Header list of 1aj4.pdb file
Complete list - 3 20 Bytes
HEADER MUSCLE PROTEIN 14-MAY-97 1AJ4
TITLE STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 1 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CTNC;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: CARDIAC TROPONIN C, CALCIUM IONS BOUND AT SITES II,
COMPND 8 III AND IV
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGAN: HEART;
SOURCE 7 TISSUE: MUSCLE;
SOURCE 8 CELLULAR_LOCATION: THIN FILAMENT;
SOURCE 9 GENE: CTNC(A-CYS);
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET-23D;
SOURCE 14 EXPRESSION_SYSTEM_GENE: CTNC(A-CYS)
KEYWDS CARDIAC, MUSCLE PROTEIN, REGULATORY, CALCIUM BINDING
EXPDTA SOLUTION NMR
AUTHOR S.K.SIA,M.X.LI,L.SPYRACOPOULOS,S.M.GAGNE,W.LIU,J.A.PUTKEY,B.D.SYKES
REVDAT 4 03-NOV-21 1AJ4 1 REMARK SEQADV LINK
REVDAT 3 19-MAY-09 1AJ4 1 REMARK
REVDAT 2 24-FEB-09 1AJ4 1 VERSN
REVDAT 1 20-MAY-98 1AJ4 0
JRNL AUTH S.K.SIA,M.X.LI,L.SPYRACOPOULOS,S.M.GAGNE,W.LIU,J.A.PUTKEY,
JRNL AUTH 2 B.D.SYKES
JRNL TITL STRUCTURE OF CARDIAC MUSCLE TROPONIN C UNEXPECTEDLY REVEALS
JRNL TITL 2 A CLOSED REGULATORY DOMAIN.
JRNL REF J.BIOL.CHEM. V. 272 18216 1997
JRNL REFN ISSN 0021-9258
JRNL PMID 9218458
JRNL DOI 10.1074/JBC.272.29.18216
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: CALCULATIONS OF THE N- AND C-DOMAINS
REMARK 3 WERE PERFORMED SEPARATELY BECAUSE THE CENTRAL LINKER IS
REMARK 3 UNSTRUCTURED AND FLEXIBLE IN SOLUTION. THE ORIENTATION OF THE
REMARK 3 TWO DOMAINS WITH RESPECT TO EACH OTHER AND THE STRUCTURE OF THE
REMARK 3 CENTRAL LINKER (RESIDUES 86 - 94) ARE THEREFORE UNDEFINED. THE N-
REMARK 3 DOMAIN (2 - 85) AND C-DOMAIN (95 - 161) IN THIS STRUCTURE ARE
REMARK 3 THE STRUCTURES IN THE ENSEMBLES CLOSEST TO THE UNMINIMIZED
REMARK 3 AVERAGE STRUCTURES. IN PARTICULAR, THE N-DOMAIN HERE CORRESPONDS
REMARK 3 TO MODEL 25 IN 2CTN, AND THE C-DOMAIN TO MODEL 3 IN 3CTN. THE
REMARK 3 CENTRAL LINKER HERE IS THE RESULT OF ENERGY MINIMIZATION WITHOUT
REMARK 3 EXPERIMENTAL RESTRAINTS, AND IS ADDED ONLY AS A TOOL OF
REMARK 3 CONVENIENCE.
REMARK 4
REMARK 4 1AJ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170879.
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 : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : SMALLEST RMSD TO THE AVERAGE
REMARK 210 STRUCTURE
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 RES C SSSEQI
REMARK 465 ALA A 1
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 ILE A 61 H ASP A 65 1.46
REMARK 500 O THR A 13 H GLN A 16 1.53
REMARK 500 O VAL A 28 H ALA A 31 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 LEU A 12 165.91 -43.55
REMARK 500 ALA A 31 -160.07 -77.51
REMARK 500 GLU A 32 -38.25 -146.30
REMARK 500 LEU A 48 -82.31 -76.97
REMARK 500 ASP A 73 -164.27 -107.56
REMARK 500 MET A 85 -64.21 -104.58
REMARK 500 ASP A 87 113.83 59.12
REMARK 500 SER A 89 -52.86 -177.57
REMARK 500 LYS A 90 174.43 -56.60
REMARK 500 LYS A 92 101.19 -179.27
REMARK 500 THR A 93 -124.17 -146.98
REMARK 500 ASP A 105 88.50 -56.43
REMARK 500 THR A 124 21.42 -140.73
REMARK 500 GLU A 126 -154.28 -74.95
REMARK 500 ASN A 144 72.18 47.97
REMARK 500 VAL A 160 -54.86 -158.08
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 ARG A 46 0.22 SIDE CHAIN
REMARK 500 ARG A 83 0.31 SIDE CHAIN
REMARK 500 ARG A 102 0.32 SIDE CHAIN
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 162 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 65 CG
REMARK 620 2 ASP A 65 OD1 30.8
REMARK 620 3 ASP A 65 OD2 30.6 60.6
REMARK 620 4 ASP A 67 OD1 61.0 55.6 66.6
REMARK 620 5 SER A 69 OG 86.9 108.8 60.0 67.3
REMARK 620 6 THR A 71 O 104.0 114.1 98.4 164.4 110.0
REMARK 620 7 THR A 71 OG1 142.7 172.7 112.5 120.5 64.2 68.2
REMARK 620 8 GLU A 76 OE1 80.6 69.8 100.6 123.3 154.3 52.8 115.3
REMARK 620 9 GLU A 76 OE2 113.2 86.3 142.3 110.9 156.6 77.9 101.0 47.2
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 163 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 105 OD1
REMARK 620 2 ASN A 107 OD1 124.0
REMARK 620 3 ASP A 109 OD1 90.7 71.2
REMARK 620 4 TYR A 111 O 72.2 135.7 67.5
REMARK 620 5 GLU A 116 OE1 66.3 120.6 157.0 103.7
REMARK 620 6 GLU A 116 OE2 114.7 84.7 152.2 129.1 49.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 164 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 OD1
REMARK 620 2 ASN A 143 OD1 55.4
REMARK 620 3 ASP A 145 OD1 63.2 75.9
REMARK 620 4 ASP A 145 OD2 106.4 86.9 46.2
REMARK 620 5 ARG A 147 O 97.3 142.8 68.7 76.8
REMARK 620 6 GLU A 152 OE2 110.3 69.4 138.9 109.6 147.6
REMARK 620 7 GLU A 152 OE1 64.0 61.6 124.8 147.4 133.5 53.5
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 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 164
DBREF 1AJ4 A 3 161 UNP P09860 TNNC1_CHICK 3 161
SEQADV 1AJ4 SER A 35 UNP P09860 CYS 35 ENGINEERED MUTATION
SEQADV 1AJ4 SER A 84 UNP P09860 CYS 84 ENGINEERED MUTATION
SEQRES 1 A 161 ALA ALA ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR
SEQRES 2 A 161 GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE
SEQRES 3 A 161 PHE VAL LEU GLY ALA GLU ASP GLY SER ILE SER THR LYS
SEQRES 4 A 161 GLU LEU GLY LYS VAL MET ARG MET LEU GLY GLN ASN PRO
SEQRES 5 A 161 THR PRO GLU GLU LEU GLN GLU MET ILE ASP GLU VAL ASP
SEQRES 6 A 161 GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU
SEQRES 7 A 161 VAL MET MET VAL ARG SER MET LYS ASP ASP SER LYS GLY
SEQRES 8 A 161 LYS THR GLU GLU GLU LEU SER ASP LEU PHE ARG MET PHE
SEQRES 9 A 161 ASP LYS ASN ALA ASP GLY TYR ILE ASP LEU GLU GLU LEU
SEQRES 10 A 161 LYS ILE MET LEU GLN ALA THR GLY GLU THR ILE THR GLU
SEQRES 11 A 161 ASP ASP ILE GLU GLU LEU MET LYS ASP GLY ASP LYS ASN
SEQRES 12 A 161 ASN ASP GLY ARG ILE ASP TYR ASP GLU PHE LEU GLU PHE
SEQRES 13 A 161 MET LYS GLY VAL GLU
HET CA A 162 1
HET CA A 163 1
HET CA A 164 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 3(CA 2+)
HELIX 1 HN LYS A 6 GLU A 10 1 5
HELIX 2 HA GLU A 14 VAL A 28 1 15
HELIX 3 HB THR A 38 LEU A 48 1 11
HELIX 4 HC PRO A 54 VAL A 64 1 11
HELIX 5 HD PHE A 74 ARG A 83 1 10
HELIX 6 HE GLU A 95 MET A 103 1 9
HELIX 7 HF LEU A 114 ALA A 123 1 10
HELIX 8 HG GLU A 130 GLY A 140 1 11
HELIX 9 HH TYR A 150 LYS A 158 1 9
SHEET 1 S1 2 SER A 35 SER A 37 0
SHEET 2 S1 2 THR A 71 ASP A 73 -1 N VAL A 72 O ILE A 36
SHEET 1 S2 2 TYR A 111 ASP A 113 0
SHEET 2 S2 2 ARG A 147 ASP A 149 -1 O ILE A 148 N ILE A 112
LINK CG ASP A 65 CA CA A 162 1555 1555 2.38
LINK OD1 ASP A 65 CA CA A 162 1555 1555 2.08
LINK OD2 ASP A 65 CA CA A 162 1555 1555 2.18
LINK OD1 ASP A 67 CA CA A 162 1555 1555 2.81
LINK OG SER A 69 CA CA A 162 1555 1555 2.74
LINK O THR A 71 CA CA A 162 1555 1555 2.81
LINK OG1 THR A 71 CA CA A 162 1555 1555 2.75
LINK OE1 GLU A 76 CA CA A 162 1555 1555 2.78
LINK OE2 GLU A 76 CA CA A 162 1555 1555 2.57
LINK OD1 ASP A 105 CA CA A 163 1555 1555 2.81
LINK OD1 ASN A 107 CA CA A 163 1555 1555 2.78
LINK OD1 ASP A 109 CA CA A 163 1555 1555 2.10
LINK O TYR A 111 CA CA A 163 1555 1555 2.08
LINK OE1 GLU A 116 CA CA A 163 1555 1555 2.42
LINK OE2 GLU A 116 CA CA A 163 1555 1555 2.68
LINK OD1 ASP A 141 CA CA A 164 1555 1555 2.77
LINK OD1 ASN A 143 CA CA A 164 1555 1555 2.77
LINK OD1 ASP A 145 CA CA A 164 1555 1555 2.45
LINK OD2 ASP A 145 CA CA A 164 1555 1555 2.93
LINK O ARG A 147 CA CA A 164 1555 1555 2.16
LINK OE2 GLU A 152 CA CA A 164 1555 1555 2.26
LINK OE1 GLU A 152 CA CA A 164 1555 1555 2.50
SITE 1 AC1 5 ASP A 65 ASP A 67 SER A 69 THR A 71
SITE 2 AC1 5 GLU A 76
SITE 1 AC2 6 ASP A 105 ASN A 107 ASP A 109 TYR A 111
SITE 2 AC2 6 ILE A 112 GLU A 116
SITE 1 AC3 5 ASP A 141 ASN A 143 ASP A 145 ARG A 147
SITE 2 AC3 5 GLU A 152
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
Complete list - 3 20 Bytes