Header list of 1ghh.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 19-DEC-00 1GHH
TITLE SOLUTION STRUCTURE OF DINI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DAMAGE-INDUCIBLE PROTEIN I;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DINI;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS BICELLE, DINI, DIPOLAR COUPLING, LIQUID CRYSTAL, PF1, RECA, PROTEIN
KEYWDS 2 BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.E.RAMIREZ,O.N.VOLOSHIN,R.D.CAMERINI-OTERO,A.BAX
REVDAT 3 23-FEB-22 1GHH 1 REMARK
REVDAT 2 24-FEB-09 1GHH 1 VERSN
REVDAT 1 10-JAN-01 1GHH 0
SPRSDE 10-JAN-01 1GHH 1F0A
JRNL AUTH B.E.RAMIREZ,O.N.VOLOSHIN,R.D.CAMERINI-OTERO,A.BAX
JRNL TITL SOLUTION STRUCTURE OF DINI PROVIDES INSIGHT INTO ITS MODE OF
JRNL TITL 2 RECA INACTIVATION.
JRNL REF PROTEIN SCI. V. 9 2161 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 11152126
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED IN A THREE
REMARK 3 STAGE PROCESS. IN THE FIRST STAGE, FOLDS WERE CALCULATED FROM A
REMARK 3 FULLY-EXTENDED CHAIN BASED ONLY ON TORSION AND NOE RESTRAINTS.
REMARK 3 IN THE SECOND STAGE, THE TEN BEST STRUCTURES OF STAGE 1 WERE
REMARK 3 USED AS STARTING STRUCTURES IN A SIMULATED ANNEALING CALCULATION
REMARK 3 THAT INCLUDED DIPOLAR RESTRAINTS MEASURED IN BICELLES. IN THE
REMARK 3 LAST STAGE, THE TEN LOWEST ENERGY STRUCTURES OF STAGE 2 WERE
REMARK 3 USED AS STARTING STRUCTURES IN A SIMULATED ANNEALING CALCULATION
REMARK 3 THAT ALSO INCLUDED DIPOLAR RESTRAINTS MEASURED IN A PHAGE LIQUID
REMARK 3 CRYSTAL.
REMARK 4
REMARK 4 1GHH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000001518.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0; 298.0; 302.0
REMARK 210 PH : 6.6; 6.6; 6.6
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM DINI U-13C,15N, 20 MM
REMARK 210 PHOSPHATE BUFFER, 100 MM NACL;
REMARK 210 PH 6.6; 95% H2O, 5% D2O; 0.6 MM
REMARK 210 DINI U-13C,15N, 20 MM PHOSPHATE
REMARK 210 BUFFER, 100 MM NACL; PH 6.6; 99%
REMARK 210 D2O, 1% H2O; 0.6 MM DINI U-13C,
REMARK 210 15N, 20 MM PHOSPHATE BUFFER, 100
REMARK 210 MM NACL; PH 6.6; BICELLE OR
REMARK 210 PHAGE LIQUID CRYSTAL, 95% H2O, 5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY; HNCG;
REMARK 210 HN(CO)CG; IPAP_15N_HSQC; HNCO;
REMARK 210 (HA)CA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS IN CARTESIAN SPACE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING TWO SETS OF DIPOLAR
REMARK 210 COUPLING RESTRAINTS. ONE SET WAS RECORDED IN A BICELLE LIQUID
REMARK 210 CRYSTAL SOLUTION; THE OTHER SET WAS RECORDED IN A PHAGE LIQUID
REMARK 210 CRYSTAL SOLUTION. SEE CITATION 1 FOR DETAILS ON SOLUTION
REMARK 210 CONDITIONS. A TOTAL OF 127 N-H, 135 CA-HA, 138 CA-CO, 61 N-CO,
REMARK 210 AND 64 CO-HN DIPOLAR RESTRAINTS WERE USED IN THE STRUCTURE
REMARK 210 CALCULATION. ADDITIONAL RESTRAINTS INCLUDED 592 INTRARESIDUE,
REMARK 210 278 SHORT RANGE, 104 MEDIUM RANGE, AND 140 LONG RANGE NOE
REMARK 210 RESTRAINTS AS WELL AS 76 PHI, 51 PSI, AND 21 CHI1 DIHEDRAL
REMARK 210 RESTRAINTS. A CONFORMATIONAL DATABASE WAS EMPLOYED IN THE
REMARK 210 SIMULATED ANNEALING CALCULATION. NO RADIUS OF GYRATION TERM WAS
REMARK 210 EMPLOYED IN THE SIMULATED ANNEALING CALCULATION.
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: 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 PRO A 14 H GLY A 16 1.46
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 PRO A 14 150.31 -48.17
REMARK 500 1 ALA A 15 48.76 -56.86
REMARK 500 2 PRO A 14 151.31 -46.80
REMARK 500 2 ALA A 15 51.48 -58.29
REMARK 500 3 PRO A 14 150.36 -47.39
REMARK 500 3 ALA A 15 50.87 -57.15
REMARK 500 4 ALA A 15 50.39 -56.72
REMARK 500 5 ALA A 15 51.04 -56.79
REMARK 500 6 PRO A 14 150.63 -47.77
REMARK 500 6 ALA A 15 50.40 -57.73
REMARK 500 7 ALA A 15 47.54 -57.09
REMARK 500 8 PRO A 14 152.90 -49.01
REMARK 500 8 ALA A 15 50.56 -58.11
REMARK 500 9 ALA A 15 52.10 -57.18
REMARK 500 10 PRO A 14 150.85 -48.02
REMARK 500 10 ALA A 15 51.79 -56.91
REMARK 500 11 ALA A 15 52.53 -56.69
REMARK 500 12 ALA A 15 48.56 -56.63
REMARK 500 13 ALA A 15 49.28 -56.98
REMARK 500 14 ALA A 15 50.91 -56.58
REMARK 500 15 ALA A 15 49.56 -56.39
REMARK 500 16 PRO A 14 151.63 -49.02
REMARK 500 16 ALA A 15 53.46 -58.44
REMARK 500 17 ALA A 15 49.09 -55.82
REMARK 500 18 PRO A 14 150.81 -49.85
REMARK 500 18 ALA A 15 49.08 -57.95
REMARK 500 19 ALA A 15 48.55 -57.09
REMARK 500 20 PRO A 14 150.06 -47.31
REMARK 500 20 ALA A 15 48.33 -56.29
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 1 ARG A 2 0.31 SIDE CHAIN
REMARK 500 1 ARG A 27 0.29 SIDE CHAIN
REMARK 500 1 ARG A 28 0.27 SIDE CHAIN
REMARK 500 1 ARG A 43 0.19 SIDE CHAIN
REMARK 500 1 ARG A 62 0.27 SIDE CHAIN
REMARK 500 2 ARG A 2 0.10 SIDE CHAIN
REMARK 500 2 ARG A 27 0.19 SIDE CHAIN
REMARK 500 2 ARG A 28 0.30 SIDE CHAIN
REMARK 500 2 ARG A 62 0.28 SIDE CHAIN
REMARK 500 3 ARG A 28 0.30 SIDE CHAIN
REMARK 500 3 ARG A 62 0.19 SIDE CHAIN
REMARK 500 4 ARG A 43 0.25 SIDE CHAIN
REMARK 500 4 ARG A 62 0.23 SIDE CHAIN
REMARK 500 5 ARG A 2 0.30 SIDE CHAIN
REMARK 500 5 ARG A 27 0.19 SIDE CHAIN
REMARK 500 5 ARG A 28 0.30 SIDE CHAIN
REMARK 500 5 ARG A 43 0.25 SIDE CHAIN
REMARK 500 5 ARG A 62 0.10 SIDE CHAIN
REMARK 500 6 ARG A 27 0.30 SIDE CHAIN
REMARK 500 6 ARG A 28 0.31 SIDE CHAIN
REMARK 500 6 ARG A 62 0.31 SIDE CHAIN
REMARK 500 7 ARG A 2 0.24 SIDE CHAIN
REMARK 500 7 ARG A 27 0.25 SIDE CHAIN
REMARK 500 7 ARG A 28 0.08 SIDE CHAIN
REMARK 500 7 ARG A 43 0.20 SIDE CHAIN
REMARK 500 7 ARG A 62 0.29 SIDE CHAIN
REMARK 500 8 ARG A 2 0.30 SIDE CHAIN
REMARK 500 8 ARG A 27 0.21 SIDE CHAIN
REMARK 500 8 ARG A 62 0.29 SIDE CHAIN
REMARK 500 9 ARG A 2 0.20 SIDE CHAIN
REMARK 500 9 ARG A 27 0.31 SIDE CHAIN
REMARK 500 9 ARG A 28 0.25 SIDE CHAIN
REMARK 500 9 ARG A 43 0.28 SIDE CHAIN
REMARK 500 9 ARG A 62 0.12 SIDE CHAIN
REMARK 500 10 ARG A 2 0.30 SIDE CHAIN
REMARK 500 10 ARG A 27 0.25 SIDE CHAIN
REMARK 500 10 ARG A 28 0.27 SIDE CHAIN
REMARK 500 10 ARG A 62 0.08 SIDE CHAIN
REMARK 500 11 ARG A 2 0.19 SIDE CHAIN
REMARK 500 11 ARG A 27 0.15 SIDE CHAIN
REMARK 500 11 ARG A 28 0.21 SIDE CHAIN
REMARK 500 11 ARG A 43 0.24 SIDE CHAIN
REMARK 500 11 ARG A 62 0.25 SIDE CHAIN
REMARK 500 12 ARG A 2 0.30 SIDE CHAIN
REMARK 500 12 ARG A 28 0.09 SIDE CHAIN
REMARK 500 13 ARG A 2 0.24 SIDE CHAIN
REMARK 500 13 ARG A 27 0.12 SIDE CHAIN
REMARK 500 13 ARG A 28 0.27 SIDE CHAIN
REMARK 500 13 ARG A 43 0.29 SIDE CHAIN
REMARK 500 13 ARG A 62 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 80 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GHH A 1 81 UNP P0ABR1 DINI_ECOLI 1 81
SEQRES 1 A 81 MET ARG ILE GLU VAL THR ILE ALA LYS THR SER PRO LEU
SEQRES 2 A 81 PRO ALA GLY ALA ILE ASP ALA LEU ALA GLY GLU LEU SER
SEQRES 3 A 81 ARG ARG ILE GLN TYR ALA PHE PRO ASP ASN GLU GLY HIS
SEQRES 4 A 81 VAL SER VAL ARG TYR ALA ALA ALA ASN ASN LEU SER VAL
SEQRES 5 A 81 ILE GLY ALA THR LYS GLU ASP LYS GLN ARG ILE SER GLU
SEQRES 6 A 81 ILE LEU GLN GLU THR TRP GLU SER ALA ASP ASP TRP PHE
SEQRES 7 A 81 VAL SER GLU
HELIX 1 1 GLY A 16 PHE A 33 1 18
HELIX 2 2 THR A 56 SER A 73 1 18
HELIX 3 3 SER A 73 PHE A 78 1 6
SHEET 1 A 3 HIS A 39 ALA A 45 0
SHEET 2 A 3 ARG A 2 ALA A 8 1 N ILE A 3 O HIS A 39
SHEET 3 A 3 ASN A 49 ILE A 53 -1 O ASN A 49 N THR A 6
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 - b 23 2 Bytes