Header list of 1jq4.pdb file
Complete list - b 23 2 Bytes
HEADER OXIDOREDUCTASE 03-AUG-01 1JQ4
TITLE [2FE-2S] DOMAIN OF METHANE MONOOXYGENASE REDUCTASE FROM METHYLOCOCCUS
TITLE 2 CAPSULATUS (BATH)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHANE MONOOXYGENASE COMPONENT C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: METHANE MONOOXYGENASE REDUCTASE;
COMPND 6 EC: 1.14.13.25;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHYLOCOCCUS CAPSULATUS STR. BATH;
SOURCE 3 ORGANISM_TAXID: 243233;
SOURCE 4 STRAIN: BATH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRED-FD
KEYWDS [2FE-2S] FERREDOXIN, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.MUELLER,A.A.LUGOVSKOY,G.WAGNER,S.J.LIPPARD
REVDAT 4 23-FEB-22 1JQ4 1 REMARK LINK
REVDAT 3 24-FEB-09 1JQ4 1 VERSN
REVDAT 2 01-APR-03 1JQ4 1 JRNL
REVDAT 1 09-JAN-02 1JQ4 0
JRNL AUTH J.MULLER,A.A.LUGOVSKOY,G.WAGNER,S.J.LIPPARD
JRNL TITL NMR STRUCTURE OF THE [2FE-2S] FERREDOXIN DOMAIN FROM SOLUBLE
JRNL TITL 2 METHANE MONOOXYGENASE REDUCTASE AND INTERACTION WITH ITS
JRNL TITL 3 HYDROXYLASE.
JRNL REF BIOCHEMISTRY V. 41 42 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11772001
JRNL DOI 10.1021/BI015668K
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97.0, X-PLOR 3.84
REMARK 3 AUTHORS : MSI (FELIX), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HIGH-RESOLUTION NMR
REMARK 4
REMARK 4 1JQ4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014056.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50 MM NA PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM PROTEIN; 50 MM NA
REMARK 210 PHOSPHATE PH 7.0; 1 MM DTT; 1.5
REMARK 210 MM NA DITHIONITE; 0.1 % NAN3;
REMARK 210 PROTEASE INHIBITOR
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : A STANDARD SET OF NMR
REMARK 210 EXPERIMENTS REQUIRED FOR HIGH
REMARK 210 RESOLUTION STRUCTURE
REMARK 210 DETERMINATION; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 400 MHZ; 750
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, XEASY 1.3.9, VNMR
REMARK 210 5.1A, XWINNMR 2.5
REMARK 210 METHOD USED : NMR
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
REMARK 210
REMARK 210 REMARK: NULL
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
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 23 -76.68 59.40
REMARK 500 1 ASP A 26 100.14 27.88
REMARK 500 1 ASN A 35 -29.38 172.74
REMARK 500 1 SER A 40 -89.08 -57.51
REMARK 500 1 SER A 41 -96.04 -164.97
REMARK 500 1 CYS A 50 57.81 -68.09
REMARK 500 1 GLU A 72 -71.42 -68.08
REMARK 500 1 LEU A 78 -153.75 -170.51
REMARK 500 1 ARG A 83 -61.37 -102.58
REMARK 500 1 THR A 84 95.94 54.48
REMARK 500 1 THR A 97 -39.96 -162.14
REMARK 500 2 SER A 23 -74.93 61.43
REMARK 500 2 ASP A 26 106.03 34.55
REMARK 500 2 ASN A 35 -30.77 174.11
REMARK 500 2 MET A 39 23.71 -169.83
REMARK 500 2 SER A 40 -90.96 48.94
REMARK 500 2 SER A 41 -81.94 -163.59
REMARK 500 2 CYS A 50 56.01 -68.97
REMARK 500 2 GLU A 72 -70.98 -68.22
REMARK 500 2 LEU A 78 -157.08 -167.54
REMARK 500 2 ARG A 83 -42.46 -160.48
REMARK 500 2 THR A 84 173.55 46.69
REMARK 500 2 THR A 97 26.35 -159.53
REMARK 500 3 SER A 23 -71.05 62.32
REMARK 500 3 GLU A 25 31.84 -90.93
REMARK 500 3 ASN A 35 -28.55 170.09
REMARK 500 3 PHE A 37 87.64 -150.49
REMARK 500 3 SER A 40 -146.88 -64.54
REMARK 500 3 SER A 41 -42.41 -142.94
REMARK 500 3 CYS A 50 56.90 -69.90
REMARK 500 3 GLU A 72 -70.81 -67.99
REMARK 500 3 LEU A 78 -150.99 -166.97
REMARK 500 3 THR A 84 106.11 70.41
REMARK 500 3 PRO A 86 43.31 -75.45
REMARK 500 3 THR A 97 -40.78 -158.55
REMARK 500 4 SER A 23 -74.33 61.21
REMARK 500 4 ASN A 35 -26.32 167.26
REMARK 500 4 PHE A 37 82.34 -162.00
REMARK 500 4 MET A 39 30.10 -171.58
REMARK 500 4 SER A 40 -94.86 44.41
REMARK 500 4 SER A 41 -73.51 -164.20
REMARK 500 4 ALA A 48 -3.96 72.79
REMARK 500 4 GLU A 72 -70.83 -68.27
REMARK 500 4 LEU A 78 -153.13 -164.01
REMARK 500 4 ARG A 83 -61.30 -155.29
REMARK 500 4 THR A 84 174.00 47.08
REMARK 500 4 PRO A 86 38.67 -86.28
REMARK 500 4 THR A 97 -44.30 -160.44
REMARK 500 5 SER A 23 -75.70 59.44
REMARK 500 5 ASN A 35 -27.40 171.94
REMARK 500
REMARK 500 THIS ENTRY HAS 127 RAMACHANDRAN OUTLIERS.
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 3 0.31 SIDE CHAIN
REMARK 500 1 ARG A 18 0.26 SIDE CHAIN
REMARK 500 1 ARG A 22 0.25 SIDE CHAIN
REMARK 500 1 ARG A 33 0.29 SIDE CHAIN
REMARK 500 1 ARG A 43 0.30 SIDE CHAIN
REMARK 500 1 ARG A 83 0.31 SIDE CHAIN
REMARK 500 2 ARG A 3 0.28 SIDE CHAIN
REMARK 500 2 ARG A 18 0.31 SIDE CHAIN
REMARK 500 2 ARG A 22 0.30 SIDE CHAIN
REMARK 500 2 ARG A 33 0.26 SIDE CHAIN
REMARK 500 2 ARG A 43 0.27 SIDE CHAIN
REMARK 500 2 ARG A 83 0.22 SIDE CHAIN
REMARK 500 3 ARG A 3 0.30 SIDE CHAIN
REMARK 500 3 ARG A 18 0.29 SIDE CHAIN
REMARK 500 3 ARG A 22 0.29 SIDE CHAIN
REMARK 500 3 ARG A 33 0.27 SIDE CHAIN
REMARK 500 3 ARG A 43 0.23 SIDE CHAIN
REMARK 500 3 ARG A 83 0.31 SIDE CHAIN
REMARK 500 4 ARG A 3 0.32 SIDE CHAIN
REMARK 500 4 ARG A 18 0.31 SIDE CHAIN
REMARK 500 4 ARG A 22 0.31 SIDE CHAIN
REMARK 500 4 ARG A 33 0.30 SIDE CHAIN
REMARK 500 4 ARG A 43 0.28 SIDE CHAIN
REMARK 500 4 ARG A 83 0.27 SIDE CHAIN
REMARK 500 5 ARG A 3 0.27 SIDE CHAIN
REMARK 500 5 ARG A 18 0.30 SIDE CHAIN
REMARK 500 5 ARG A 22 0.26 SIDE CHAIN
REMARK 500 5 ARG A 33 0.32 SIDE CHAIN
REMARK 500 5 ARG A 43 0.32 SIDE CHAIN
REMARK 500 5 ARG A 83 0.32 SIDE CHAIN
REMARK 500 6 ARG A 3 0.26 SIDE CHAIN
REMARK 500 6 ARG A 18 0.31 SIDE CHAIN
REMARK 500 6 ARG A 22 0.29 SIDE CHAIN
REMARK 500 6 ARG A 33 0.29 SIDE CHAIN
REMARK 500 6 ARG A 43 0.31 SIDE CHAIN
REMARK 500 6 ARG A 83 0.29 SIDE CHAIN
REMARK 500 7 ARG A 3 0.29 SIDE CHAIN
REMARK 500 7 ARG A 18 0.25 SIDE CHAIN
REMARK 500 7 ARG A 22 0.31 SIDE CHAIN
REMARK 500 7 ARG A 33 0.23 SIDE CHAIN
REMARK 500 7 ARG A 43 0.31 SIDE CHAIN
REMARK 500 7 ARG A 83 0.27 SIDE CHAIN
REMARK 500 8 ARG A 3 0.30 SIDE CHAIN
REMARK 500 8 ARG A 18 0.30 SIDE CHAIN
REMARK 500 8 ARG A 22 0.29 SIDE CHAIN
REMARK 500 8 ARG A 33 0.31 SIDE CHAIN
REMARK 500 8 ARG A 43 0.32 SIDE CHAIN
REMARK 500 8 ARG A 83 0.31 SIDE CHAIN
REMARK 500 9 ARG A 3 0.32 SIDE CHAIN
REMARK 500 9 ARG A 18 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS.
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 FES A 99 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 42 SG
REMARK 620 2 FES A 99 S1 110.9
REMARK 620 3 FES A 99 S2 121.2 105.8
REMARK 620 4 CYS A 47 SG 95.4 110.8 112.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 99 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 50 SG
REMARK 620 2 FES A 99 S1 94.7
REMARK 620 3 FES A 99 S2 115.5 105.8
REMARK 620 4 CYS A 82 SG 117.1 109.8 111.8
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 FES A 99
DBREF 1JQ4 A 1 98 UNP P22868 MMOC_METCA 1 98
SEQRES 1 A 98 MET GLN ARG VAL HIS THR ILE THR ALA VAL THR GLU ASP
SEQRES 2 A 98 GLY GLU SER LEU ARG PHE GLU CYS ARG SER ASP GLU ASP
SEQRES 3 A 98 VAL ILE THR ALA ALA LEU ARG GLN ASN ILE PHE LEU MET
SEQRES 4 A 98 SER SER CYS ARG GLU GLY GLY CYS ALA THR CYS LYS ALA
SEQRES 5 A 98 LEU CYS SER GLU GLY ASP TYR ASP LEU LYS GLY CYS SER
SEQRES 6 A 98 VAL GLN ALA LEU PRO PRO GLU GLU GLU GLU GLU GLY LEU
SEQRES 7 A 98 VAL LEU LEU CYS ARG THR TYR PRO LYS THR ASP LEU GLU
SEQRES 8 A 98 ILE GLU LEU PRO TYR THR HIS
HET FES A 99 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
HELIX 1 1 VAL A 27 GLN A 34 1 8
HELIX 2 2 VAL A 66 LEU A 69 1 4
HELIX 3 3 PRO A 71 GLY A 77 1 7
SHEET 1 A 4 GLU A 15 ARG A 22 0
SHEET 2 A 4 VAL A 4 THR A 11 -1 N ALA A 9 O LEU A 17
SHEET 3 A 4 GLU A 91 GLU A 93 1 N ILE A 92 O THR A 8
SHEET 4 A 4 CYS A 54 GLU A 56 -1 N GLU A 56 O GLU A 91
SHEET 1 B 2 LYS A 51 ALA A 52 0
SHEET 2 B 2 VAL A 79 LEU A 80 -1 N VAL A 79 O ALA A 52
LINK SG CYS A 42 FE1 FES A 99 1555 1555 2.22
LINK SG CYS A 47 FE1 FES A 99 1555 1555 2.29
LINK SG CYS A 50 FE2 FES A 99 1555 1555 2.36
LINK SG CYS A 82 FE2 FES A 99 1555 1555 2.29
SITE 1 AC1 7 SER A 41 CYS A 42 GLY A 45 GLY A 46
SITE 2 AC1 7 CYS A 47 CYS A 50 CYS A 82
CRYST1 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