Header list of 1qck.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 06-MAY-99 1QCK
TITLE SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF,
TITLE 2 NMR, REGULARIZED MEAN STRUCTURE PLUS 20 INDIVIDUAL SIMULATED
TITLE 3 ANNEALING STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (BARRIER-TO-AUTOINTEGRATION FACTOR);
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA-BINDING PROTEIN, INTEGRATION, AIDS, RETROVIRUSES, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR G.M.CLORE
REVDAT 4 02-MAR-22 1QCK 1 REMARK
REVDAT 3 24-FEB-09 1QCK 1 VERSN
REVDAT 2 16-JUN-00 1QCK 1 EXPDTA DBREF
REVDAT 1 23-JUN-99 1QCK 0
JRNL AUTH J.JUSZEWSKI,A.M.GRONENBORN,G.M.CLORE
JRNL TITL IMPROVING THE PACKING AND ACCURACY OF NMR STRUCTURES WITH A
JRNL TITL 2 PSEUDOPOTENTIAL FOR THE RADIUS OF GYRATION
JRNL REF J.AM.CHEM.SOC. V. 121 2337 1999
JRNL REFN ISSN 0002-7863
JRNL DOI 10.1021/JA9843730
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.CAI,Y.HUANG,R.ZHENG,S.Q.WEI,R.GHIRLANDO,M.S.LEE,R.CRAIGIE,
REMARK 1 AUTH 2 A.M.GRONENBORN,G.M.CLORE
REMARK 1 TITL SOLUTION STRUCTURE OF THE CELLULAR FACTOR BAF RESPONSIBLE
REMARK 1 TITL 2 FOR PROTECTING RETROVIRAL DNA FROM AUTOINTEGRATION
REMARK 1 REF NAT.STRUCT.BIOL. V. 5 903 1998
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/2345
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS/XPLOR MODIFIED
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE REMARK 7
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT.
REMARK 3 229, 129 - 136 USING THE PROGRAM (BRUNGER)
REMARK 3 MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL.
REMARK 3 (1984) J.MAGN.RESON. SERIES B 104, 99 - 103), CARBON
REMARK 3 CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J.MAGN.RESON.
REMARK 3 SERIES B 106, 92 - 96) RESTRAINTS, 1H CHEMICAL SHIFT
REMARK 3 RESTRAINTS (KUSZEWSKI ET AL. (1995) J.MAGN.RESON. SERIES
REMARK 3 B 107, 293-297; (1996) J.MAGN.RESON. SERIES B 112,
REMARK 3 79-81), A CONFORMATIONAL DATABASE POTENTIAL
REMARK 3 (KUSZWESKI ET AL. (1996) PROTEIN SCI. 5, 1067-108 AND
REMARK 3 (1997) J.MAGN.RESON. 125, 171-177), AND A TERM FOR THE
REMARK 3 RADIUS OF GYRATION (KUSZEWSKI ET AL. (1999) J. AM. CHEM.
REMARK 3 SOC. 121, 2337-2338).
REMARK 3
REMARK 3 THE 3D STRUCTURE OF THE 21 KDA BAF DIMER WAS SOLVED BY
REMARK 3 MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR
REMARK 3 BASED ON 1655 EXPERIMENTAL RESTRAINTS (PER MONOMER):
REMARK 3 (A) INTRASUBUNIT: 288 SEQUENTIAL (|I-J|=1), 267 MEDIUM
REMARK 3 RANGE (1 < |I-J| >=5) AND 190 LONG RANGE (|I-J| >5)
REMARK 3 INTERRESIDUE, AND 7 INTRARESIDUE APPROXIMATE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS; 64 DISTANCE RESTRAINTS FOR 32
REMARK 3 HYDROGEN BONDS; 257 TORSION ANGLE (84 PHI, 78 PSI, 60 CHI1
REMARK 3 29 CHI2 AND 6 CHI3) RESTRAINTS; 66 THREE-BOND HN-HA
REMARK 3 COUPLING CONSTANT RESTRAINTS; 165 (87 CALPHA AND 78 CBETA)
REMARK 3 13C SHIFT RESTRAINTS; 44 1H METHYL PROTON CHEMICAL SHIFTS;
REMARK 3 259 DIPOLAR COUPLINGS (76 N-H, 76 CALPHA-C', 55 N-C'
REMARK 3 AND 52 HN-C').
REMARK 3 (B) 48 INTERSUBUNIT INTERPROTON DISTANCE RESTRAINTS.
REMARK 3
REMARK 3 RMS DEVIATIONS FOR RESTRAINED MINIMIZED MEAN STRUCTURE
REMARK 3 BOND LENGTHS : 0.0065
REMARK 3 BOND ANGLES : 0.645
REMARK 3 IMPROPER ANGLES : 0.809
REMARK 3 TORSION ANGLES : 0.44
REMARK 3 NOE : 0.024
REMARK 3 3JHNA COUP : 0.95
REMARK 3 13C SHIFTS RMS CA, CB (PPM): 1.06, 1.22
REMARK 3 DIPOLAR COUPLINGS NH CACO NCO HNCO
REMARK 3 RMS DIPOLAR (HZ): 0.48 1.35 0.49 1.27
REMARK 3 1H METHYL SHIFTS: 0.213
REMARK 3
REMARK 3 RESIDUE 500 WITH ATOMS OO, X, Y AND Z REPRESENTS THE
REMARK 3 MOLECULAR ALIGNMENT TENSOR FOR THE DIPOLAR COUPLINGS
REMARK 3 MEASURED IN A DILUTE LIQUID CRYSTAL.
REMARK 3 ATOM 2811 X ANI 500 206.152-144.189 1.390 1.00 94.16
REMARK 3 ATOM 2812 Y ANI 500 205.428-140.345 3.032 1.00 94.09
REMARK 3 ATOM 2813 Z ANI 500 202.691-142.020 0.244 1.00 93.80
REMARK 3 ATOM 2814 OO ANI 500 205.638-141.460 0.255 1.00 93.81
REMARK 3
REMARK 3 THE STRUCTURE IN THIS ENTRY IS THE RESTRAINED REGULARIZED
REMARK 3 MEAN STRUCTURE AND THE LAST NUMERIC COLUMN REPRESENTS THE
REMARK 3 RMS OF THE 40 INDIVIDUAL SIMULATED ANNEALING STRUCTURES
REMARK 3 FOUND IN PDB ENTRY 2EZY ABOUT THE MEAN COORDINATE
REMARK 3 POSITIONS. THE LAST NUMERIC COLUMN IN THE INDIVIDUAL SA
REMARK 3 STRUCTURES HAS NO MEANING.
REMARK 4
REMARK 4 1QCK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000001010.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600; DMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS/XPLOR MODIFIED
REMARK 210 METHOD USED : SEE REMARK 7
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : INDIVIDUAL SIMULATED ANNEALING
REMARK 210 STRUCTURES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE FIRST STRUCTURE IN THIS ENTRY IS THE RESTRAINED
REMARK 210 REGULARIZED MEAN STRUCTURE. THE REMAINING STRUCTURES ARE THE 20
REMARK 210 SIMULATED ANNEALING STRUCTURES
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: 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 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 4 PHE B 10 CG
REMARK 470 8 VAL A 20 O
REMARK 470 11 LYS B 32 C
REMARK 470 15 ALA A 42 N
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 CYS B 85 H LEU B 89 1.49
REMARK 500 O MET B 1 H THR B 3 1.51
REMARK 500 O MET A 1 H THR A 3 1.51
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 1 PHE B 88 CB PHE B 88 CG 0.163
REMARK 500 1 PHE B 88 CG PHE B 88 CD1 0.118
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 THR A 2 61.74 -56.30
REMARK 500 1 PRO A 14 160.01 -40.01
REMARK 500 1 PHE A 39 74.31 -106.43
REMARK 500 1 LYS A 54 19.47 56.85
REMARK 500 1 THR B 2 61.68 -56.03
REMARK 500 1 PRO B 14 160.05 -39.97
REMARK 500 1 PHE B 39 74.18 -107.15
REMARK 500 2 THR A 2 -159.90 56.39
REMARK 500 2 PRO A 14 161.17 -39.67
REMARK 500 2 PHE A 39 73.48 -104.81
REMARK 500 2 THR B 2 -160.01 56.45
REMARK 500 2 PRO B 14 161.14 -39.59
REMARK 500 2 PHE B 39 73.44 -104.75
REMARK 500 2 LYS B 54 19.95 58.27
REMARK 500 3 PRO A 14 156.86 -35.87
REMARK 500 3 LYS A 54 19.96 59.28
REMARK 500 3 CYS A 67 -37.00 -131.00
REMARK 500 3 PRO B 14 156.94 -35.93
REMARK 500 3 CYS B 67 -37.04 -131.00
REMARK 500 4 PRO A 14 155.29 -40.61
REMARK 500 4 PHE A 39 77.12 -106.23
REMARK 500 4 PRO B 14 155.33 -40.58
REMARK 500 4 PHE B 39 76.95 -106.36
REMARK 500 5 PRO A 14 155.12 -35.36
REMARK 500 5 PHE A 39 76.97 -104.70
REMARK 500 5 PHE A 88 -88.17 -105.56
REMARK 500 5 PRO B 14 155.13 -35.37
REMARK 500 5 PHE B 39 76.89 -104.72
REMARK 500 5 LYS B 54 19.99 60.00
REMARK 500 5 PHE B 88 -87.69 -104.34
REMARK 500 6 PRO A 14 155.63 -37.29
REMARK 500 6 PHE A 39 75.59 -106.51
REMARK 500 6 LYS A 54 19.62 59.19
REMARK 500 6 CYS A 67 -30.15 -132.32
REMARK 500 6 ALA A 69 152.90 -50.00
REMARK 500 6 PHE A 88 -86.73 -105.70
REMARK 500 6 PRO B 14 155.67 -37.35
REMARK 500 6 PHE B 39 75.45 -106.26
REMARK 500 6 LYS B 54 19.74 58.93
REMARK 500 6 CYS B 67 -30.00 -132.41
REMARK 500 6 PHE B 88 -86.24 -104.57
REMARK 500 7 THR A 2 -37.67 65.58
REMARK 500 7 PRO A 14 158.20 -40.33
REMARK 500 7 PHE A 39 77.07 -106.56
REMARK 500 7 LYS A 54 19.44 58.85
REMARK 500 7 ALA A 69 153.00 -49.99
REMARK 500 7 PHE A 88 -84.86 -102.59
REMARK 500 7 THR B 2 -37.83 65.57
REMARK 500 7 PRO B 14 158.20 -40.25
REMARK 500 7 PHE B 39 77.00 -106.30
REMARK 500
REMARK 500 THIS ENTRY HAS 141 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QCK A 1 89 UNP O75531 BAF_HUMAN 1 89
DBREF 1QCK B 1 89 UNP O75531 BAF_HUMAN 1 89
SEQRES 1 A 89 MET THR THR SER GLN LYS HIS ARG ASP PHE VAL ALA GLU
SEQRES 2 A 89 PRO MET GLY GLU LYS PRO VAL GLY SER LEU ALA GLY ILE
SEQRES 3 A 89 GLY GLU VAL LEU GLY LYS LYS LEU GLU GLU ARG GLY PHE
SEQRES 4 A 89 ASP LYS ALA TYR VAL VAL LEU GLY GLN PHE LEU VAL LEU
SEQRES 5 A 89 LYS LYS ASP GLU ASP LEU PHE ARG GLU TRP LEU LYS ASP
SEQRES 6 A 89 THR CYS GLY ALA ASN ALA LYS GLN SER ARG ASP CYS PHE
SEQRES 7 A 89 GLY CYS LEU ARG GLU TRP CYS ASP ALA PHE LEU
SEQRES 1 B 89 MET THR THR SER GLN LYS HIS ARG ASP PHE VAL ALA GLU
SEQRES 2 B 89 PRO MET GLY GLU LYS PRO VAL GLY SER LEU ALA GLY ILE
SEQRES 3 B 89 GLY GLU VAL LEU GLY LYS LYS LEU GLU GLU ARG GLY PHE
SEQRES 4 B 89 ASP LYS ALA TYR VAL VAL LEU GLY GLN PHE LEU VAL LEU
SEQRES 5 B 89 LYS LYS ASP GLU ASP LEU PHE ARG GLU TRP LEU LYS ASP
SEQRES 6 B 89 THR CYS GLY ALA ASN ALA LYS GLN SER ARG ASP CYS PHE
SEQRES 7 B 89 GLY CYS LEU ARG GLU TRP CYS ASP ALA PHE LEU
HELIX 1 1 GLN A 5 ALA A 12 1 8
HELIX 2 2 VAL A 20 SER A 22 5 3
HELIX 3 3 GLU A 28 ARG A 37 1 10
HELIX 4 4 ALA A 42 VAL A 51 1 10
HELIX 5 5 GLU A 56 CYS A 67 1 12
HELIX 6 6 ALA A 71 ALA A 87 1 17
HELIX 7 7 GLN B 5 ALA B 12 1 8
HELIX 8 8 VAL B 20 SER B 22 5 3
HELIX 9 9 GLU B 28 ARG B 37 1 10
HELIX 10 10 ALA B 42 VAL B 51 1 10
HELIX 11 11 GLU B 56 CYS B 67 1 12
HELIX 12 12 ALA B 71 ALA B 87 1 17
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