Header list of 1s24.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 08-JAN-04 1S24
TITLE RUBREDOXIN DOMAIN II FROM PSEUDOMONAS OLEOVORANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUBREDOXIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RUBREDOXIN C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: TWO-IRON RUBREDOXIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS OLEOVORANS;
SOURCE 3 ORGANISM_TAXID: 301;
SOURCE 4 GENE: ALKG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RUBREDOXIN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.PERRY,W.TAMBYRAJAH,J.G.GROSSMANN,L.Y.LIAN,N.S.SCRUTTON
REVDAT 3 02-MAR-22 1S24 1 REMARK LINK
REVDAT 2 24-FEB-09 1S24 1 VERSN
REVDAT 1 04-MAY-04 1S24 0
JRNL AUTH A.PERRY,W.TAMBYRAJAH,J.G.GROSSMANN,L.Y.LIAN,N.S.SCRUTTON
JRNL TITL SOLUTION STRUCTURE OF THE TWO-IRON RUBREDOXIN OF PSEUDOMONAS
JRNL TITL 2 OLEOVORANS DETERMINED BY NMR SPECTROSCOPY AND SOLUTION X-RAY
JRNL TITL 3 SCATTERING AND INTERACTIONS WITH RUBREDOXIN REDUCTASE.
JRNL REF BIOCHEMISTRY V. 43 3167 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15023067
JRNL DOI 10.1021/BI035817U
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), NILGES (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S24 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021270.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 310; 298; 310
REMARK 210 PH : 6.0; 6.0; 7.6; 7.6
REMARK 210 IONIC STRENGTH : 40MM; 40MM; 40MM; 40MM
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 10MM RUBREDOXIN C-TERMINAL
REMARK 210 DOMAIN; 20 MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER, 10MM CD(II)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.0, CNS 1.0
REMARK 210 METHOD USED : ARIA PROTOCOL WAS USED TO DEAL
REMARK 210 WITH AMBIGUOUS DISTANCE
REMARK 210 RESTRAINTS AND SOME NOE
REMARK 210 ASSIGNMENT. SIMULATING ANNEALING
REMARK 210 WAS USED.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 20 STRUCTURES WITH THE
REMARK 210 LOWEST
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 PRO A -30
REMARK 465 THR A -29
REMARK 465 SER A -28
REMARK 465 LEU A -27
REMARK 465 GLU A -26
REMARK 465 LYS A -25
REMARK 465 LEU A -24
REMARK 465 PRO A -23
REMARK 465 SER A -22
REMARK 465 ALA A -21
REMARK 465 ASP A -20
REMARK 465 VAL A -19
REMARK 465 LYS A -18
REMARK 465 GLY A -17
REMARK 465 GLN A -16
REMARK 465 ASP A -15
REMARK 465 LEU A -14
REMARK 465 TYR A -13
REMARK 465 LYS A -12
REMARK 465 THR A -11
REMARK 465 GLN A -10
REMARK 465 PRO A -9
REMARK 465 PRO A -8
REMARK 465 ARG A -7
REMARK 465 SER A -6
REMARK 465 ASP A -5
REMARK 465 ALA A -4
REMARK 465 GLN A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 LYS A 0
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
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 LEU A 18 62.30 -176.68
REMARK 500 1 THR A 26 150.89 -49.33
REMARK 500 1 PRO A 27 95.77 -62.45
REMARK 500 1 PRO A 35 -163.42 -62.12
REMARK 500 1 CYS A 43 -75.15 -111.32
REMARK 500 1 THR A 46 -167.45 -78.49
REMARK 500 1 GLU A 54 172.79 54.23
REMARK 500 2 LEU A 18 69.59 -176.96
REMARK 500 2 PHE A 25 83.81 -66.72
REMARK 500 2 THR A 26 152.54 -49.77
REMARK 500 2 PRO A 27 106.99 -58.04
REMARK 500 2 ILE A 34 109.82 -58.68
REMARK 500 2 PRO A 35 -161.51 -62.02
REMARK 500 2 CYS A 39 -160.89 -173.94
REMARK 500 2 CYS A 43 -70.34 -92.40
REMARK 500 2 THR A 46 -162.24 -67.42
REMARK 500 3 LEU A 18 65.05 -176.49
REMARK 500 3 THR A 26 151.29 -49.46
REMARK 500 3 PRO A 35 -155.77 -58.83
REMARK 500 3 CYS A 39 -164.58 -128.96
REMARK 500 3 ASP A 42 40.69 -157.49
REMARK 500 3 CYS A 43 -59.51 -141.88
REMARK 500 3 GLU A 54 72.08 -165.01
REMARK 500 4 CYS A 7 96.93 -67.67
REMARK 500 4 LEU A 18 68.45 -175.55
REMARK 500 4 PRO A 27 106.57 -56.15
REMARK 500 4 PRO A 35 -169.72 -69.52
REMARK 500 4 CYS A 39 -160.53 -162.36
REMARK 500 4 CYS A 43 -46.15 -141.57
REMARK 500 4 THR A 46 -159.85 -109.25
REMARK 500 5 CYS A 7 92.20 -63.93
REMARK 500 5 LEU A 18 64.39 -176.57
REMARK 500 5 PRO A 35 94.91 -46.94
REMARK 500 5 ASP A 36 -46.32 -175.48
REMARK 500 5 ASP A 37 32.60 -171.58
REMARK 500 5 CYS A 39 -161.34 -169.66
REMARK 500 5 ASP A 42 50.76 -148.10
REMARK 500 5 CYS A 43 -45.63 -136.58
REMARK 500 5 GLU A 54 126.70 -172.84
REMARK 500 5 GLU A 55 52.66 -151.56
REMARK 500 6 LEU A 18 68.48 -173.42
REMARK 500 6 PRO A 27 95.51 -54.54
REMARK 500 6 PRO A 35 -164.65 -61.82
REMARK 500 6 CYS A 43 -75.04 -111.86
REMARK 500 6 ALA A 45 -169.17 -113.66
REMARK 500 7 LEU A 18 69.34 -176.61
REMARK 500 7 THR A 26 151.40 -47.86
REMARK 500 7 PRO A 27 104.92 -56.96
REMARK 500 7 PRO A 35 -150.60 -62.91
REMARK 500 7 CYS A 39 -160.89 -162.24
REMARK 500
REMARK 500 THIS ENTRY HAS 148 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 57 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 7 SG
REMARK 620 2 CYS A 10 SG 97.4
REMARK 620 3 CYS A 40 SG 90.9 116.5
REMARK 620 4 CYS A 43 SG 143.6 88.0 118.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 57
DBREF 1S24 A -30 56 UNP P00272 RUBR2_PSEOL 86 172
SEQRES 1 A 87 PRO THR SER LEU GLU LYS LEU PRO SER ALA ASP VAL LYS
SEQRES 2 A 87 GLY GLN ASP LEU TYR LYS THR GLN PRO PRO ARG SER ASP
SEQRES 3 A 87 ALA GLN GLY GLY LYS ALA TYR LEU LYS TRP ILE CYS ILE
SEQRES 4 A 87 THR CYS GLY HIS ILE TYR ASP GLU ALA LEU GLY ASP GLU
SEQRES 5 A 87 ALA GLU GLY PHE THR PRO GLY THR ARG PHE GLU ASP ILE
SEQRES 6 A 87 PRO ASP ASP TRP CYS CYS PRO ASP CYS GLY ALA THR LYS
SEQRES 7 A 87 GLU ASP TYR VAL LEU TYR GLU GLU LYS
HET CD A 57 1
HETNAM CD CADMIUM ION
FORMUL 2 CD CD 2+
HELIX 1 1 ARG A 30 ILE A 34 5 5
HELIX 2 2 THR A 46 GLU A 48 5 3
SHEET 1 A 3 ILE A 13 ASP A 15 0
SHEET 2 A 3 LYS A 4 CYS A 7 -1 N TRP A 5 O TYR A 14
SHEET 3 A 3 TYR A 50 LEU A 52 -1 O VAL A 51 N ILE A 6
LINK SG CYS A 7 CD CD A 57 1555 1555 2.57
LINK SG CYS A 10 CD CD A 57 1555 1555 2.49
LINK SG CYS A 40 CD CD A 57 1555 1555 2.57
LINK SG CYS A 43 CD CD A 57 1555 1555 2.58
SITE 1 AC1 4 CYS A 7 CYS A 10 CYS A 40 CYS A 43
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