 11 B 146 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG
SEQRES 12 B 146 MET TYR SER
SEQRES 1 D 146 PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN
SEQRES 2 D 146 ALA ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL
SEQRES 3 D 146 VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET
SEQRES 4 D 146 PHE SER ALA LEU SER GLU GLY ALA THR PRO GLN ASP LEU
SEQRES 5 D 146 ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA
SEQRES 6 D 146 MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA
SEQRES 7 D 146 GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE
SEQRES 8 D 146 ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE
SEQRES 9 D 146 ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP
SEQRES 10 D 146 MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR
SEQRES 11 D 146 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG
SEQRES 12 D 146 MET TYR SER
HET SO4 A 133 5
HET SO4 D 2 5
HETNAM SO4 SULFATE ION
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 HOH *274(H2 O)
HELIX 1 1 SER A 9 ILE A 19 1 11
HELIX 2 2 LYS A 30 PHE A 44 1 15
HELIX 3 3 ASN A 47 GLU A 52 5 6
HELIX 4 4 THR A 53 GLN A 69 1 17
HELIX 5 5 LEU A 75 GLN A 90 1 16
HELIX 6 6 ASP A 96 GLU A 107 1 12
HELIX 7 7 SER B 148 ALA B 163 1 16
HELIX 8 8 GLU B 167 SER B 176 1 10
HELIX 9 9 THR B 180 VAL B 191 1 12
HELIX 10 10 HIS B 194 LEU B 215 1 22
HELIX 11 11 ILE B 223 GLN B 227 5 5
HELIX 12 12 ARG B 232 ALA B 237 1 6
HELIX 13 13 THR B 242 HIS B 252 1 11
HELIX 14 14 PRO B 257 SER B 278 1 22
HELIX 15 15 SER D 148 ALA D 163 1 16
HELIX 16 16 GLU D 167 SER D 176 1 10
HELIX 17 17 THR D 180 THR D 190 1 11
HELIX 18 18 HIS D 194 HIS D 216 1 23
HELIX 19 19 ARG D 232 ALA D 237 1 6
HELIX 20 20 THR D 242 HIS D 252 1 11
HELIX 21 21 PRO D 257 TYR D 277 1 21
CISPEP 1 ASN B 253 PRO B 254 0 2.31
CISPEP 2 ASN D 253 PRO D 254 0 0.70
SITE 1 AC1 5 ARG A 22 GLY A 25 LYS A 26 LYS A 27
SITE 2 AC1 5 HOH A 150
SITE 1 AC2 8 SER B 148 PRO B 149 ARG B 150 GLN D 145
SITE 2 AC2 8 ILE D 147 SER D 148 THR D 151 HOH D 294
CRYST1 111.027 111.027 113.427 90.00 90.00 90.00 P 41 21 2 16
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 0.009007 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009007 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008816 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
