Header list of 1spy.pdb file
Complete list - r 2 2 Bytes
HEADER MUSCLE PROTEIN 14-JUL-97 1SPY
TITLE REGULATORY DOMAIN OF HUMAN CARDIAC TROPONIN C IN THE CALCIUM-FREE
TITLE 2 STATE, NMR, 40 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: REGULATORY;
COMPND 5 SYNONYM: CNTNC;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS MUSCLE PROTEIN, CALCIUM-BINDING, TROPONIN C, MUSCLE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR L.SPYRACOPOULOS,M.X.LI,S.K.SIA,S.M.GAGNE,M.CHANDRA,R.J.SOLARO,
AUTHOR 2 B.D.SYKES
REVDAT 3 02-MAR-22 1SPY 1 REMARK
REVDAT 2 24-FEB-09 1SPY 1 VERSN
REVDAT 1 16-SEP-98 1SPY 0
JRNL AUTH L.SPYRACOPOULOS,M.X.LI,S.K.SIA,S.M.GAGNE,M.CHANDRA,
JRNL AUTH 2 R.J.SOLARO,B.D.SYKES
JRNL TITL CALCIUM-INDUCED STRUCTURAL TRANSITION IN THE REGULATORY
JRNL TITL 2 DOMAIN OF HUMAN CARDIAC TROPONIN C.
JRNL REF BIOCHEMISTRY V. 36 12138 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9315850
JRNL DOI 10.1021/BI971223D
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1SPY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176469.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : C13; N15-NOESY; HNHA; HACAHB;
REMARK 210 HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; UNITY INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 43
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 13
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED APO CARDIAC N-TROPONIN C.
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 PHE A 20 H PHE A 24 1.46
REMARK 500 O ASP A 65 H GLY A 68 1.52
REMARK 500 OD1 ASP A 73 H GLU A 76 1.54
REMARK 500 O SER A 37 H GLU A 40 1.58
REMARK 500 O ILE A 61 H ASP A 65 1.59
REMARK 500 O THR A 13 H GLN A 16 1.59
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 ASP A 2 -38.68 -158.43
REMARK 500 1 ASP A 3 107.85 55.70
REMARK 500 1 LEU A 29 100.80 -59.52
REMARK 500 1 GLU A 32 -69.83 67.37
REMARK 500 1 ASP A 33 -42.11 -174.68
REMARK 500 1 MET A 85 -161.95 -76.65
REMARK 500 1 LYS A 86 -153.91 -118.78
REMARK 500 1 ASP A 87 125.68 66.17
REMARK 500 2 ASP A 2 -86.13 -135.58
REMARK 500 2 PHE A 27 37.87 -144.57
REMARK 500 2 LEU A 29 104.12 -51.83
REMARK 500 2 ALA A 31 81.01 52.19
REMARK 500 2 GLU A 32 -72.97 62.63
REMARK 500 2 ASP A 33 80.97 169.85
REMARK 500 2 ASP A 65 43.61 -97.58
REMARK 500 2 SER A 69 43.23 170.39
REMARK 500 2 ASP A 73 -169.66 -109.38
REMARK 500 2 MET A 85 59.94 -154.47
REMARK 500 2 ASP A 87 91.21 61.24
REMARK 500 3 PHE A 27 33.93 -152.56
REMARK 500 3 LEU A 29 28.47 39.27
REMARK 500 3 ALA A 31 -149.87 -79.65
REMARK 500 3 GLU A 32 -75.79 -46.14
REMARK 500 3 LEU A 57 -74.97 -70.04
REMARK 500 3 ASP A 87 -68.15 -161.10
REMARK 500 4 ASP A 2 93.95 44.35
REMARK 500 4 THR A 13 -166.88 -103.86
REMARK 500 4 ALA A 31 -171.16 170.08
REMARK 500 4 GLU A 32 24.42 -147.35
REMARK 500 4 ASP A 33 48.34 -162.57
REMARK 500 4 GLU A 66 43.35 -79.90
REMARK 500 4 ASP A 67 25.76 -168.07
REMARK 500 4 SER A 69 67.79 -178.75
REMARK 500 4 MET A 85 -77.39 -63.95
REMARK 500 4 LYS A 86 -90.58 -116.64
REMARK 500 4 ASP A 88 55.73 -117.32
REMARK 500 5 ASP A 2 -157.77 -113.29
REMARK 500 5 PHE A 27 33.62 -145.25
REMARK 500 5 LEU A 29 100.15 -41.29
REMARK 500 5 ALA A 31 159.46 65.43
REMARK 500 5 GLU A 32 -74.67 -39.63
REMARK 500 5 ASP A 33 119.66 -168.59
REMARK 500 5 PRO A 52 -159.77 -73.09
REMARK 500 5 ASP A 65 41.13 -104.82
REMARK 500 5 LYS A 86 -63.22 66.36
REMARK 500 6 LEU A 29 98.94 -46.49
REMARK 500 6 ALA A 31 77.73 -169.48
REMARK 500 6 GLU A 32 -69.76 61.10
REMARK 500 6 ASP A 33 -38.96 -177.22
REMARK 500 6 PRO A 52 -161.69 -73.46
REMARK 500
REMARK 500 THIS ENTRY HAS 328 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 46 0.28 SIDE CHAIN
REMARK 500 1 ARG A 83 0.27 SIDE CHAIN
REMARK 500 2 ARG A 46 0.23 SIDE CHAIN
REMARK 500 2 ARG A 83 0.32 SIDE CHAIN
REMARK 500 3 ARG A 46 0.23 SIDE CHAIN
REMARK 500 3 ARG A 83 0.20 SIDE CHAIN
REMARK 500 4 ARG A 46 0.26 SIDE CHAIN
REMARK 500 4 ARG A 83 0.18 SIDE CHAIN
REMARK 500 5 ARG A 46 0.32 SIDE CHAIN
REMARK 500 5 ARG A 83 0.31 SIDE CHAIN
REMARK 500 6 ARG A 46 0.29 SIDE CHAIN
REMARK 500 6 ARG A 83 0.29 SIDE CHAIN
REMARK 500 7 ARG A 46 0.21 SIDE CHAIN
REMARK 500 7 ARG A 83 0.28 SIDE CHAIN
REMARK 500 8 ARG A 46 0.23 SIDE CHAIN
REMARK 500 8 ARG A 83 0.30 SIDE CHAIN
REMARK 500 9 ARG A 46 0.32 SIDE CHAIN
REMARK 500 9 ARG A 83 0.19 SIDE CHAIN
REMARK 500 10 ARG A 46 0.10 SIDE CHAIN
REMARK 500 10 ARG A 83 0.28 SIDE CHAIN
REMARK 500 11 ARG A 46 0.29 SIDE CHAIN
REMARK 500 11 ARG A 83 0.31 SIDE CHAIN
REMARK 500 12 ARG A 46 0.24 SIDE CHAIN
REMARK 500 12 ARG A 83 0.22 SIDE CHAIN
REMARK 500 13 ARG A 46 0.18 SIDE CHAIN
REMARK 500 13 ARG A 83 0.22 SIDE CHAIN
REMARK 500 14 ARG A 83 0.30 SIDE CHAIN
REMARK 500 15 ARG A 46 0.29 SIDE CHAIN
REMARK 500 16 ARG A 46 0.28 SIDE CHAIN
REMARK 500 16 ARG A 83 0.26 SIDE CHAIN
REMARK 500 17 ARG A 46 0.11 SIDE CHAIN
REMARK 500 17 ARG A 83 0.28 SIDE CHAIN
REMARK 500 18 ARG A 46 0.25 SIDE CHAIN
REMARK 500 18 ARG A 83 0.21 SIDE CHAIN
REMARK 500 19 ARG A 46 0.17 SIDE CHAIN
REMARK 500 19 ARG A 83 0.18 SIDE CHAIN
REMARK 500 20 ARG A 46 0.24 SIDE CHAIN
REMARK 500 20 ARG A 83 0.23 SIDE CHAIN
REMARK 500 21 ARG A 46 0.24 SIDE CHAIN
REMARK 500 21 ARG A 83 0.18 SIDE CHAIN
REMARK 500 22 ARG A 46 0.28 SIDE CHAIN
REMARK 500 22 ARG A 83 0.24 SIDE CHAIN
REMARK 500 23 ARG A 46 0.28 SIDE CHAIN
REMARK 500 23 ARG A 83 0.08 SIDE CHAIN
REMARK 500 24 ARG A 46 0.20 SIDE CHAIN
REMARK 500 24 ARG A 83 0.31 SIDE CHAIN
REMARK 500 25 ARG A 83 0.31 SIDE CHAIN
REMARK 500 26 ARG A 46 0.32 SIDE CHAIN
REMARK 500 26 ARG A 83 0.14 SIDE CHAIN
REMARK 500 27 ARG A 46 0.26 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 76 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE II.
DBREF 1SPY A 1 89 UNP P63316 TNNC1_HUMAN 1 89
SEQRES 1 A 89 MET ASP ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR
SEQRES 2 A 89 GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE
SEQRES 3 A 89 PHE VAL LEU GLY 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
HELIX 1 1 TYR A 5 GLN A 11 1 7
HELIX 2 2 GLU A 14 PHE A 27 1 14
HELIX 3 3 LEU A 41 LEU A 48 1 8
HELIX 4 4 PRO A 54 VAL A 64 1 11
HELIX 5 5 GLU A 76 CYS A 84 1 9
SHEET 1 S1 2 CYS A 35 SER A 37 0
SHEET 2 S1 2 THR A 71 ASP A 73 -1
SITE 1 CAB 12 ASP A 65 GLU A 66 ASP A 67 GLY A 68
SITE 2 CAB 12 SER A 69 GLY A 70 THR A 71 VAL A 72
SITE 3 CAB 12 ASP A 73 PHE A 74 ASP A 75 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