Header list of 1qpm.pdb file
Complete list - r 2 2 Bytes
HEADER VIRAL PROTEIN 26-MAY-99 1QPM
TITLE NMR STRUCTURE OF THE MU BACTERIOPHAGE REPRESSOR DNA-BINDING DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (MU BACTERIOPHAGE C REPRESSOR PROTEIN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE MU;
SOURCE 3 ORGANISM_TAXID: 10677;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS HELIX-TURN-HELIX, MU BACTERIOPHAGE, REPRESSOR, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 26
MDLTYP MINIMIZED AVERAGE
AUTHOR U.ILANGOVAN,J.M.WOJCIAK,K.M.CONNOLLY,R.T.CLUBB
REVDAT 4 02-MAR-22 1QPM 1 REMARK
REVDAT 3 24-FEB-09 1QPM 1 VERSN
REVDAT 2 29-DEC-99 1QPM 1 JRNL HEADER REMARK
REVDAT 1 04-JUN-99 1QPM 0
JRNL AUTH U.ILANGOVAN,J.M.WOJCIAK,K.M.CONNOLLY,R.T.CLUBB
JRNL TITL NMR STRUCTURE AND FUNCTIONAL STUDIES OF THE MU REPRESSOR
JRNL TITL 2 DNA-BINDING DOMAIN.
JRNL REF BIOCHEMISTRY V. 38 8367 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10387082
JRNL DOI 10.1021/BI990530B
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843, X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: INFORMATION IN PRIMARY REFERENCE
REMARK 4
REMARK 4 1QPM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000009119.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300.0
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM REPRESSOR U-15N,13C 50MM
REMARK 210 PHOSPHATE (PH 6.2); 100MM NACL;
REMARK 210 2.5MM D-DTT; 93% H2O, 7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE PRIMARY REFERENCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON- BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 26
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING HETERONUCLEAR NMR METHODS.
REMARK 210 COMPLETE
REMARK 210 INFORMATION IN PRIMARY REFERENCE.
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 LEU A 77 H THR A 81 1.52
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 SER A 31 -168.31 -70.03
REMARK 500 1 GLU A 50 26.96 -68.25
REMARK 500 1 LYS A 56 80.94 59.83
REMARK 500 1 PRO A 66 155.05 -41.55
REMARK 500 1 SER A 80 -34.74 -150.51
REMARK 500 2 SER A 31 -165.86 -71.69
REMARK 500 2 LYS A 56 164.70 53.93
REMARK 500 2 PRO A 66 164.75 -40.88
REMARK 500 3 SER A 31 -166.24 -70.86
REMARK 500 3 LYS A 56 -141.47 52.01
REMARK 500 4 LYS A 56 113.40 57.08
REMARK 500 4 PRO A 66 160.10 -36.28
REMARK 500 4 SER A 80 -5.26 56.80
REMARK 500 5 SER A 31 -167.42 -71.07
REMARK 500 5 TRP A 44 156.36 -47.21
REMARK 500 5 GLU A 50 -144.24 36.45
REMARK 500 5 LYS A 53 162.92 55.84
REMARK 500 5 LYS A 56 167.70 54.40
REMARK 500 5 PRO A 66 168.46 -44.90
REMARK 500 6 SER A 31 -167.91 -69.99
REMARK 500 6 TRP A 44 172.57 -51.80
REMARK 500 6 LYS A 56 126.17 57.64
REMARK 500 6 PRO A 66 169.55 -43.10
REMARK 500 6 LEU A 79 -75.65 -85.71
REMARK 500 7 MET A 28 79.11 -119.74
REMARK 500 7 SER A 31 -163.72 -71.87
REMARK 500 7 GLU A 50 -156.62 36.37
REMARK 500 7 LYS A 56 146.49 57.45
REMARK 500 7 PRO A 66 158.66 -39.25
REMARK 500 8 SER A 31 -169.62 -70.08
REMARK 500 8 VAL A 52 -90.98 -84.32
REMARK 500 8 LYS A 56 118.69 54.97
REMARK 500 8 PRO A 66 164.30 -41.66
REMARK 500 9 SER A 31 -158.67 -74.82
REMARK 500 9 GLU A 50 168.04 54.73
REMARK 500 9 LYS A 53 -48.75 -155.21
REMARK 500 9 LYS A 56 -179.39 52.10
REMARK 500 9 ALA A 57 -169.94 -170.10
REMARK 500 9 PRO A 66 166.03 -44.56
REMARK 500 10 SER A 31 -168.54 -71.14
REMARK 500 10 GLU A 50 26.45 -77.88
REMARK 500 10 LYS A 56 76.09 57.89
REMARK 500 10 PRO A 66 161.57 -42.29
REMARK 500 11 SER A 31 -166.97 -70.96
REMARK 500 11 LYS A 56 -138.00 50.16
REMARK 500 11 PRO A 66 157.93 -35.95
REMARK 500 12 SER A 31 -164.13 -70.90
REMARK 500 12 VAL A 52 33.25 -172.86
REMARK 500 12 LYS A 53 19.52 57.87
REMARK 500 12 PRO A 66 158.52 -43.72
REMARK 500
REMARK 500 THIS ENTRY HAS 114 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QPM A 13 81 UNP P06019 RPC1_BPMU 13 81
SEQRES 1 A 69 LYS SER ILE TRP CYS SER PRO GLN GLU ILE MET ALA ALA
SEQRES 2 A 69 ASP GLY MET PRO GLY SER VAL ALA GLY VAL HIS TYR ARG
SEQRES 3 A 69 ALA ASN VAL GLN GLY TRP THR LYS ARG LYS LYS GLU GLY
SEQRES 4 A 69 VAL LYS GLY GLY LYS ALA VAL GLU TYR ASP VAL MET SER
SEQRES 5 A 69 MET PRO THR LYS GLU ARG GLU GLN VAL ILE ALA HIS LEU
SEQRES 6 A 69 GLY LEU SER THR
HELIX 1 1 SER A 18 ALA A 24 1 7
HELIX 2 2 SER A 31 GLN A 42 1 12
HELIX 3 3 VAL A 62 MET A 65 5 4
HELIX 4 4 PRO A 66 LEU A 79 1 14
SHEET 1 A 2 LYS A 46 LYS A 49 0
SHEET 2 A 2 ALA A 57 TYR A 60 -1 O ALA A 57 N LYS A 49
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