Header list of 1rwd.pdb file
Complete list - 27 202 Bytes
HEADER ELECTRON TRANSPORT 16-DEC-03 1RWD
TITLE BACKBONE NMR STRUCTURE OF A MUTANT P. FURIOSUS RUBREDOXIN USING
TITLE 2 RESIDUAL DIPOLAR COUPLINGS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUBREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RD;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 GENE: RUB, PF1282;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NCM533;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS RESIDUAL DIPOLAR COUPLINGS, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, SOUTHEAST COLLABORATORY FOR STRUCTURAL
KEYWDS 3 GENOMICS, SECSG, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR F.TIAN,H.VALAFAR,J.H.PRESTEGARD,SOUTHEAST COLLABORATORY FOR
AUTHOR 2 STRUCTURAL GENOMICS (SECSG)
REVDAT 4 27-OCT-21 1RWD 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1RWD 1 VERSN
REVDAT 2 01-FEB-05 1RWD 1 AUTHOR KEYWDS REMARK
REVDAT 1 23-DEC-03 1RWD 0
SPRSDE 23-DEC-03 1RWD 1M2Y
JRNL AUTH F.TIAN,H.VALAFAR,J.H.PRESTEGARD
JRNL TITL A DIPOLAR COUPLING BASED STRATEGY FOR SIMULTANEOUS RESONANCE
JRNL TITL 2 ASSIGNMENT AND STRUCTURE DETERMINATION OF PROTEIN BACKBONES
JRNL REF J.AM.CHEM.SOC. V. 123 11791 2001
JRNL REFN ISSN 0002-7863
JRNL PMID 11716736
JRNL DOI 10.1021/JA011806H
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REDCRAFT 1.0, XPLOR-NIH 2.9.1
REMARK 3 AUTHORS : VALAFAR, H. & PRESTEGARD, J.H. (REDCRAFT),
REMARK 3 SCHWIETERS, C.D., KUSZEWSKI, J.J., TJANDRA, N. &
REMARK 3 CLORE, G.M. (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RDCS WERE USED IN THE INITIAL ASSEMBLY
REMARK 3 OF 6 FRAGMENTS. RDCS FROM TWO MEDIA WERE USED TO SET RELATIVE
REMARK 3 ORIENTATION OF FRAGMENTS. TRANSLATIONAL RELATIONSHIPS OF
REMARK 3 FRAGMENTS WERE DICTATED BY SEQUENCE CONNECTIVITIES. THE
REMARK 3 ASSEMBLED STRUCTURE WAS MINIMIZED USING A MOLECULAR FORCE FIELD
REMARK 3 AND RDC ERROR FUNCTION. ALL SIDECHAIN ATOMS BEYOND CB ARE
REMARK 3 MISSING.
REMARK 4
REMARK 4 1RWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000021090.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 6.3; 6.3
REMARK 210 IONIC STRENGTH : 100 MM NACL; 50 MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 4.5 MM RUBREDOXIN U-15N; 50 MM
REMARK 210 NA PHOSPHATE; 100 MM NACL; PH
REMARK 210 6.3; 2.5 MM RUBREDOXIN U-15N; 50
REMARK 210 MM NA PHOSPHATE ; 50 MM NACL; PH
REMARK 210 6.3; 7% BICELLE (3:1 DMPC:DHPC
REMARK 210 WITH 4% CTAB RELATIVE TO DMPC);
REMARK 210 4.5 MM RUBREDOXIN U-15N; 50 MM
REMARK 210 NA PHOSPHATE; 100 MM NACL; PH
REMARK 210 6.3; PF1 PHAGE SAMPLE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SOFT HNCA-E.COSY; MODIFIED HNCO;
REMARK 210 PHASE-MODULATED HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : REDCAT 1.0
REMARK 210 METHOD USED : RDC DIRECTED FRAGMENT ASSEMBLY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 STRUCTURE WAS DETERMINED USING RESIDUAL DIPOLAR COUPLINGS FROM
REMARK 210 BACKBONE ATOM
REMARK 210 PAIRS; MODELED AS AN ALA-GLY POLYPEPTIDE
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 51
REMARK 465 GLU A 52
REMARK 465 ASP A 53
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 LYS A 28 C PHE A 29 N -0.139
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 ILE A 7 -66.33 -98.20
REMARK 500 TYR A 10 144.14 -25.69
REMARK 500 TYR A 12 34.07 -75.80
REMARK 500 ASP A 13 97.93 -35.01
REMARK 500 ASP A 18 71.82 -158.04
REMARK 500 GLU A 30 12.30 -68.59
REMARK 500 ILE A 40 -74.65 -89.70
REMARK 500 GLU A 47 38.36 -70.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M2Y RELATED DB: PDB
REMARK 900 SAME PROTEIN, STRUCTURE WAS CALCULATED WITH AN INTERACTIVE, AS
REMARK 900 OPPOSED TO AUTOMATED, RESIDUE ASSEMBLY PROCEDURE. SUBSEQUENT
REMARK 900 REFINEMENT BY MINIMIZATION USED AN INCOMPLETE RESTRAINT SET.
REMARK 900 RELATED ID: PFU-1210573-001 RELATED DB: TARGETDB
DBREF 1RWD A 1 53 UNP P24297 RUBR_PYRFU 1 53
SEQADV 1RWD TYR A 3 UNP P24297 TRP 3 ENGINEERED MUTATION
SEQADV 1RWD VAL A 23 UNP P24297 ILE 23 ENGINEERED MUTATION
SEQADV 1RWD ILE A 32 UNP P24297 LEU 32 ENGINEERED MUTATION
SEQRES 1 A 53 ALA LYS TYR VAL CYS LYS ILE CYS GLY TYR ILE TYR ASP
SEQRES 2 A 53 GLU ASP ALA GLY ASP PRO ASP ASN GLY VAL SER PRO GLY
SEQRES 3 A 53 THR LYS PHE GLU GLU ILE PRO ASP ASP TRP VAL CYS PRO
SEQRES 4 A 53 ILE CYS GLY ALA PRO LYS SER GLU PHE GLU LYS LEU GLU
SEQRES 5 A 53 ASP
HELIX 1 1 ASP A 18 GLY A 22 5 5
HELIX 2 2 LYS A 28 ILE A 32 5 5
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
Complete list - 27 202 Bytes