HEADER VIRAL PROTEIN 08-JAN-16 5HGO
TITLE HEXAMERIC HIV-1 CA R18G MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAPSID PROTEIN P24;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PR55GAG;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11676;
SOURCE 5 GENE: GAG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS CAPSID, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.JACQUES,L.C.JAMES
REVDAT 6 10-JAN-24 5HGO 1 SSBOND
REVDAT 5 24-JAN-18 5HGO 1 SOURCE
REVDAT 4 13-SEP-17 5HGO 1 REMARK
REVDAT 3 31-AUG-16 5HGO 1 JRNL
REVDAT 2 24-AUG-16 5HGO 1 JRNL
REVDAT 1 10-AUG-16 5HGO 0
JRNL AUTH D.A.JACQUES,W.A.MCEWAN,L.HILDITCH,A.J.PRICE,G.J.TOWERS,
JRNL AUTH 2 L.C.JAMES
JRNL TITL HIV-1 USES DYNAMIC CAPSID PORES TO IMPORT NUCLEOTIDES AND
JRNL TITL 2 FUEL ENCAPSIDATED DNA SYNTHESIS.
JRNL REF NATURE V. 536 349 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 27509857
JRNL DOI 10.1038/NATURE19098
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0124
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 17285
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 921
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1246
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1573
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 105
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.07000
REMARK 3 B22 (A**2) : 6.07000
REMARK 3 B33 (A**2) : -12.13000
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): 0.036
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.030
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.572
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1644 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1578 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2240 ; 1.046 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3638 ; 0.876 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 212 ; 4.982 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 68 ;37.215 ;24.706
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 282 ;11.276 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;15.230 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 254 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1858 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 352 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 833 ; 1.387 ; 2.752
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 832 ; 1.388 ; 2.749
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1041 ; 2.219 ; 4.615
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.878
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.122
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 145
REMARK 3 ORIGIN FOR THE GROUP (A): 69.4238 -87.1167 -12.2837
REMARK 3 T TENSOR
REMARK 3 T11: 0.0088 T22: 0.0140
REMARK 3 T33: 0.0875 T12: 0.0068
REMARK 3 T13: -0.0021 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.3648 L22: 0.6326
REMARK 3 L33: 1.0406 L12: 0.0575
REMARK 3 L13: -0.0746 L23: -0.3940
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: 0.0416 S13: -0.0152
REMARK 3 S21: -0.0679 S22: -0.0357 S23: 0.0031
REMARK 3 S31: 0.0401 S32: 0.0882 S33: 0.0184
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 146 A 999
REMARK 3 ORIGIN FOR THE GROUP (A): 58.7452-113.8960 11.0924
REMARK 3 T TENSOR
REMARK 3 T11: 0.0366 T22: 0.0074
REMARK 3 T33: 0.0925 T12: -0.0012
REMARK 3 T13: 0.0015 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 2.2781 L22: 2.2559
REMARK 3 L33: 1.9519 L12: 0.7951
REMARK 3 L13: 0.3574 L23: -1.0365
REMARK 3 S TENSOR
REMARK 3 S11: 0.0455 S12: -0.0949 S13: -0.1310
REMARK 3 S21: 0.0925 S22: -0.0366 S23: -0.1219
REMARK 3 S31: 0.1489 S32: -0.0243 S33: -0.0089
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5HGO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.12
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18210
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 46.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.16600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.83100
REMARK 200 R SYM FOR SHELL (I) : NULL
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 2.5.7
REMARK 200 STARTING MODEL: 3H4E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG550MME (13-14%), KSCN (0.15M), TRIS
REMARK 280 (0.1M, PH 8.5), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z
REMARK 290 6555 X-Y,X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -157.28753
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 136.21500
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -78.64377
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 90.81000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 -157.28753
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 0.500000 0.866025 0.000000 90.81000
REMARK 350 BIOMT2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 0.500000 -0.866025 0.000000 -45.40500
REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 -78.64377
REMARK 350 BIOMT3 6 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 ALA A 88
REMARK 465 GLY A 89
REMARK 465 PRO A 90
REMARK 465 ALA A 177
REMARK 465 SER A 178
REMARK 465 GLN A 179
REMARK 465 GLU A 180
REMARK 465 VAL A 181
REMARK 465 LYS A 182
REMARK 465 ASN A 183
REMARK 465 ALA A 184
REMARK 465 ALA A 185
REMARK 465 THR A 186
REMARK 465 GLU A 187
REMARK 465 GLY A 220
REMARK 465 VAL A 221
REMARK 465 GLY A 222
REMARK 465 GLY A 223
REMARK 465 PRO A 224
REMARK 465 GLY A 225
REMARK 465 HIS A 226
REMARK 465 LYS A 227
REMARK 465 ALA A 228
REMARK 465 ARG A 229
REMARK 465 VAL A 230
REMARK 465 LEU A 231
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 LEU A 6 CG CD1 CD2
REMARK 470 GLN A 7 CG CD OE1 NE2
REMARK 470 GLN A 9 CG CD OE1 NE2
REMARK 470 HIS A 87 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 91 CG1 CG2 CD1
REMARK 470 LYS A 158 CG CD CE NZ
REMARK 470 LYS A 203 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 31 -123.92 49.76
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5HGO A 1 231 UNP P12493 GAG_HV1N5 133 363
SEQADV 5HGO CYS A 14 UNP P12493 ALA 146 ENGINEERED MUTATION
SEQADV 5HGO GLY A 18 UNP P12493 ARG 150 ENGINEERED MUTATION
SEQADV 5HGO CYS A 45 UNP P12493 GLU 177 ENGINEERED MUTATION
SEQADV 5HGO ALA A 184 UNP P12493 TRP 316 ENGINEERED MUTATION
SEQADV 5HGO ALA A 185 UNP P12493 MET 317 ENGINEERED MUTATION
SEQRES 1 A 231 PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN
SEQRES 2 A 231 CYS ILE SER PRO GLY THR LEU ASN ALA TRP VAL LYS VAL
SEQRES 3 A 231 VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET
SEQRES 4 A 231 PHE SER ALA LEU SER CYS GLY ALA THR PRO GLN ASP LEU
SEQRES 5 A 231 ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA
SEQRES 6 A 231 MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA
SEQRES 7 A 231 GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE
SEQRES 8 A 231 ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE
SEQRES 9 A 231 ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP
SEQRES 10 A 231 MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR
SEQRES 11 A 231 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG
SEQRES 12 A 231 MET TYR SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY
SEQRES 13 A 231 PRO LYS GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR
SEQRES 14 A 231 LYS THR LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS
SEQRES 15 A 231 ASN ALA ALA THR GLU THR LEU LEU VAL GLN ASN ALA ASN
SEQRES 16 A 231 PRO ASP CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY
SEQRES 17 A 231 ALA THR LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL
SEQRES 18 A 231 GLY GLY PRO GLY HIS LYS ALA ARG VAL LEU
FORMUL 2 HOH *105(H2 O)
HELIX 1 AA1 SER A 16 ALA A 31 1 16
HELIX 2 AA2 GLU A 35 SER A 44 1 10
HELIX 3 AA3 THR A 48 THR A 58 1 11
HELIX 4 AA4 HIS A 62 HIS A 84 1 23
HELIX 5 AA5 ARG A 100 ALA A 105 1 6
HELIX 6 AA6 THR A 110 HIS A 120 1 11
HELIX 7 AA7 PRO A 125 SER A 146 1 22
HELIX 8 AA8 SER A 149 ILE A 153 5 5
HELIX 9 AA9 PRO A 160 GLN A 176 1 17
HELIX 10 AB1 LEU A 189 ASN A 193 1 5
HELIX 11 AB2 ASN A 195 GLY A 206 1 12
HELIX 12 AB3 THR A 210 GLN A 219 1 10
SHEET 1 AA1 2 ILE A 2 GLN A 4 0
SHEET 2 AA1 2 MET A 10 HIS A 12 -1 O VAL A 11 N VAL A 3
SSBOND 1 CYS A 14 CYS A 45 1555 6445 2.87
SSBOND 2 CYS A 198 CYS A 218 1555 1555 2.05
CISPEP 1 ASN A 121 PRO A 122 0 -0.55
CRYST1 90.810 90.810 56.880 90.00 90.00 120.00 P 6 6
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 0.011012 0.006358 0.000000 0.00000
SCALE2 0.000000 0.012716 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017581 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
