HEADER OXIDOREDUCTASE 30-MAR-10 2KW0
TITLE SOLUTION STRUCTURE OF N-TERMINAL DOMAIN OF CCMH FROM ESCHERICHIA.COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CCMH PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 19-100;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 511693;
SOURCE 4 STRAIN: BL21;
SOURCE 5 GENE: B2194, B21_02080, CCMH, JW2182, YEJP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET22B
KEYWDS OXIDOREDUCTASE, CYTOCHROME C MATURATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.HONG,X.ZHENG,H.HU,D.LIN
REVDAT 3 26-FEB-20 2KW0 1 SEQADV
REVDAT 2 07-NOV-12 2KW0 1 JRNL
REVDAT 1 13-JUL-11 2KW0 0
JRNL AUTH X.M.ZHENG,J.HONG,H.Y.LI,D.H.LIN,H.Y.HU
JRNL TITL BIOCHEMICAL PROPERTIES AND CATALYTIC DOMAIN STRUCTURE OF THE
JRNL TITL 2 CCMH PROTEIN FROM ESCHERICHIA COLI.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1824 1394 2012
JRNL REFN ISSN 0006-3002
JRNL PMID 22789558
JRNL DOI 10.1016/J.BBAPAP.2012.06.017
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KW0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000101642.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN-1, 10 % D2O-2, 50
REMARK 210 MM SODIUM PHOSPHATE-3, 100 MM
REMARK 210 SODIUM CHLORIDE-4, 5 MM DTT-5,
REMARK 210 90% H2O/10% D2O; 1 MM PROTEIN-6,
REMARK 210 100 % D2O-7, 50 MM SODIUM
REMARK 210 PHOSPHATE-8, 100 MM SODIUM
REMARK 210 CHLORIDE-9, 5 MM DTT-10, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D CBCA(CO)NH;
REMARK 210 3D HNCACB; 3D HN(CO)CA; 3D HNCO;
REMARK 210 3D H(CCO)NH; 3D C(CO)NH; 3D 1H-
REMARK 210 15N NOESY; 3D HCCH-TOCSY; 3D 1H-
REMARK 210 13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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 : 1
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 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 MET A 18
REMARK 465 LEU A 100
REMARK 465 GLU A 101
REMARK 465 HIS A 102
REMARK 465 HIS A 103
REMARK 465 HIS A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
REMARK 465 HIS A 107
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 ILE A 20 -88.07 -89.92
REMARK 500 1 ASP A 21 -147.20 -152.41
REMARK 500 1 LEU A 23 80.83 -69.94
REMARK 500 1 ASP A 27 -161.00 -162.27
REMARK 500 1 GLN A 47 63.36 -108.80
REMARK 500 1 SER A 50 -132.68 51.84
REMARK 500 1 ALA A 52 -72.48 -70.42
REMARK 500 1 PRO A 96 -154.40 -76.03
REMARK 500 2 ILE A 20 -83.42 -141.49
REMARK 500 2 ASP A 27 -165.03 -163.16
REMARK 500 2 PRO A 44 72.58 -66.02
REMARK 500 2 PRO A 96 -164.49 -70.75
REMARK 500 3 ILE A 20 -42.00 175.79
REMARK 500 3 ASP A 21 -150.94 -161.81
REMARK 500 3 ASP A 27 -166.54 -172.22
REMARK 500 3 GLN A 47 46.80 -87.26
REMARK 500 3 ASN A 48 -39.64 -166.95
REMARK 500 3 ASN A 49 -75.87 72.83
REMARK 500 3 ASN A 55 -4.47 65.65
REMARK 500 4 ILE A 20 -41.87 -170.10
REMARK 500 4 ASP A 21 -148.79 -145.17
REMARK 500 4 PRO A 96 -79.80 -58.39
REMARK 500 5 PRO A 44 37.41 -70.35
REMARK 500 5 CYS A 46 -43.66 70.63
REMARK 500 5 ASN A 48 146.05 178.08
REMARK 500 5 SER A 50 -112.01 52.79
REMARK 500 5 ALA A 52 -70.72 -79.67
REMARK 500 5 PRO A 96 -168.34 -75.30
REMARK 500 6 ASP A 21 -154.54 -149.78
REMARK 500 6 ASP A 27 -165.32 -161.28
REMARK 500 6 PRO A 44 88.24 -61.34
REMARK 500 6 LYS A 45 117.56 -173.94
REMARK 500 6 GLN A 47 50.15 -97.98
REMARK 500 6 TYR A 87 31.35 -95.95
REMARK 500 7 ASP A 21 -148.19 -160.45
REMARK 500 7 CYS A 46 -57.19 70.01
REMARK 500 7 PRO A 96 -78.94 -51.14
REMARK 500 8 ASP A 21 -164.64 -70.85
REMARK 500 8 PRO A 44 46.09 -71.94
REMARK 500 8 CYS A 46 -60.46 69.95
REMARK 500 8 ASN A 48 90.27 -165.77
REMARK 500 8 SER A 50 144.89 70.55
REMARK 500 8 ASP A 53 55.68 -153.88
REMARK 500 8 PRO A 96 -158.31 -75.86
REMARK 500 9 ILE A 20 -39.19 172.63
REMARK 500 9 ASP A 21 -146.58 -151.72
REMARK 500 9 ASP A 27 -165.55 -170.79
REMARK 500 9 PRO A 44 15.61 -67.47
REMARK 500 9 CYS A 46 -69.39 70.17
REMARK 500 9 ASN A 48 -27.16 178.11
REMARK 500
REMARK 500 THIS ENTRY HAS 111 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 16802 RELATED DB: BMRB
DBREF 2KW0 A 19 99 UNP C5W6T4 C5W6T4_ECOBB 19 99
SEQADV 2KW0 MET A 18 UNP C5W6T4 INITIATING METHIONINE
SEQADV 2KW0 LEU A 100 UNP C5W6T4 EXPRESSION TAG
SEQADV 2KW0 GLU A 101 UNP C5W6T4 EXPRESSION TAG
SEQADV 2KW0 HIS A 102 UNP C5W6T4 EXPRESSION TAG
SEQADV 2KW0 HIS A 103 UNP C5W6T4 EXPRESSION TAG
SEQADV 2KW0 HIS A 104 UNP C5W6T4 EXPRESSION TAG
SEQADV 2KW0 HIS A 105 UNP C5W6T4 EXPRESSION TAG
SEQADV 2KW0 HIS A 106 UNP C5W6T4 EXPRESSION TAG
SEQADV 2KW0 HIS A 107 UNP C5W6T4 EXPRESSION TAG
SEQRES 1 A 90 MET THR ILE ASP VAL LEU GLN PHE LYS ASP GLU ALA GLN
SEQRES 2 A 90 GLU GLN GLN PHE ARG GLN LEU THR GLU GLU LEU ARG CYS
SEQRES 3 A 90 PRO LYS CYS GLN ASN ASN SER ILE ALA ASP SER ASN SER
SEQRES 4 A 90 MET ILE ALA THR ASP LEU ARG GLN LYS VAL TYR GLU LEU
SEQRES 5 A 90 MET GLN GLU GLY LYS SER LYS LYS GLU ILE VAL ASP TYR
SEQRES 6 A 90 MET VAL ALA ARG TYR GLY ASN PHE VAL THR TYR ASP PRO
SEQRES 7 A 90 PRO LEU THR PRO LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 ASP A 27 GLU A 40 1 14
HELIX 2 2 SER A 56 GLY A 73 1 18
HELIX 3 3 SER A 75 GLY A 88 1 14
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
(ATOM LINES ARE NOT SHOWN.)
END