HEADER VIRAL PROTEIN 14-MAY-07 2PXR
TITLE CRYSTAL STRUCTURE OF HIV-1 CA146 IN THE PRESENCE OF CAP-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAG-POL POLYPROTEIN (PR160GAG-POL);
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: NL43
KEYWDS VIRAL CAPSID, HIV-1, ANTI-VIRAL, SMALL MOLECULE INHIBITION, VIRAL
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.N.KELLY
REVDAT 5 21-FEB-24 2PXR 1 REMARK LINK
REVDAT 4 13-JUL-11 2PXR 1 VERSN
REVDAT 3 24-FEB-09 2PXR 1 VERSN
REVDAT 2 16-OCT-07 2PXR 1 JRNL
REVDAT 1 25-SEP-07 2PXR 0
JRNL AUTH B.N.KELLY,S.KYERE,I.KINDE,C.TANG,B.R.HOWARD,H.ROBINSON,
JRNL AUTH 2 W.I.SUNDQUIST,M.F.SUMMERS,C.P.HILL
JRNL TITL STRUCTURE OF THE ANTIVIRAL ASSEMBLY INHIBITOR CAP-1 COMPLEX
JRNL TITL 2 WITH THE HIV-1 CA PROTEIN.
JRNL REF J.MOL.BIOL. V. 373 355 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17826792
JRNL DOI 10.1016/J.JMB.2007.07.070
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 21916
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.163
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 : 1107
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1146
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1129
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 179
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.90000
REMARK 3 B22 (A**2) : -1.16000
REMARK 3 B33 (A**2) : 0.26000
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): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.088
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.664
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1223 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1666 ; 1.873 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 148 ; 5.519 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 57 ;37.792 ;25.088
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 224 ;14.835 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;20.499 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 185 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 925 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 618 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 864 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 127 ; 0.188 ; 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): 68 ; 0.262 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.239 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 3 ; 0.063 ; 0.200
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): 764 ; 2.024 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1225 ; 2.961 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 520 ; 3.757 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 441 ; 5.544 ; 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): 1284 ; 2.506 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 182 ; 8.637 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1192 ; 7.007 ; 3.000
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 : 1.40
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. AUTHORS ALSO STATE THAT THE STRUCTURE 2PXR WAS
REMARK 3 DETERMINED BY X-RAY CRYSTALLOGRAPHY FROM CRYSTALS OF CA146 THAT
REMARK 3 WERE GROWN IN THE PRESENCE OF CAP-1. CAP-1 IS NOT VISIBLE IN
REMARK 3 ELECTRON DENSITY MAPS, ALTHOUGH NMR DATA PROVIDED LIGAND-PROTEIN
REMARK 3 NOES THAT ALLOWED THEM TO BUILD A JOINT REFINED STRUCTURE 2JPR.
REMARK 4
REMARK 4 2PXR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042898.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-05
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 : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21930
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 53.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.31800
REMARK 200 R SYM FOR SHELL (I) : 0.31800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH, 5% PEG 8000, 20% PEG
REMARK 280 300, 10% GLYCEROL, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 286K
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 53.14300
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 53.14300
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 21.09350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.38850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.09350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.38850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.14300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.09350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 31.38850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.14300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.09350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 31.38850
REMARK 290 SMTRY3 8 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: THE BIOLOGICAL ASSEMBLY IS A HEXAMER
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -164.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -53.14300
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL C 400 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN C 402 LIES ON A SPECIAL POSITION.
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 SER C 146
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 CD1 ILE C 37 OD1 ASN C 139 2.14
REMARK 500 O HOH C 439 O HOH C 572 2.18
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 C 544 O HOH C 544 4565 2.16
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 ARG C 100 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG C 100 NE - CZ - NH2 ANGL. DEV. = -5.4 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 GLN C 63 -76.10 54.35
REMARK 500 GLN C 63 -69.85 34.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 84 ND1
REMARK 620 2 HIS C 87 ND1 112.7
REMARK 620 3 GLU C 98 OE1 97.1 120.9
REMARK 620 4 GLU C 98 OE2 102.9 101.6 19.7
REMARK 620 5 HOH C 509 O 104.4 114.6 104.8 120.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 120 NE2
REMARK 620 2 HIS C 120 NE2 21.5
REMARK 620 3 HOH C 574 O 118.1 131.2
REMARK 620 4 HOH C 574 O 96.2 108.6 96.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PWM RELATED DB: PDB
REMARK 900 UNLIGANDED CA146 A92E REAL CELL
REMARK 900 RELATED ID: 2PWO RELATED DB: PDB
REMARK 900 UNLIGANDED CA146 A92E PSUEDO CELL
REMARK 900 RELATED ID: 2JPR RELATED DB: PDB
DBREF 2PXR C 1 146 UNP P12497 POL_HV1N5 133 278
SEQRES 1 C 146 PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN
SEQRES 2 C 146 ALA ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL
SEQRES 3 C 146 VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET
SEQRES 4 C 146 PHE SER ALA LEU SER GLU GLY ALA THR PRO GLN ASP LEU
SEQRES 5 C 146 ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA
SEQRES 6 C 146 MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA
SEQRES 7 C 146 GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE
SEQRES 8 C 146 ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE
SEQRES 9 C 146 ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP
SEQRES 10 C 146 MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR
SEQRES 11 C 146 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG
SEQRES 12 C 146 MET TYR SER
HET CL C 400 1
HET ZN C 401 1
HET ZN C 402 1
HETNAM CL CHLORIDE ION
HETNAM ZN ZINC ION
FORMUL 2 CL CL 1-
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 HOH *179(H2 O)
HELIX 1 1 SER C 16 ALA C 31 1 16
HELIX 2 2 GLU C 35 LEU C 43 1 9
HELIX 3 3 THR C 48 THR C 58 1 11
HELIX 4 4 VAL C 59 HIS C 62 5 4
HELIX 5 5 GLN C 63 HIS C 84 1 22
HELIX 6 6 ARG C 100 ALA C 105 1 6
HELIX 7 7 THR C 110 THR C 119 1 10
HELIX 8 8 PRO C 125 TYR C 145 1 21
SHEET 1 A 2 ILE C 2 GLN C 4 0
SHEET 2 A 2 MET C 10 HIS C 12 -1 O VAL C 11 N VAL C 3
LINK ND1 HIS C 84 ZN ZN C 401 3554 1555 2.04
LINK ND1 HIS C 87 ZN ZN C 401 1555 1555 2.09
LINK OE1AGLU C 98 ZN ZN C 401 3554 1555 1.93
LINK OE2BGLU C 98 ZN ZN C 401 3554 1555 1.96
LINK NE2AHIS C 120 ZN ZN C 402 1555 1555 1.96
LINK NE2BHIS C 120 ZN ZN C 402 1555 1555 2.19
LINK ZN ZN C 401 O HOH C 509 1555 1555 2.02
LINK ZN ZN C 402 O HOH C 574 1555 1555 2.54
LINK ZN ZN C 402 O HOH C 574 1555 3554 2.48
CISPEP 1 ASN C 121 PRO C 122 0 -3.31
SITE 1 AC1 2 GLN C 50 LEU C 111
SITE 1 AC2 4 HIS C 84 HIS C 87 GLU C 98 HOH C 509
SITE 1 AC3 2 HIS C 120 HOH C 574
CRYST1 42.187 62.777 106.286 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 0.023704 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015929 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009409 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
