Header list of 1mxl.pdb file
Complete list - b 23 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 22-APR-99 1MXL
TITLE STRUCTURE OF CARDIAC TROPONIN C-TROPONIN I COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (TROPONIN C);
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: REGULATORY N-DOMAIN RESIDUES 1-89;
COMPND 5 SYNONYM: CNTNC;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: CALCIUM SATURATED N-DOMAIN OF CARDIAC TROPONIN C IN
COMPND 8 COMPLEX WITH CARDIAC TROPONIN I 147-163;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROTEIN (TROPONIN I);
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: CARDIAC TROPONIN I RESIDUES 147-163;
COMPND 13 SYNONYM: CNTNI PEPTIDE;
COMPND 14 ENGINEERED: YES;
COMPND 15 OTHER_DETAILS: CARDIAC TROPONIN I 147-163 IN COMPLEX WITH THE N-
COMPND 16 DOMAIN OF CARDIAC TROPONIN C
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: BL21(DE3) PLYSS;
SOURCE 6 ORGAN: HEART;
SOURCE 7 TISSUE: MUSCLE;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 11 EXPRESSION_SYSTEM_TISSUE: MUSCLE;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR: PET3D;
SOURCE 14 OTHER_DETAILS: HOMO SAPIENS;
SOURCE 15 MOL_ID: 2;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. ITS PARENT
SOURCE 18 PROTEIN IS NATURALLY FOUND IN HEART TISSUE OF HOMO SAPIENS (HUMAN).
KEYWDS TROPONIN, MUSCLE CONTRACTION, REGULATORY PROTEIN, CALCIUM-BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR M.X.LI,L.SPYRACOPOULOS,B.D.SYKES
REVDAT 4 23-FEB-22 1MXL 1 REMARK LINK
REVDAT 3 24-FEB-09 1MXL 1 VERSN
REVDAT 2 01-APR-03 1MXL 1 JRNL
REVDAT 1 06-JUL-99 1MXL 0
JRNL AUTH M.X.LI,L.SPYRACOPOULOS,B.D.SYKES
JRNL TITL BINDING OF CARDIAC TROPONIN-I147-163 INDUCES A STRUCTURAL
JRNL TITL 2 OPENING IN HUMAN CARDIAC TROPONIN-C.
JRNL REF BIOCHEMISTRY V. 38 8289 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10387074
JRNL DOI 10.1021/BI9901679
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1MXL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000925.
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 : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% WATER/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-NOESY; 2D-TOCSY; 15N-NOESY;
REMARK 210 15N13C-NOESY; HCCHTOCSY; 15N-
REMARK 210 HSQC; 13C-HSQC; HNHA; CBCA(CO)
REMARK 210 NNH; HNCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITYPLUS
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 : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 18
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED TROPONIN C AND A SYNTHETIC
REMARK 210 TROPONIN I PEPTIDE
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I
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 SER C 37 HG1 THR C 38 1.48
REMARK 500 O GLN C 58 H ASP C 62 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 C 2 -159.69 -143.07
REMARK 500 1 GLN C 11 36.88 -94.01
REMARK 500 1 LEU C 29 87.03 -57.40
REMARK 500 1 SER C 37 32.70 -158.35
REMARK 500 1 THR C 38 -51.14 74.83
REMARK 500 1 ASN C 51 84.98 -178.38
REMARK 500 1 VAL C 64 36.42 -141.45
REMARK 500 1 MET C 85 -83.22 -44.81
REMARK 500 1 ASP C 88 27.59 -154.23
REMARK 500 1 LEU I 11 -165.17 -126.14
REMARK 500 1 ALA I 14 25.36 -148.00
REMARK 500 1 ALA I 16 43.15 -144.46
REMARK 500 2 ASP C 3 54.48 -106.88
REMARK 500 2 LEU C 12 -169.46 -59.14
REMARK 500 2 LEU C 29 100.25 -59.34
REMARK 500 2 CYS C 35 -166.29 -106.32
REMARK 500 2 SER C 37 37.99 -158.05
REMARK 500 2 THR C 38 -54.68 71.38
REMARK 500 2 ASN C 51 98.76 -164.31
REMARK 500 2 THR C 53 173.62 -53.69
REMARK 500 2 LEU C 57 -72.30 -56.41
REMARK 500 2 LYS C 86 54.52 -159.38
REMARK 500 2 ASP C 87 76.90 -152.59
REMARK 500 2 SER I 3 -179.67 -65.18
REMARK 500 2 LEU I 12 66.77 65.83
REMARK 500 2 ALA I 14 -172.89 55.52
REMARK 500 2 ALA I 16 -38.54 -177.71
REMARK 500 3 ASP C 2 48.05 -170.26
REMARK 500 3 ASP C 3 78.00 51.58
REMARK 500 3 LEU C 29 101.62 -43.42
REMARK 500 3 GLU C 32 -64.84 -102.56
REMARK 500 3 SER C 37 32.61 -157.82
REMARK 500 3 THR C 38 -44.33 78.38
REMARK 500 3 ASP C 67 19.86 -152.66
REMARK 500 3 CYS C 84 46.24 -95.97
REMARK 500 3 SER I 3 69.26 62.18
REMARK 500 4 ASP C 3 108.05 -43.71
REMARK 500 4 ILE C 4 -36.24 -141.86
REMARK 500 4 SER C 37 41.13 -154.98
REMARK 500 4 THR C 38 -57.54 72.05
REMARK 500 4 ASN C 51 96.85 -168.43
REMARK 500 4 THR C 53 176.55 -54.42
REMARK 500 4 GLU C 66 57.40 -119.17
REMARK 500 4 ASP C 67 -36.65 -146.56
REMARK 500 4 SER C 69 -70.58 -101.65
REMARK 500 4 MET C 85 -159.39 -66.65
REMARK 500 4 LYS C 86 108.83 -176.30
REMARK 500 4 ASP C 88 156.65 180.00
REMARK 500 4 LEU I 11 20.32 -149.13
REMARK 500 4 ARG I 15 29.30 -154.45
REMARK 500
REMARK 500 THIS ENTRY HAS 495 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 C 46 0.27 SIDE CHAIN
REMARK 500 1 ARG C 83 0.30 SIDE CHAIN
REMARK 500 1 ARG I 1 0.32 SIDE CHAIN
REMARK 500 1 ARG I 15 0.23 SIDE CHAIN
REMARK 500 2 ARG C 46 0.32 SIDE CHAIN
REMARK 500 2 ARG C 83 0.26 SIDE CHAIN
REMARK 500 2 ARG I 1 0.30 SIDE CHAIN
REMARK 500 2 ARG I 15 0.14 SIDE CHAIN
REMARK 500 3 ARG C 46 0.21 SIDE CHAIN
REMARK 500 3 ARG C 83 0.30 SIDE CHAIN
REMARK 500 3 ARG I 1 0.09 SIDE CHAIN
REMARK 500 3 ARG I 15 0.18 SIDE CHAIN
REMARK 500 4 ARG C 46 0.10 SIDE CHAIN
REMARK 500 4 ARG C 83 0.20 SIDE CHAIN
REMARK 500 4 ARG I 1 0.26 SIDE CHAIN
REMARK 500 4 ARG I 15 0.32 SIDE CHAIN
REMARK 500 5 ARG C 83 0.30 SIDE CHAIN
REMARK 500 5 ARG I 1 0.22 SIDE CHAIN
REMARK 500 5 ARG I 15 0.27 SIDE CHAIN
REMARK 500 6 ARG C 46 0.30 SIDE CHAIN
REMARK 500 6 ARG C 83 0.21 SIDE CHAIN
REMARK 500 6 ARG I 1 0.15 SIDE CHAIN
REMARK 500 6 ARG I 15 0.24 SIDE CHAIN
REMARK 500 7 ARG C 46 0.30 SIDE CHAIN
REMARK 500 7 ARG C 83 0.28 SIDE CHAIN
REMARK 500 7 ARG I 1 0.22 SIDE CHAIN
REMARK 500 7 ARG I 15 0.30 SIDE CHAIN
REMARK 500 8 ARG C 46 0.23 SIDE CHAIN
REMARK 500 8 ARG C 83 0.21 SIDE CHAIN
REMARK 500 8 ARG I 1 0.17 SIDE CHAIN
REMARK 500 8 ARG I 15 0.28 SIDE CHAIN
REMARK 500 9 ARG C 46 0.30 SIDE CHAIN
REMARK 500 9 ARG C 83 0.25 SIDE CHAIN
REMARK 500 9 ARG I 1 0.32 SIDE CHAIN
REMARK 500 9 ARG I 15 0.28 SIDE CHAIN
REMARK 500 10 ARG C 46 0.25 SIDE CHAIN
REMARK 500 10 ARG C 83 0.30 SIDE CHAIN
REMARK 500 10 ARG I 1 0.25 SIDE CHAIN
REMARK 500 10 ARG I 15 0.31 SIDE CHAIN
REMARK 500 11 ARG C 46 0.20 SIDE CHAIN
REMARK 500 11 ARG C 83 0.25 SIDE CHAIN
REMARK 500 11 ARG I 15 0.18 SIDE CHAIN
REMARK 500 12 ARG C 83 0.30 SIDE CHAIN
REMARK 500 12 ARG I 1 0.29 SIDE CHAIN
REMARK 500 12 ARG I 15 0.14 SIDE CHAIN
REMARK 500 13 ARG C 83 0.31 SIDE CHAIN
REMARK 500 13 ARG I 1 0.31 SIDE CHAIN
REMARK 500 13 ARG I 15 0.28 SIDE CHAIN
REMARK 500 14 ARG C 46 0.19 SIDE CHAIN
REMARK 500 14 ARG C 83 0.21 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 150 PLANE DEVIATIONS.
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 C 90 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 65 OD2
REMARK 620 2 ASP C 67 OD1 81.2
REMARK 620 3 ASP C 67 OD2 120.2 55.8
REMARK 620 4 SER C 69 OG 84.8 92.7 61.1
REMARK 620 5 THR C 71 O 92.4 158.8 112.7 66.4
REMARK 620 6 GLU C 76 OE2 152.2 93.3 76.5 122.8 101.3
REMARK 620 7 GLU C 76 OE1 99.7 119.3 135.7 148.0 81.7 59.3
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 C 90
DBREF 1MXL C 1 89 UNP P63316 TNNC1_HUMAN 1 89
DBREF 1MXL I 1 17 UNP P19429 TNNI3_HUMAN 147 163
SEQRES 1 C 89 MET ASP ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR
SEQRES 2 C 89 GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE
SEQRES 3 C 89 PHE VAL LEU GLY ALA GLU ASP GLY CYS ILE SER THR LYS
SEQRES 4 C 89 GLU LEU GLY LYS VAL MET ARG MET LEU GLY GLN ASN PRO
SEQRES 5 C 89 THR PRO GLU GLU LEU GLN GLU MET ILE ASP GLU VAL ASP
SEQRES 6 C 89 GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU
SEQRES 7 C 89 VAL MET MET VAL ARG CYS MET LYS ASP ASP SER
SEQRES 1 I 17 ARG ILE SER ALA ASP ALA MET MET GLN ALA LEU LEU GLY
SEQRES 2 I 17 ALA ARG ALA LYS
HET CA C 90 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
HELIX 1 1 ILE C 4 GLU C 10 1 7
HELIX 2 2 GLU C 14 VAL C 28 1 15
HELIX 3 3 LEU C 41 LEU C 48 1 8
HELIX 4 4 PRO C 54 VAL C 64 1 11
HELIX 5 5 PHE C 74 VAL C 82 1 9
HELIX 6 6 ALA I 4 ALA I 10 1 7
LINK OD2 ASP C 65 CA CA C 90 1555 1555 2.80
LINK OD1 ASP C 67 CA CA C 90 1555 1555 2.13
LINK OD2 ASP C 67 CA CA C 90 1555 1555 2.44
LINK OG SER C 69 CA CA C 90 1555 1555 2.71
LINK O THR C 71 CA CA C 90 1555 1555 2.70
LINK OE2 GLU C 76 CA CA C 90 1555 1555 2.28
LINK OE1 GLU C 76 CA CA C 90 1555 1555 2.05
SITE 1 AC1 5 ASP C 65 ASP C 67 SER C 69 THR C 71
SITE 2 AC1 5 GLU C 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 - b 23 2 Bytes