HEADER METAL BINDING PROTEIN 11-FEB-14 2MKP
TITLE N DOMAIN OF CARDIAC TROPONIN C BOUND TO THE SWITCH FRAGMENT OF FAST
TITLE 2 SKELETAL TROPONIN I AT PH 6
CAVEAT 2MKP CHIRALITY ERROR AT CA ATOM OF GLY C42.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C, SLOW SKELETAL AND CARDIAC MUSCLES;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: UNP RESIDUES 1-89;
COMPND 5 SYNONYM: TN-C;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TROPONIN I, FAST SKELETAL MUSCLE;
COMPND 9 CHAIN: I;
COMPND 10 FRAGMENT: UNP RESIDUES 116-132;
COMPND 11 SYNONYM: TROPONIN I, FAST-TWITCH ISOFORM;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TNNC1, TNNC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-3A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: TNNI2;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TROPONIN C, TROPONIN I, EF-HAND, CALCIUM BINDING, ISCHEMIA, METAL
KEYWDS 2 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR I.M.ROBERTSON,S.E.PINEDA-SANABRIA,P.C.HOLMES,B.D.SYKES
REVDAT 2 18-JUN-14 2MKP 1 JRNL
REVDAT 1 26-FEB-14 2MKP 0
JRNL AUTH I.M.ROBERTSON,S.E.PINEDA-SANABRIA,P.C.HOLMES,B.D.SYKES
JRNL TITL CONFORMATION OF THE CRITICAL PH SENSITIVE REGION OF TROPONIN
JRNL TITL 2 DEPENDS UPON A SINGLE RESIDUE IN TROPONIN I.
JRNL REF ARCH.BIOCHEM.BIOPHYS. V.-553 40 2014
JRNL REFN ISSN 0003-9861
JRNL PMID 24333682
JRNL DOI 10.1016/J.ABB.2013.12.003
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PSVS, X-PLOR_NIH
REMARK 3 AUTHORS : BHATTACHARYA AND MONTELIONE (PSVS), SCHWIETERS,
REMARK 3 KUSZEWSKI, TJANDRA AND CLORE (X-PLOR_NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEMI-RIGID SIMULATED ANNEALING. STNI
REMARK 3 WAS DOCKED ONTO CNTNC. CNTNC BACKBONE WAS KEPT RIGID AND SIDE
REMARK 3 CHAIN'S WERE ALLOWED TO ROTATE.
REMARK 4
REMARK 4 2MKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-14.
REMARK 100 THE RCSB ID CODE IS RCSB103730.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : 0.12
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.2-0.3 MM [U-95% 13C; U-95%
REMARK 210 15N] CNTNC, 2-2.5 MM STNI(115-
REMARK 210 131), 0.25 MM DSS, 100 MM
REMARK 210 POTASSIUM CHLORIDE, 10 MM
REMARK 210 IMIDAZOLE, 10 MM CALCIUM, 95%
REMARK 210 H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D CBCA(CO)NH; 3D C(CO)NH; 3D
REMARK 210 HNCACB; 3D H(CCO)NH; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-13C NOESY ALIPHATIC;
REMARK 210 2D 1H-1H NOESY; 2D 1H-1H TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMRJ, PSVS, NMRDRAW, NMRPIPE,
REMARK 210 NMRVIEW, X-PLOR_NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: 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 ALA C 23 H PHE C 27 1.55
REMARK 500 O GLU C 56 H GLU C 59 1.55
REMARK 500 O GLN C 58 H ASP C 62 1.56
REMARK 500 OD1 ASP C 67 H SER C 69 1.57
REMARK 500 O PHE C 24 HG12 VAL C 28 1.57
REMARK 500 O PHE C 24 CG1 VAL C 28 2.00
REMARK 500 O LEU I 122 O LEU I 126 2.17
REMARK 500 OD1 ASP C 65 OD1 ASP C 67 2.18
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 GLN C 11 44.83 -93.39
REMARK 500 1 LEU C 29 93.59 -68.55
REMARK 500 1 CYS C 35 -167.88 -128.32
REMARK 500 1 SER C 37 42.51 -154.08
REMARK 500 1 THR C 38 -57.42 70.79
REMARK 500 1 ARG C 46 -36.85 -39.00
REMARK 500 1 ASN C 51 81.16 -175.96
REMARK 500 1 VAL C 64 53.44 -147.77
REMARK 500 1 CYS C 84 40.95 -109.38
REMARK 500 1 MET C 85 -76.54 -57.90
REMARK 500 1 ASP C 88 36.39 -152.86
REMARK 500 1 MET I 116 130.32 58.36
REMARK 500 1 ALA I 124 -84.77 -80.47
REMARK 500 2 GLN C 11 45.43 -93.89
REMARK 500 2 LEU C 29 95.18 -65.82
REMARK 500 2 CYS C 35 -168.32 -129.25
REMARK 500 2 SER C 37 40.78 -157.27
REMARK 500 2 THR C 38 -55.05 70.65
REMARK 500 2 ARG C 46 -36.64 -39.21
REMARK 500 2 ASN C 51 81.94 -175.70
REMARK 500 2 VAL C 64 51.82 -145.64
REMARK 500 2 CYS C 84 41.05 -109.49
REMARK 500 2 MET C 85 -75.76 -56.96
REMARK 500 2 ASP C 88 35.63 -154.73
REMARK 500 2 ALA I 124 -84.20 -77.00
REMARK 500 2 LEU I 125 -50.00 -29.81
REMARK 500 2 SER I 128 -67.83 55.09
REMARK 500 2 HIS I 130 -136.83 -165.38
REMARK 500 3 GLN C 11 45.10 -95.06
REMARK 500 3 PHE C 24 -38.51 -38.49
REMARK 500 3 LEU C 29 94.51 -65.74
REMARK 500 3 CYS C 35 -168.17 -128.70
REMARK 500 3 SER C 37 42.25 -157.24
REMARK 500 3 THR C 38 -55.14 69.88
REMARK 500 3 ARG C 46 -37.33 -39.16
REMARK 500 3 ASN C 51 80.42 -178.10
REMARK 500 3 VAL C 64 50.95 -146.24
REMARK 500 3 MET C 85 -75.21 -59.05
REMARK 500 3 ASP C 88 34.49 -154.63
REMARK 500 3 ALA I 124 -74.85 -83.23
REMARK 500 4 GLN C 11 43.17 -94.39
REMARK 500 4 PHE C 24 -38.42 -38.30
REMARK 500 4 LEU C 29 95.38 -66.88
REMARK 500 4 CYS C 35 -168.35 -129.78
REMARK 500 4 SER C 37 40.53 -159.68
REMARK 500 4 THR C 38 -57.00 70.75
REMARK 500 4 ARG C 46 -38.31 -38.42
REMARK 500 4 ASN C 51 81.88 -176.40
REMARK 500 4 VAL C 64 58.99 -146.91
REMARK 500 4 MET C 80 -18.10 -49.66
REMARK 500
REMARK 500 THIS ENTRY HAS 131 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 1 CA C 101 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 71 O
REMARK 620 2 GLU C 76 OE2 109.3
REMARK 620 3 ASP C 67 OD1 144.8 78.1
REMARK 620 4 ASP C 67 OD2 103.3 57.9 50.3
REMARK 620 5 GLU C 76 OE1 71.6 50.1 127.7 97.7
REMARK 620 6 SER C 69 OG 71.8 124.0 75.8 67.3 135.4
REMARK 620 7 ASP C 65 OD2 121.5 119.0 78.8 129.1 117.4 103.2
REMARK 620 8 ASP C 65 OD1 164.6 81.3 46.5 91.7 110.1 112.0 43.6
REMARK 620 N 1 2 3 4 5 6 7
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 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19789 RELATED DB: BMRB
DBREF 2MKP C 1 89 UNP P63316 TNNC1_HUMAN 1 89
DBREF 2MKP I 115 131 UNP P48788 TNNI2_HUMAN 116 132
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 MET SER ALA ASP ALA MET LEU LYS ALA LEU LEU GLY
SEQRES 2 I 17 SER LYS HIS LYS
HET CA C 101 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
HELIX 1 1 TYR C 5 GLN C 11 1 7
HELIX 2 2 THR C 13 PHE C 27 1 15
HELIX 3 3 GLU C 40 GLY C 49 1 10
HELIX 4 4 THR C 53 GLU C 63 1 11
HELIX 5 5 ASP C 75 ARG C 83 1 9
HELIX 6 6 SER I 117 ALA I 124 1 8
LINK O THR C 71 CA CA C 101 1555 1555 2.44
LINK OE2 GLU C 76 CA CA C 101 1555 1555 2.48
LINK OD1 ASP C 67 CA CA C 101 1555 1555 2.53
LINK OD2 ASP C 67 CA CA C 101 1555 1555 2.54
LINK OE1 GLU C 76 CA CA C 101 1555 1555 2.60
LINK OG SER C 69 CA CA C 101 1555 1555 2.71
LINK OD2 ASP C 65 CA CA C 101 1555 1555 2.89
LINK OD1 ASP C 65 CA CA C 101 1555 1555 2.91
SITE 1 AC1 6 ASP C 65 ASP C 67 SER C 69 GLY C 70
SITE 2 AC1 6 THR C 71 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
(ATOM LINES ARE NOT SHOWN.)
END
