HEADER CALCIUM-REGULATED MUSCLE CONTRACTION 04-MAR-98 1TCF
TITLE CRYSTAL STRUCTURE OF CALCIUM-SATURATED RABBIT SKELETAL TROPONIN C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MUSCLE CONTRACTION, CALCIUM-BINDING, TROPONIN, E-F HAND, OPEN
KEYWDS 2 CONFORMATION REGULATORY DOMAIN, CALCIUM-REGULATED MUSCLE CONTRACTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SOMAN,G.N.PHILLIPS JR.
REVDAT 6 14-FEB-24 1TCF 1 REMARK
REVDAT 5 03-NOV-21 1TCF 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1TCF 1 VERSN
REVDAT 3 17-JAN-06 1TCF 1 JRNL
REVDAT 2 03-MAY-05 1TCF 1 AUTHOR
REVDAT 1 27-MAY-98 1TCF 0
JRNL AUTH J.SOMAN,T.TAO,G.N.PHILLIPS JR
JRNL TITL CONFORMATIONAL VARIATION OF CALCIUM-BOUND TROPONIN C.
JRNL REF PROTEINS V. 37 510 1999
JRNL REFN ISSN 0887-3585
JRNL PMID 10651267
JRNL DOI 10.1002/(SICI)1097-0134(19991201)37:4<510::AID-PROT2>3.3.CO;
JRNL DOI 2 2-K
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 68.0
REMARK 3 NUMBER OF REFLECTIONS : 9587
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.278
REMARK 3 FREE R VALUE : 0.358
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 463
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.017
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1286
REMARK 3 BIN R VALUE (WORKING SET) : 0.3530
REMARK 3 BIN FREE R VALUE : 0.4380
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 69
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.053
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1231
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 197
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.38000
REMARK 3 B22 (A**2) : -1.75000
REMARK 3 B33 (A**2) : 0.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.57000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.060
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.310 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.250 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.860 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.820 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TCF 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_1000176612.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : SIEMENS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10911
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 77.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40-50% MPD, 50MM SODIUM ACETATE 5MM
REMARK 280 CACL2, PH 5.6.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 29.80000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR A 1
REMARK 465 VAL A 158
REMARK 465 GLN A 159
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HOH A 287 O HOH A 344 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ASP A 24 NH2 ARG A 100 2646 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 13 CG GLU A 13 CD 0.096
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 13 OE1 - CD - OE2 ANGL. DEV. = -10.0 DEGREES
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 ASP A 27 70.57 -69.82
REMARK 500 ASP A 63 77.56 -48.90
REMARK 500 ALA A 106 65.30 26.45
REMARK 500 HIS A 125 -83.07 -40.25
REMARK 500 VAL A 126 113.34 54.50
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 164 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 14 OE1
REMARK 620 2 GLU A 14 OE2 51.0
REMARK 620 3 HOH A 176 O 89.4 128.4
REMARK 620 4 HOH A 219 O 85.6 75.3 69.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 160 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 27 OD1
REMARK 620 2 ASP A 29 OD1 81.8
REMARK 620 3 ASP A 33 O 90.5 149.3
REMARK 620 4 GLU A 38 OE1 100.5 131.4 79.1
REMARK 620 5 GLU A 38 OE2 101.0 81.2 129.5 50.5
REMARK 620 6 HOH A 182 O 99.6 81.1 70.9 143.8 150.5
REMARK 620 7 HOH A 215 O 166.2 99.3 95.1 68.3 65.8 94.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 161 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 63 OD1
REMARK 620 2 ASP A 65 OD1 89.2
REMARK 620 3 SER A 67 OG 99.2 68.9
REMARK 620 4 THR A 69 O 78.4 153.0 89.3
REMARK 620 5 GLU A 74 OE1 100.6 131.0 151.8 75.3
REMARK 620 6 GLU A 74 OE2 88.5 83.6 151.1 119.5 49.4
REMARK 620 7 HOH A 175 O 170.1 81.2 75.3 109.4 87.5 92.6
REMARK 620 N 1 2 3 4 5 6
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 103 OD1
REMARK 620 2 ASN A 105 OD1 74.3
REMARK 620 3 ASN A 105 ND2 112.3 41.5
REMARK 620 4 ASP A 107 OD1 84.0 70.1 90.4
REMARK 620 5 TYR A 109 O 100.7 150.4 144.6 80.5
REMARK 620 6 GLU A 114 OE1 114.0 131.0 98.9 154.1 78.0
REMARK 620 7 GLU A 114 OE2 92.7 79.3 62.3 149.0 130.2 52.9
REMARK 620 N 1 2 3 4 5 6
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 139 OD1
REMARK 620 2 ASN A 141 OD1 77.1
REMARK 620 3 ASP A 143 OD1 69.9 67.5
REMARK 620 4 ARG A 145 O 77.2 142.3 77.9
REMARK 620 5 GLU A 150 OE1 121.2 133.1 156.3 84.2
REMARK 620 6 GLU A 150 OE2 90.8 87.5 150.9 120.0 52.8
REMARK 620 7 HOH A 229 O 162.9 99.9 93.4 96.6 73.2 105.9
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 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 164
DBREF 1TCF A 1 159 UNP P02586 TNNC2_RABIT 1 159
SEQADV 1TCF LEU A 98 UNP P02586 CYS 98 ENGINEERED MUTATION
SEQRES 1 A 159 THR ASP GLN GLN ALA GLU ALA ARG SER TYR LEU SER GLU
SEQRES 2 A 159 GLU MET ILE ALA GLU PHE LYS ALA ALA PHE ASP MET PHE
SEQRES 3 A 159 ASP ALA ASP GLY GLY GLY ASP ILE SER VAL LYS GLU LEU
SEQRES 4 A 159 GLY THR VAL MET ARG MET LEU GLY GLN THR PRO THR LYS
SEQRES 5 A 159 GLU GLU LEU ASP ALA ILE ILE GLU GLU VAL ASP GLU ASP
SEQRES 6 A 159 GLY SER GLY THR ILE ASP PHE GLU GLU PHE LEU VAL MET
SEQRES 7 A 159 MET VAL ARG GLN MET LYS GLU ASP ALA LYS GLY LYS SER
SEQRES 8 A 159 GLU GLU GLU LEU ALA GLU LEU PHE ARG ILE PHE ASP ARG
SEQRES 9 A 159 ASN ALA ASP GLY TYR ILE ASP ALA GLU GLU LEU ALA GLU
SEQRES 10 A 159 ILE PHE ARG ALA SER GLY GLU HIS VAL THR ASP GLU GLU
SEQRES 11 A 159 ILE GLU SER LEU MET LYS ASP GLY ASP LYS ASN ASN ASP
SEQRES 12 A 159 GLY ARG ILE ASP PHE ASP GLU PHE LEU LYS MET MET GLU
SEQRES 13 A 159 GLY VAL GLN
HET CA A 160 1
HET CA A 161 1
HET CA A 162 1
HET CA A 163 1
HET CA A 164 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 5(CA 2+)
FORMUL 7 HOH *197(H2 O)
HELIX 1 1 ALA A 5 TYR A 10 1 6
HELIX 2 2 GLU A 13 PHE A 26 1 14
HELIX 3 3 VAL A 36 MET A 45 1 10
HELIX 4 4 LYS A 52 VAL A 62 1 11
HELIX 5 5 PHE A 72 MET A 83 1 12
HELIX 6 6 GLU A 93 PHE A 102 1 10
HELIX 7 7 ALA A 112 SER A 122 1 11
HELIX 8 8 ASP A 128 GLY A 138 1 11
HELIX 9 9 PHE A 148 GLU A 156 1 9
SHEET 1 A 2 ASP A 33 ILE A 34 0
SHEET 2 A 2 ILE A 70 ASP A 71 -1 O ILE A 70 N ILE A 34
LINK OE1 GLU A 14 CA CA A 164 1555 1555 2.49
LINK OE2 GLU A 14 CA CA A 164 1555 1555 2.36
LINK OD1 ASP A 27 CA CA A 160 1555 1555 2.32
LINK OD1 ASP A 29 CA CA A 160 1555 1555 2.30
LINK O ASP A 33 CA CA A 160 1555 1555 2.48
LINK OE1 GLU A 38 CA CA A 160 1555 1555 2.54
LINK OE2 GLU A 38 CA CA A 160 1555 1555 2.52
LINK OD1 ASP A 63 CA CA A 161 1555 1555 2.36
LINK OD1 ASP A 65 CA CA A 161 1555 1555 2.40
LINK OG SER A 67 CA CA A 161 1555 1555 2.24
LINK O THR A 69 CA CA A 161 1555 1555 2.46
LINK OE1 GLU A 74 CA CA A 161 1555 1555 2.68
LINK OE2 GLU A 74 CA CA A 161 1555 1555 2.54
LINK OD1 ASP A 103 CA CA A 162 1555 1555 2.49
LINK OD1 ASN A 105 CA CA A 162 1555 1555 2.43
LINK ND2 ASN A 105 CA CA A 162 1555 1555 3.37
LINK OD1 ASP A 107 CA CA A 162 1555 1555 2.45
LINK O TYR A 109 CA CA A 162 1555 1555 2.25
LINK OE1 GLU A 114 CA CA A 162 1555 1555 2.42
LINK OE2 GLU A 114 CA CA A 162 1555 1555 2.54
LINK OD1 ASP A 139 CA CA A 163 1555 1555 2.61
LINK OD1 ASN A 141 CA CA A 163 1555 1555 2.44
LINK OD1 ASP A 143 CA CA A 163 1555 1555 2.40
LINK O ARG A 145 CA CA A 163 1555 1555 2.61
LINK OE1 GLU A 150 CA CA A 163 1555 1555 2.55
LINK OE2 GLU A 150 CA CA A 163 1555 1555 2.31
LINK CA CA A 160 O HOH A 182 1555 1555 2.66
LINK CA CA A 160 O HOH A 215 1555 1555 2.49
LINK CA CA A 161 O HOH A 175 1555 1555 2.22
LINK CA CA A 163 O HOH A 229 1555 1555 2.45
LINK CA CA A 164 O HOH A 176 1555 1555 2.48
LINK CA CA A 164 O HOH A 219 1555 1555 2.46
SITE 1 AC1 6 ASP A 27 ASP A 29 ASP A 33 GLU A 38
SITE 2 AC1 6 HOH A 182 HOH A 215
SITE 1 AC2 6 ASP A 63 ASP A 65 SER A 67 THR A 69
SITE 2 AC2 6 GLU A 74 HOH A 175
SITE 1 AC3 5 ASP A 103 ASN A 105 ASP A 107 TYR A 109
SITE 2 AC3 5 GLU A 114
SITE 1 AC4 6 ASP A 139 ASN A 141 ASP A 143 ARG A 145
SITE 2 AC4 6 GLU A 150 HOH A 229
SITE 1 AC5 3 GLU A 14 HOH A 176 HOH A 219
CRYST1 32.100 59.600 48.000 90.00 101.10 90.00 P 1 21 1 2
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 0.031153 0.000000 0.006112 0.00000
SCALE2 0.000000 0.016779 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021231 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
