Header list of 1pve.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 27-JUN-03 1PVE
TITLE SOLUTION STRUCTURE OF XPC BINDING DOMAIN OF HHR23B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: XPC BINDING DOMAIN;
COMPND 5 SYNONYM: HHR23B;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HH23B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS HHR23B, XPC BINDING DOMAIN, NMR SOLUTION STRUCTURE, NUCLEOTIDE
KEYWDS 2 EXCISION REPAIR, CHAPS, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.KIM,K.-S.RYU,H.J.KIM,B.-S.CHOI
REVDAT 4 02-MAR-22 1PVE 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1PVE 1 VERSN
REVDAT 2 21-JUN-05 1PVE 1 JRNL
REVDAT 1 10-AUG-04 1PVE 0
JRNL AUTH B.KIM,K.S.RYU,H.J.KIM,S.J.CHO,B.S.CHOI
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE XPC-BINDING
JRNL TITL 2 DOMAIN OF THE HUMAN DNA REPAIR PROTEIN HHR23B.
JRNL REF FEBS J. V. 272 2467 2005
JRNL REFN ISSN 1742-464X
JRNL PMID 15885096
JRNL DOI 10.1111/J.1742-4658.2005.04667.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.3C, AMBER 7
REMARK 3 AUTHORS : VARIAN (VNMR), DAVID A. CASE ETC (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PVE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019601.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 40MM SODIUM PHOSPHATE, 160MM
REMARK 210 SODIUM CHLORIDE, 10MM CHAPS
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM HHR23B(275-342) U-15N, 13C;
REMARK 210 40MM PHOSPHATE BUFFER NA; 10MM
REMARK 210 CHAPS NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, CYANA 1.6
REMARK 210 METHOD USED : AUTOMATIC NOE ASSIGNMENT,
REMARK 210 DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
REMARK 210
REMARK 210 REMARK: THE STRUCTURES ARE BASED ON A TOTAL OF 1312 RESTRAINTS,
REMARK 210 1242 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 70 DIHEDRAL ANGLE
REMARK 210 RESTRAINTS ( 14 FROM JHNHA AND 56 FROM TALOS)
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
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 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 3 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 7 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 7 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 11 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 12 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 13 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 13 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 14 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 15 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 16 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 18 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 20 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.3 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 1 MET A 4 86.22 -156.16
REMARK 500 1 GLN A 17 -47.68 -130.75
REMARK 500 3 SER A 2 37.78 -153.96
REMARK 500 3 LEU A 6 -10.02 61.53
REMARK 500 3 HIS A 50 28.47 -141.63
REMARK 500 3 ALA A 65 -10.39 -144.76
REMARK 500 4 GLN A 17 -50.46 -128.83
REMARK 500 4 ASN A 40 73.35 -154.16
REMARK 500 4 HIS A 50 20.80 -140.63
REMARK 500 5 HIS A 50 24.30 -141.69
REMARK 500 5 GLU A 64 -166.03 58.96
REMARK 500 6 LEU A 6 20.00 57.64
REMARK 500 6 ARG A 10 26.97 -69.97
REMARK 500 6 PRO A 61 154.25 -49.91
REMARK 500 7 GLN A 23 2.75 -67.87
REMARK 500 7 ASN A 40 73.20 -151.87
REMARK 500 8 GLU A 7 -26.52 -150.57
REMARK 500 8 GLN A 23 2.30 -68.91
REMARK 500 9 LEU A 6 -6.57 60.94
REMARK 500 10 ASN A 11 19.79 -144.46
REMARK 500 10 GLN A 17 -51.15 -128.12
REMARK 500 10 GLN A 23 2.26 -67.95
REMARK 500 10 ASN A 40 72.90 -151.84
REMARK 500 10 GLN A 63 -2.65 63.32
REMARK 500 11 MET A 4 153.19 65.43
REMARK 500 11 GLN A 23 0.68 -66.40
REMARK 500 11 ASN A 40 72.69 -153.66
REMARK 500 12 ASN A 11 22.22 -144.23
REMARK 500 12 GLN A 14 -22.96 48.56
REMARK 500 12 GLN A 17 -51.26 -131.68
REMARK 500 12 GLU A 64 -42.96 72.41
REMARK 500 12 ALA A 65 -8.47 -141.61
REMARK 500 13 GLN A 14 -15.98 59.14
REMARK 500 13 GLN A 23 1.44 -69.13
REMARK 500 13 ASN A 40 76.13 -158.82
REMARK 500 13 HIS A 50 27.52 -141.18
REMARK 500 13 GLU A 64 -40.51 -137.92
REMARK 500 13 ALA A 65 18.90 47.78
REMARK 500 14 ALA A 65 -28.49 58.19
REMARK 500 15 MET A 4 21.77 -151.06
REMARK 500 15 ARG A 10 2.52 -69.72
REMARK 500 16 ASN A 40 74.75 -155.19
REMARK 500 17 SER A 2 91.54 -69.68
REMARK 500 17 GLN A 17 -42.04 -135.02
REMARK 500 17 HIS A 50 26.18 -140.78
REMARK 500 18 SER A 2 -31.17 -142.20
REMARK 500 18 HIS A 3 -22.21 -150.70
REMARK 500 18 ASN A 40 61.26 -151.36
REMARK 500 18 GLN A 63 17.69 55.48
REMARK 500 18 GLU A 64 -31.46 -147.11
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
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 20 ARG A 19 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PVE A 5 72 UNP P54727 RD23B_HUMAN 275 342
SEQADV 1PVE GLY A 1 UNP P54727 CLONING ARTIFACT
SEQADV 1PVE SER A 2 UNP P54727 CLONING ARTIFACT
SEQADV 1PVE HIS A 3 UNP P54727 CLONING ARTIFACT
SEQADV 1PVE MET A 4 UNP P54727 CLONING ARTIFACT
SEQRES 1 A 72 GLY SER HIS MET PRO LEU GLU PHE LEU ARG ASN GLN PRO
SEQRES 2 A 72 GLN PHE GLN GLN MET ARG GLN ILE ILE GLN GLN ASN PRO
SEQRES 3 A 72 SER LEU LEU PRO ALA LEU LEU GLN GLN ILE GLY ARG GLU
SEQRES 4 A 72 ASN PRO GLN LEU LEU GLN GLN ILE SER GLN HIS GLN GLU
SEQRES 5 A 72 HIS PHE ILE GLN MET LEU ASN GLU PRO VAL GLN GLU ALA
SEQRES 6 A 72 GLY GLY GLN GLY GLY GLY GLY
HELIX 1 1 LEU A 6 ARG A 10 5 5
HELIX 2 2 GLN A 17 GLN A 23 1 7
HELIX 3 3 ASN A 25 SER A 27 5 3
HELIX 4 4 LEU A 28 ARG A 38 1 11
HELIX 5 5 ASN A 40 GLN A 49 1 10
HELIX 6 6 HIS A 50 GLU A 60 1 11
HELIX 7 7 GLU A 64 GLY A 69 5 6
CISPEP 1 GLY A 71 GLY A 72 8 -0.26
CISPEP 2 GLY A 67 GLN A 68 9 -3.55
CISPEP 3 SER A 2 HIS A 3 16 -0.77
CISPEP 4 GLU A 64 ALA A 65 19 -7.18
CISPEP 5 GLY A 67 GLN A 68 19 -4.85
CISPEP 6 GLY A 71 GLY A 72 19 -5.20
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes