Header list of 1r2u.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 29-SEP-03 1R2U
TITLE NMR STRUCTURE OF THE N DOMAIN OF TROUT CARDIAC TROPONIN C AT 30 C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ONCORHYNCHUS MYKISS;
SOURCE 3 ORGANISM_COMMON: RAINBOW TROUT;
SOURCE 4 ORGANISM_TAXID: 8022;
SOURCE 5 ORGAN: HEART;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS EF-HAND, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR T.M.BLUMENSCHEIN,T.E.GILLIS,G.F.TIBBITS,B.D.SYKES
REVDAT 3 02-MAR-22 1R2U 1 REMARK LINK
REVDAT 2 24-FEB-09 1R2U 1 VERSN
REVDAT 1 08-JUN-04 1R2U 0
JRNL AUTH T.M.BLUMENSCHEIN,T.E.GILLIS,G.F.TIBBITS,B.D.SYKES
JRNL TITL EFFECT OF TEMPERATURE ON THE STRUCTURE OF TROUT TROPONIN C
JRNL REF BIOCHEMISTRY V. 43 4955 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15109253
JRNL DOI 10.1021/BI035504Z
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.E.GILLIS,T.M.A.BLUMENSCHEIN,B.D.SYKES,G.F.TIBBITS
REMARK 1 TITL EFFECT OF TEMPERATURE AND THE F27W MUTATION ON THE CA2+
REMARK 1 TITL 2 ACTIVATED STRUCTURAL TRANSITION OF TROUT CARDIAC TROPONIN C
REMARK 1 REF BIOCHEMISTRY V. 42 6418 2003
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI0340494
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE APRIL 2001, X-PLOR 3.851
REMARK 3 AUTHORS : DELAGLIO, F., GRZESIEK, S., VUISTER, G.W., ZHU,
REMARK 3 G., PFEIFER, J., BAX, A. (NMRPIPE), BRUNGER, A.T.
REMARK 3 (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R2U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020367.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.34 MM N-DOMAIN OF TROUT
REMARK 210 CARDIAC TROPONIN C U-15N; 10 MM
REMARK 210 IMIDAZOL; 100 MM KCL; 0.03% NAN3;
REMARK 210 20 MM DTT; 0.2 MM DSS; ~4 MM
REMARK 210 CACL2; 1.34 MM N-DOMAIN OF TROUT
REMARK 210 CARDIAC TROPONIN C U-15N; 10 MM
REMARK 210 IMIDAZOL; 100 MM KCL; 0.03% NAN3;
REMARK 210 20 MM DTT; 0.2 MM DSS; ~4 MM
REMARK 210 CACL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N HSQC; DIPSI-HSQC; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB; 2D
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, NMRVIEW 5.0.4
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
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 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 O VAL A 79 H ARG A 83 1.60
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 28 38.08 -92.20
REMARK 500 1 ASP A 30 42.30 -151.58
REMARK 500 2 ILE A 28 34.35 -91.73
REMARK 500 2 ASP A 30 39.41 -149.18
REMARK 500 2 ASP A 65 90.87 -66.82
REMARK 500 3 ILE A 28 42.41 -92.91
REMARK 500 3 ASP A 30 31.43 -147.48
REMARK 500 4 ILE A 28 32.78 -92.86
REMARK 500 4 ASP A 30 41.73 -152.05
REMARK 500 4 ASP A 87 -63.42 -98.68
REMARK 500 5 ILE A 28 37.83 -93.92
REMARK 500 5 ASP A 30 34.39 -148.12
REMARK 500 5 ASN A 51 76.56 -153.89
REMARK 500 5 ASP A 65 89.41 -68.60
REMARK 500 5 LYS A 86 179.97 60.16
REMARK 500 6 ASN A 2 -79.92 -116.40
REMARK 500 6 ASP A 3 -45.44 178.20
REMARK 500 6 ILE A 28 38.77 -93.06
REMARK 500 6 ASP A 30 35.18 -146.09
REMARK 500 6 ASP A 65 88.32 -67.11
REMARK 500 6 LYS A 86 176.83 63.02
REMARK 500 7 ILE A 28 37.60 -93.17
REMARK 500 7 ASP A 30 44.16 -158.72
REMARK 500 8 ASN A 2 57.76 -112.87
REMARK 500 8 ILE A 28 37.13 -92.49
REMARK 500 8 ASP A 30 44.28 -153.81
REMARK 500 8 ASN A 51 86.78 -155.57
REMARK 500 8 MET A 85 52.42 -103.89
REMARK 500 9 ILE A 28 39.18 -92.44
REMARK 500 9 ASP A 30 32.51 -147.96
REMARK 500 9 ASN A 51 75.64 -151.42
REMARK 500 9 ASP A 65 89.94 -66.90
REMARK 500 10 ILE A 28 32.07 -93.68
REMARK 500 10 ASP A 30 42.28 -153.62
REMARK 500 10 ILE A 61 -70.16 -51.55
REMARK 500 11 ILE A 28 31.04 -95.14
REMARK 500 11 ASP A 30 43.22 -158.44
REMARK 500 11 ASN A 51 86.50 -152.97
REMARK 500 11 ASP A 87 -70.63 -78.43
REMARK 500 11 ASP A 88 51.74 -169.18
REMARK 500 12 ILE A 28 39.26 -93.32
REMARK 500 12 ASP A 30 39.50 -152.33
REMARK 500 12 ASN A 51 75.94 -154.52
REMARK 500 12 ILE A 61 -72.98 -55.94
REMARK 500 13 ASP A 30 40.13 -144.98
REMARK 500 13 ASP A 65 95.95 -63.47
REMARK 500 13 MET A 85 -74.36 -58.72
REMARK 500 13 LYS A 86 -81.41 60.04
REMARK 500 13 ASP A 87 85.28 65.09
REMARK 500 14 ASN A 2 79.04 58.02
REMARK 500
REMARK 500 THIS ENTRY HAS 177 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 CA A 90 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 65 OD1
REMARK 620 2 ASP A 67 OD2 82.5
REMARK 620 3 ASP A 67 OD1 73.8 40.6
REMARK 620 4 SER A 69 OG 112.3 99.7 67.7
REMARK 620 5 THR A 71 O 121.4 133.5 164.7 105.0
REMARK 620 6 GLU A 76 OE1 62.3 70.9 101.5 169.3 85.5
REMARK 620 7 GLU A 76 OE2 103.7 58.6 99.0 134.9 76.3 44.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 90
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8467 RELATED DB: BMRB
REMARK 900 RESSONACE ASSIGNMENTS FOR THE N DOMAIN OF TROUT CARDIAC TROPONIN C
REMARK 900 AT 30 C
DBREF 1R2U A 1 89 UNP Q7ZZB9 Q7ZZB9_ONCMY 1 89
SEQRES 1 A 89 MET ASN ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR
SEQRES 2 A 89 ASP GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE
SEQRES 3 A 89 PHE ILE GLN ASP ALA GLU ASP GLY CYS ILE SER THR LYS
SEQRES 4 A 89 GLU LEU GLY LYS VAL MET ARG MET LEU GLY GLN ASN PRO
SEQRES 5 A 89 THR PRO GLU GLU LEU GLN GLU MET ILE ASP GLU VAL ASP
SEQRES 6 A 89 GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU
SEQRES 7 A 89 VAL MET MET VAL ARG CYS MET LYS ASP ASP SER
HET CA A 90 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 1 ASP A 3 GLU A 10 1 8
HELIX 2 2 THR A 13 ILE A 26 1 14
HELIX 3 3 GLU A 40 GLY A 49 1 10
HELIX 4 4 THR A 53 ASP A 65 1 13
HELIX 5 5 ASP A 73 ARG A 83 1 11
SHEET 1 A 2 ILE A 36 SER A 37 0
SHEET 2 A 2 THR A 71 VAL A 72 -1 O VAL A 72 N ILE A 36
LINK OD1 ASP A 65 CA CA A 90 1555 1555 2.82
LINK OD2 ASP A 67 CA CA A 90 1555 1555 3.26
LINK OD1 ASP A 67 CA CA A 90 1555 1555 2.12
LINK OG SER A 69 CA CA A 90 1555 1555 2.83
LINK O THR A 71 CA CA A 90 1555 1555 2.00
LINK OE1 GLU A 76 CA CA A 90 1555 1555 2.84
LINK OE2 GLU A 76 CA CA A 90 1555 1555 2.81
SITE 1 AC1 5 ASP A 65 ASP A 67 SER A 69 THR A 71
SITE 2 AC1 5 GLU A 76
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