Header list of 1sr3.pdb file
Complete list - r 2 2 Bytes
HEADER CHAPERONE 22-MAR-04 1SR3
TITLE SOLUTION STRUCTURE OF THE HEME CHAPERONE CCME OF ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APO-CCME;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE APO-CCME-H6(C-TERMINAL DOMAIN);
COMPND 5 SYNONYM: CYTOCHROME C-TYPE BIOGENESIS PROTEIN CCME;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 CELLULAR_LOCATION: PERIPLASM;
SOURCE 5 GENE: CCME;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: EC06;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEC415
KEYWDS OB FOLD, BETA BARREL, FLEXIBLE C-TERMINAL DOMAIN, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.ENGGIST,L.THONY-MEYER,P.GUNTERT,K.PERVUSHIN
REVDAT 3 02-MAR-22 1SR3 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1SR3 1 VERSN
REVDAT 1 06-APR-04 1SR3 0
SPRSDE 06-APR-04 1SR3 1LIZ
JRNL AUTH E.ENGGIST,L.THONY-MEYER,P.GUNTERT,K.PERVUSHIN
JRNL TITL NMR STRUCTURE OF THE HEME CHAPERONE CCME REVEALS A NOVEL
JRNL TITL 2 FUNCTIONAL MOTIF
JRNL REF STRUCTURE V. 10 1551 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 12429096
JRNL DOI 10.1016/S0969-2126(02)00885-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT, P. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SR3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021939.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1MM APO-CCME-H6 U-98% 13C; U
REMARK 210 -98% 15N; 50MM PHOSPHATE BUFFER,
REMARK 210 PH 7.2, 300MM NACL, 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 2D_TROSY; 3D_
REMARK 210 TROSY_HNCA; 3D_TROSY_HNCACB;
REMARK 210 CBCA(CO)NH; HCCH-TOCSA; 15N_
REMARK 210 EDITED_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, PROSA, CANDID
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 GLU A 144
REMARK 465 ALA A 145
REMARK 465 ASN A 146
REMARK 465 HIS A 147
REMARK 465 ARG A 148
REMARK 465 ARG A 149
REMARK 465 PRO A 150
REMARK 465 ALA A 151
REMARK 465 SER A 152
REMARK 465 VAL A 153
REMARK 465 TYR A 154
REMARK 465 LYS A 155
REMARK 465 ASP A 156
REMARK 465 PRO A 157
REMARK 465 ALA A 158
REMARK 465 SER A 159
REMARK 465 HIS A 160
REMARK 465 HIS A 161
REMARK 465 HIS A 162
REMARK 465 HIS A 163
REMARK 465 HIS A 164
REMARK 465 HIS A 165
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 1 VAL A 62 CA - CB - CG1 ANGL. DEV. = 16.7 DEGREES
REMARK 500 4 ARG A 61 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 7 VAL A 62 CA - CB - CG1 ANGL. DEV. = 17.6 DEGREES
REMARK 500 9 VAL A 62 CA - CB - CG1 ANGL. DEV. = 12.7 DEGREES
REMARK 500 9 VAL A 110 CA - CB - CG1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 11 LEU A 44 CB - CG - CD1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 14 VAL A 111 CA - CB - CG2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 15 LEU A 44 CB - CG - CD1 ANGL. DEV. = 10.8 DEGREES
REMARK 500 16 LEU A 44 CB - CG - CD2 ANGL. DEV. = 10.7 DEGREES
REMARK 500 19 VAL A 109 CA - CB - CG1 ANGL. DEV. = 11.9 DEGREES
REMARK 500 20 VAL A 66 CA - CB - CG1 ANGL. DEV. = 11.7 DEGREES
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 32 161.67 139.97
REMARK 500 1 ASN A 33 177.66 61.81
REMARK 500 1 ASP A 35 -161.73 52.36
REMARK 500 1 ARG A 48 -19.74 -19.05
REMARK 500 1 GLU A 49 -75.09 -121.36
REMARK 500 1 THR A 50 31.07 -164.94
REMARK 500 1 GLN A 52 175.97 176.23
REMARK 500 1 VAL A 71 94.31 -61.73
REMARK 500 1 ALA A 87 6.65 -61.34
REMARK 500 1 LYS A 117 -72.34 -150.84
REMARK 500 1 GLU A 125 -45.72 -146.05
REMARK 500 1 VAL A 126 133.70 58.97
REMARK 500 1 HIS A 130 41.61 -71.64
REMARK 500 1 ASP A 131 -65.82 67.69
REMARK 500 1 GLU A 132 154.19 65.47
REMARK 500 1 ASN A 133 -50.17 -147.10
REMARK 500 1 TYR A 134 109.26 66.63
REMARK 500 1 VAL A 139 -53.33 -165.20
REMARK 500 1 LYS A 141 20.79 -148.89
REMARK 500 2 ASN A 33 -56.47 -145.54
REMARK 500 2 ASP A 35 151.66 -37.23
REMARK 500 2 ARG A 48 -16.00 -42.70
REMARK 500 2 GLU A 49 -63.02 -122.67
REMARK 500 2 THR A 50 21.56 -170.07
REMARK 500 2 GLN A 52 168.63 173.82
REMARK 500 2 VAL A 71 105.78 -59.68
REMARK 500 2 ARG A 73 129.25 42.67
REMARK 500 2 GLU A 88 -80.84 -112.84
REMARK 500 2 LEU A 99 151.87 67.13
REMARK 500 2 GLU A 116 -64.09 -103.44
REMARK 500 2 LYS A 117 158.41 167.05
REMARK 500 2 GLU A 125 -41.48 -139.61
REMARK 500 2 VAL A 126 127.71 59.28
REMARK 500 2 HIS A 130 -91.90 -76.78
REMARK 500 2 ASP A 131 45.39 -162.81
REMARK 500 3 ARG A 31 -42.73 -149.98
REMARK 500 3 SER A 32 -65.41 65.75
REMARK 500 3 ASN A 33 135.31 61.72
REMARK 500 3 ILE A 34 165.72 61.11
REMARK 500 3 ARG A 48 -77.27 -18.18
REMARK 500 3 GLU A 49 -87.27 -66.40
REMARK 500 3 THR A 50 36.92 -174.38
REMARK 500 3 GLN A 52 -173.31 -174.42
REMARK 500 3 VAL A 71 104.45 -57.89
REMARK 500 3 ARG A 73 165.34 54.20
REMARK 500 3 GLU A 88 -71.33 -103.12
REMARK 500 3 LEU A 99 149.84 89.43
REMARK 500 3 GLU A 116 -72.34 -93.39
REMARK 500 3 LYS A 117 -86.07 -141.86
REMARK 500 3 GLU A 125 -38.31 -144.41
REMARK 500
REMARK 500 THIS ENTRY HAS 371 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 47 ARG A 48 1 -135.21
REMARK 500 ALA A 142 MET A 143 1 147.88
REMARK 500 VAL A 62 GLY A 63 2 148.84
REMARK 500 LYS A 47 ARG A 48 4 -143.80
REMARK 500 LYS A 47 ARG A 48 7 -142.91
REMARK 500 LYS A 47 ARG A 48 8 -136.63
REMARK 500 GLY A 106 GLN A 107 9 145.20
REMARK 500 ARG A 48 GLU A 49 10 146.41
REMARK 500 ARG A 48 GLU A 49 11 148.90
REMARK 500 ALA A 142 MET A 143 13 145.34
REMARK 500 SER A 32 ASN A 33 16 142.45
REMARK 500 ALA A 142 MET A 143 17 148.78
REMARK 500 ASP A 35 LEU A 36 18 148.20
REMARK 500 LYS A 47 ARG A 48 18 -142.46
REMARK 500 THR A 50 GLN A 51 19 -147.51
REMARK 500 LYS A 47 ARG A 48 20 -138.51
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 61 0.08 SIDE CHAIN
REMARK 500 2 ARG A 48 0.08 SIDE CHAIN
REMARK 500 3 ARG A 59 0.08 SIDE CHAIN
REMARK 500 3 ARG A 104 0.08 SIDE CHAIN
REMARK 500 6 ARG A 61 0.08 SIDE CHAIN
REMARK 500 7 ARG A 31 0.08 SIDE CHAIN
REMARK 500 7 TYR A 38 0.08 SIDE CHAIN
REMARK 500 7 ARG A 59 0.10 SIDE CHAIN
REMARK 500 7 ARG A 73 0.16 SIDE CHAIN
REMARK 500 7 ARG A 104 0.08 SIDE CHAIN
REMARK 500 8 TYR A 85 0.06 SIDE CHAIN
REMARK 500 8 ARG A 104 0.10 SIDE CHAIN
REMARK 500 9 TYR A 38 0.09 SIDE CHAIN
REMARK 500 9 ARG A 104 0.07 SIDE CHAIN
REMARK 500 10 ARG A 31 0.09 SIDE CHAIN
REMARK 500 11 ARG A 73 0.10 SIDE CHAIN
REMARK 500 14 TYR A 95 0.08 SIDE CHAIN
REMARK 500 15 ARG A 59 0.09 SIDE CHAIN
REMARK 500 15 ARG A 104 0.10 SIDE CHAIN
REMARK 500 16 TYR A 85 0.08 SIDE CHAIN
REMARK 500 17 TYR A 38 0.07 SIDE CHAIN
REMARK 500 17 ARG A 61 0.11 SIDE CHAIN
REMARK 500 18 ARG A 48 0.08 SIDE CHAIN
REMARK 500 18 ARG A 61 0.08 SIDE CHAIN
REMARK 500 18 TYR A 85 0.07 SIDE CHAIN
REMARK 500 19 ARG A 31 0.11 SIDE CHAIN
REMARK 500 19 TYR A 45 0.07 SIDE CHAIN
REMARK 500 19 TYR A 134 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5526 RELATED DB: BMRB
REMARK 900 5526 IS CHEMICAL SHIFT OF THE SAME PROTEIN
DBREF 1SR3 A 30 159 UNP P69490 CCME_ECOLI 30 159
SEQADV 1SR3 HIS A 160 UNP P69490 INSERTION
SEQADV 1SR3 HIS A 161 UNP P69490 INSERTION
SEQADV 1SR3 HIS A 162 UNP P69490 INSERTION
SEQADV 1SR3 HIS A 163 UNP P69490 INSERTION
SEQADV 1SR3 HIS A 164 UNP P69490 INSERTION
SEQADV 1SR3 HIS A 165 UNP P69490 INSERTION
SEQRES 1 A 136 LEU ARG SER ASN ILE ASP LEU PHE TYR THR PRO GLY GLU
SEQRES 2 A 136 ILE LEU TYR GLY LYS ARG GLU THR GLN GLN MET PRO GLU
SEQRES 3 A 136 VAL GLY GLN ARG LEU ARG VAL GLY GLY MET VAL MET PRO
SEQRES 4 A 136 GLY SER VAL GLN ARG ASP PRO ASN SER LEU LYS VAL THR
SEQRES 5 A 136 PHE THR ILE TYR ASP ALA GLU GLY SER VAL ASP VAL SER
SEQRES 6 A 136 TYR GLU GLY ILE LEU PRO ASP LEU PHE ARG GLU GLY GLN
SEQRES 7 A 136 GLY VAL VAL VAL GLN GLY GLU LEU GLU LYS GLY ASN HIS
SEQRES 8 A 136 ILE LEU ALA LYS GLU VAL LEU ALA LYS HIS ASP GLU ASN
SEQRES 9 A 136 TYR THR PRO PRO GLU VAL GLU LYS ALA MET GLU ALA ASN
SEQRES 10 A 136 HIS ARG ARG PRO ALA SER VAL TYR LYS ASP PRO ALA SER
SEQRES 11 A 136 HIS HIS HIS HIS HIS HIS
HELIX 1 1 PRO A 136 LYS A 141 1 6
SHEET 1 A 7 GLN A 72 ARG A 73 0
SHEET 2 A 7 LYS A 79 TYR A 85 -1 O THR A 81 N GLN A 72
SHEET 3 A 7 SER A 90 GLU A 96 -1 O TYR A 95 N VAL A 80
SHEET 4 A 7 HIS A 120 ALA A 123 1 O ALA A 123 N SER A 94
SHEET 5 A 7 GLY A 108 LEU A 115 -1 N GLU A 114 O LEU A 122
SHEET 6 A 7 ARG A 59 VAL A 66 -1 N LEU A 60 O GLY A 113
SHEET 7 A 7 LYS A 79 TYR A 85 -1 O TYR A 85 N MET A 65
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