HEADER CONTRACTILE PROTEIN 03-DEC-02 1J1E
TITLE CRYSTAL STRUCTURE OF THE 52KDA DOMAIN OF HUMAN CARDIAC TROPONIN IN THE
TITLE 2 CA2+ SATURATED FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: TNC;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TROPONIN T;
COMPND 9 CHAIN: B, E;
COMPND 10 FRAGMENT: CNBR FRAGMENT, RESIDUES 183-288;
COMPND 11 SYNONYM: TNT;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: TROPONIN I;
COMPND 15 CHAIN: C, F;
COMPND 16 FRAGMENT: RESIDUES 31-210;
COMPND 17 SYNONYM: TNI;
COMPND 18 ENGINEERED: YES;
COMPND 19 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: CARDIAC MUSCLE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3D;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 TISSUE: CARDIAC MUSCLE;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET3D;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 TISSUE: CARDIAC MUSCLE;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS THIN FILAMENT, MUSCLE REGULATION, CA2+ BINDING PROTEIN, EF-HAND,
KEYWDS 2 COILED-COIL, CONTRACTILE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.TAKEDA,A.YAMASHITA,K.MAEDA,Y.MAEDA
REVDAT 4 25-OCT-23 1J1E 1 REMARK
REVDAT 3 10-NOV-21 1J1E 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1J1E 1 VERSN
REVDAT 1 15-JUL-03 1J1E 0
JRNL AUTH S.TAKEDA,A.YAMASHITA,K.MAEDA,Y.MAEDA
JRNL TITL STRUCTURE OF THE CORE DOMAIN OF HUMAN CARDIAC TROPONIN IN
JRNL TITL 2 THE CA2+-SATURATED FORM
JRNL REF NATURE V. 424 35 2003
JRNL REFN ISSN 0028-0836
JRNL PMID 12840750
JRNL DOI 10.1038/NATURE01780
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.TAKEDA,T.KOBAYASHI,H.TANIGUCHI,H.HAYASHI,Y.MAEDA
REMARK 1 TITL STRUCTURAL AND FUNCTIONAL DOMAINS OF THE TROPONIN COMPLEX
REMARK 1 TITL 2 REVEALED BY LIMITED DIGESTION
REMARK 1 REF EUR.J.BIOCHEM. V. 246 611 1997
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.G.VASSYLYEV,S.TAKEDA,S.WAKATSUKI,K.MAEDA,Y.MAEDA
REMARK 1 TITL CRYSTAL STRUCTURE OF TROPONIN C IN COMPLEX WITH TROPONIN I
REMARK 1 TITL 2 FRAGMENT AT 2.3-A RESOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 95 4847 1998
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.95.9.4847
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 16015
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) : 0.251
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 819
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.42
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.38
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1502
REMARK 3 BIN R VALUE (WORKING SET) : 0.3692
REMARK 3 BIN FREE R VALUE : 0.4003
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 0.59
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 94
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5854
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 91.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -17.31600
REMARK 3 B22 (A**2) : 9.37300
REMARK 3 B33 (A**2) : 7.94300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -6.36900
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM SIGMAA (A) : 0.55
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) : 0.59
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.78
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.19
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.400
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.24
REMARK 3 BSOL : 43.90
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000005508.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-01
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : KARKPATRIC-BOETZE TYPE RH-COATED
REMARK 200 DOUBLE MIRROR (SUPER MIRRORS)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16101
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.840
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: PDB_ENTRY 1J1D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, LITHIUM CHLORIDE, TRIS-HCL,
REMARK 280 CALCIUM CHLORIDE, GLYCEROL, PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
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 84.75300
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: CHAIN A, B AND C, AND CHAIN D, E AND F ARE BIOLOGICAL
REMARK 300 HETEROTRIMER ASSEMBLIES, RESPECTIVELY.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 SER A 89
REMARK 465 LYS A 90
REMARK 465 GLY A 91
REMARK 465 HIS B 183
REMARK 465 PHE B 184
REMARK 465 GLY B 185
REMARK 465 GLY B 186
REMARK 465 TYR B 187
REMARK 465 ILE B 188
REMARK 465 GLN B 189
REMARK 465 LYS B 190
REMARK 465 GLN B 191
REMARK 465 ALA B 192
REMARK 465 GLN B 193
REMARK 465 THR B 194
REMARK 465 GLU B 195
REMARK 465 ARG B 196
REMARK 465 LYS B 197
REMARK 465 SER B 198
REMARK 465 GLY B 199
REMARK 465 LYS B 200
REMARK 465 ARG B 201
REMARK 465 GLN B 202
REMARK 465 GLN B 272
REMARK 465 LYS B 273
REMARK 465 VAL B 274
REMARK 465 SER B 275
REMARK 465 LYS B 276
REMARK 465 THR B 277
REMARK 465 ARG B 278
REMARK 465 GLY B 279
REMARK 465 LYS B 280
REMARK 465 ALA B 281
REMARK 465 LYS B 282
REMARK 465 VAL B 283
REMARK 465 THR B 284
REMARK 465 GLY B 285
REMARK 465 ARG B 286
REMARK 465 TRP B 287
REMARK 465 LYS B 288
REMARK 465 MET C 31
REMARK 465 GLU C 32
REMARK 465 PRO C 33
REMARK 465 HIS C 34
REMARK 465 GLY C 137
REMARK 465 LYS C 138
REMARK 465 PHE C 139
REMARK 465 LYS C 140
REMARK 465 ARG C 141
REMARK 465 PRO C 142
REMARK 465 THR C 143
REMARK 465 LEU C 144
REMARK 465 ARG C 145
REMARK 465 ARG C 146
REMARK 465 ALA C 163
REMARK 465 LYS C 164
REMARK 465 GLU C 165
REMARK 465 SER C 166
REMARK 465 LEU C 167
REMARK 465 ASP C 168
REMARK 465 LEU C 169
REMARK 465 ARG C 170
REMARK 465 ALA C 171
REMARK 465 HIS C 172
REMARK 465 LEU C 173
REMARK 465 LYS C 174
REMARK 465 GLN C 175
REMARK 465 VAL C 176
REMARK 465 LYS C 177
REMARK 465 LYS C 178
REMARK 465 GLU C 179
REMARK 465 ASP C 180
REMARK 465 THR C 181
REMARK 465 GLU C 182
REMARK 465 LYS C 183
REMARK 465 GLU C 184
REMARK 465 ASN C 185
REMARK 465 ARG C 186
REMARK 465 GLU C 187
REMARK 465 VAL C 188
REMARK 465 GLY C 189
REMARK 465 ASP C 190
REMARK 465 TRP C 191
REMARK 465 ARG C 192
REMARK 465 LYS C 193
REMARK 465 ASN C 194
REMARK 465 ILE C 195
REMARK 465 ASP C 196
REMARK 465 ALA C 197
REMARK 465 LEU C 198
REMARK 465 SER C 199
REMARK 465 GLY C 200
REMARK 465 MET C 201
REMARK 465 GLU C 202
REMARK 465 GLY C 203
REMARK 465 ARG C 204
REMARK 465 LYS C 205
REMARK 465 LYS C 206
REMARK 465 LYS C 207
REMARK 465 PHE C 208
REMARK 465 GLU C 209
REMARK 465 SER C 210
REMARK 465 GLY D 49
REMARK 465 GLN D 50
REMARK 465 HIS E 183
REMARK 465 PHE E 184
REMARK 465 GLY E 185
REMARK 465 GLY E 186
REMARK 465 TYR E 187
REMARK 465 ILE E 188
REMARK 465 GLN E 189
REMARK 465 LYS E 190
REMARK 465 GLN E 191
REMARK 465 ALA E 192
REMARK 465 GLN E 193
REMARK 465 THR E 194
REMARK 465 GLU E 195
REMARK 465 ARG E 196
REMARK 465 LYS E 197
REMARK 465 SER E 198
REMARK 465 GLY E 199
REMARK 465 LYS E 200
REMARK 465 ARG E 201
REMARK 465 THR E 277
REMARK 465 ARG E 278
REMARK 465 GLY E 279
REMARK 465 LYS E 280
REMARK 465 ALA E 281
REMARK 465 LYS E 282
REMARK 465 VAL E 283
REMARK 465 THR E 284
REMARK 465 GLY E 285
REMARK 465 ARG E 286
REMARK 465 TRP E 287
REMARK 465 LYS E 288
REMARK 465 MET F 31
REMARK 465 GLU F 32
REMARK 465 PRO F 33
REMARK 465 HIS F 34
REMARK 465 ALA F 35
REMARK 465 LYS F 36
REMARK 465 LYS F 37
REMARK 465 LYS F 38
REMARK 465 SER F 39
REMARK 465 GLY F 137
REMARK 465 LYS F 138
REMARK 465 PHE F 139
REMARK 465 LYS F 140
REMARK 465 ARG F 141
REMARK 465 PRO F 142
REMARK 465 THR F 143
REMARK 465 LEU F 144
REMARK 465 ARG F 145
REMARK 465 ARG F 146
REMARK 465 VAL F 147
REMARK 465 ARG F 192
REMARK 465 LYS F 193
REMARK 465 ASN F 194
REMARK 465 ILE F 195
REMARK 465 ASP F 196
REMARK 465 ALA F 197
REMARK 465 LEU F 198
REMARK 465 SER F 199
REMARK 465 GLY F 200
REMARK 465 MET F 201
REMARK 465 GLU F 202
REMARK 465 GLY F 203
REMARK 465 ARG F 204
REMARK 465 LYS F 205
REMARK 465 LYS F 206
REMARK 465 LYS F 207
REMARK 465 PHE F 208
REMARK 465 GLU F 209
REMARK 465 SER F 210
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 GLU A 32 -71.47 -51.66
REMARK 500 ASN A 51 59.57 -157.30
REMARK 500 SER A 84 2.85 -67.50
REMARK 500 MET A 85 -82.23 -45.02
REMARK 500 ASP A 105 86.76 -59.70
REMARK 500 THR A 127 92.57 -65.67
REMARK 500 GLU B 226 -52.05 -26.66
REMARK 500 ALA C 80 53.39 -91.15
REMARK 500 GLN C 81 151.54 -40.89
REMARK 500 ALA C 86 -44.64 -24.81
REMARK 500 LEU D 12 114.47 -34.26
REMARK 500 PRO D 52 -176.83 -63.76
REMARK 500 SER D 69 -0.95 -58.30
REMARK 500 SER D 89 91.21 -65.72
REMARK 500 ASP D 105 83.89 -66.12
REMARK 500 ALA D 123 -10.80 -49.83
REMARK 500 ASP D 141 67.68 -65.78
REMARK 500 ASN D 144 62.71 65.60
REMARK 500 ASP D 149 -163.92 -73.48
REMARK 500 ASP E 222 -8.03 -55.90
REMARK 500 ASN E 271 5.25 -68.26
REMARK 500 SER F 42 109.64 -39.27
REMARK 500 PRO F 82 155.45 -48.56
REMARK 500 LEU F 88 -72.98 -73.71
REMARK 500 ASP F 190 -118.49 -101.25
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 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 65 OD2
REMARK 620 2 ASP A 67 OD2 62.3
REMARK 620 3 ASP A 67 OD1 105.7 43.6
REMARK 620 4 SER A 69 OG 68.1 77.2 89.0
REMARK 620 5 THR A 71 O 83.6 131.7 140.1 58.0
REMARK 620 6 ASP A 73 OD2 138.2 112.0 82.9 153.6 116.1
REMARK 620 7 GLU A 76 OE1 74.2 86.5 102.3 142.3 117.5 64.1
REMARK 620 8 GLU A 76 OE2 93.4 139.0 144.4 126.3 70.5 63.4 53.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 105 OD1
REMARK 620 2 ASN A 107 OD1 61.7
REMARK 620 3 ASN A 107 ND2 95.0 40.1
REMARK 620 4 ASP A 109 OD1 98.8 78.2 48.1
REMARK 620 5 ASP A 109 OD2 57.4 73.0 71.3 44.1
REMARK 620 6 TYR A 111 O 74.4 128.8 129.4 84.0 61.3
REMARK 620 7 GLU A 116 OE1 95.2 134.0 158.5 147.5 129.9 71.7
REMARK 620 8 GLU A 116 OE2 83.0 76.6 102.0 150.1 138.1 124.6 60.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 OD2
REMARK 620 2 ASN A 143 OD1 69.5
REMARK 620 3 ASN A 143 ND2 118.5 52.1
REMARK 620 4 ASP A 145 OD2 110.8 60.6 57.5
REMARK 620 5 ASP A 145 OD1 82.7 76.3 99.0 42.8
REMARK 620 6 ARG A 147 O 96.2 129.3 133.5 82.6 53.3
REMARK 620 7 GLU A 152 OE1 120.9 134.3 92.1 128.1 144.7 95.4
REMARK 620 8 GLU A 152 OE2 98.0 80.2 58.3 115.8 154.6 150.4 55.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 65 OD2
REMARK 620 2 ASP D 67 OD2 84.0
REMARK 620 3 ASP D 67 OD1 123.2 39.5
REMARK 620 4 SER D 69 OG 103.8 75.0 72.5
REMARK 620 5 THR D 71 O 80.5 136.7 139.6 70.0
REMARK 620 6 ASP D 73 OD2 159.6 92.2 54.0 94.5 114.8
REMARK 620 7 GLU D 76 OE1 94.2 103.5 94.5 161.6 117.7 67.1
REMARK 620 8 GLU D 76 OE2 105.1 158.6 126.2 120.0 64.5 72.5 57.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 105 OD2
REMARK 620 2 ASN D 107 OD1 66.5
REMARK 620 3 ASN D 107 ND2 117.1 51.5
REMARK 620 4 ASP D 109 OD1 77.7 66.1 86.3
REMARK 620 5 TYR D 111 O 74.2 132.9 161.2 81.4
REMARK 620 6 GLU D 116 OE1 82.4 72.5 70.8 138.4 127.3
REMARK 620 7 GLU D 116 OE2 78.2 112.9 114.2 153.6 82.0 46.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 141 OD2
REMARK 620 2 ASN D 143 OD1 88.4
REMARK 620 3 ASN D 143 ND2 124.1 41.3
REMARK 620 4 ASP D 145 OD1 112.7 80.9 51.1
REMARK 620 5 ASP D 145 OD2 73.8 96.8 87.6 42.8
REMARK 620 6 ARG D 147 O 68.8 153.2 145.5 94.8 64.2
REMARK 620 7 GLU D 152 OE1 99.6 66.3 82.7 132.9 162.4 129.5
REMARK 620 8 GLU D 152 OE2 90.1 116.3 128.1 152.6 142.9 78.9 51.3
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 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J1D RELATED DB: PDB
REMARK 900 46 KD DOMAIN OF SAME PROTEIN AT 2.61 ANGSTROM
DBREF 1J1E A 1 161 UNP P63316 TNNC1_HUMAN 1 161
DBREF 1J1E B 183 288 UNP P45379 TNNT2_HUMAN 183 288
DBREF 1J1E C 31 210 UNP P19429 TNNI3_HUMAN 30 209
DBREF 1J1E D 1 161 UNP P63316 TNNC1_HUMAN 1 161
DBREF 1J1E E 183 288 UNP P45379 TNNT2_HUMAN 183 288
DBREF 1J1E F 31 210 UNP P19429 TNNI3_HUMAN 30 209
SEQADV 1J1E SER A 35 UNP P63316 CYS 35 ENGINEERED MUTATION
SEQADV 1J1E SER A 84 UNP P63316 CYS 84 ENGINEERED MUTATION
SEQADV 1J1E MET C 31 UNP P19429 THR 30 ENGINEERED MUTATION
SEQADV 1J1E ALA C 80 UNP P19429 CYS 79 ENGINEERED MUTATION
SEQADV 1J1E ALA C 97 UNP P19429 CYS 96 ENGINEERED MUTATION
SEQADV 1J1E SER D 35 UNP P63316 CYS 35 ENGINEERED MUTATION
SEQADV 1J1E SER D 84 UNP P63316 CYS 84 ENGINEERED MUTATION
SEQADV 1J1E MET F 31 UNP P19429 THR 30 ENGINEERED MUTATION
SEQADV 1J1E ALA F 80 UNP P19429 CYS 79 ENGINEERED MUTATION
SEQADV 1J1E ALA F 97 UNP P19429 CYS 96 ENGINEERED MUTATION
SEQRES 1 A 161 MET ASP 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 SER 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
SEQRES 1 B 106 HIS PHE GLY GLY TYR ILE GLN LYS GLN ALA GLN THR GLU
SEQRES 2 B 106 ARG LYS SER GLY LYS ARG GLN THR GLU ARG GLU LYS LYS
SEQRES 3 B 106 LYS LYS ILE LEU ALA GLU ARG ARG LYS VAL LEU ALA ILE
SEQRES 4 B 106 ASP HIS LEU ASN GLU ASP GLN LEU ARG GLU LYS ALA LYS
SEQRES 5 B 106 GLU LEU TRP GLN THR ILE TYR ASN LEU GLU ALA GLU LYS
SEQRES 6 B 106 PHE ASP LEU GLN GLU LYS PHE LYS GLN GLN LYS TYR GLU
SEQRES 7 B 106 ILE ASN VAL LEU ARG ASN ARG ILE ASN ASP ASN GLN LYS
SEQRES 8 B 106 VAL SER LYS THR ARG GLY LYS ALA LYS VAL THR GLY ARG
SEQRES 9 B 106 TRP LYS
SEQRES 1 C 180 MET GLU PRO HIS ALA LYS LYS LYS SER LYS ILE SER ALA
SEQRES 2 C 180 SER ARG LYS LEU GLN LEU LYS THR LEU LEU LEU GLN ILE
SEQRES 3 C 180 ALA LYS GLN GLU LEU GLU ARG GLU ALA GLU GLU ARG ARG
SEQRES 4 C 180 GLY GLU LYS GLY ARG ALA LEU SER THR ARG ALA GLN PRO
SEQRES 5 C 180 LEU GLU LEU ALA GLY LEU GLY PHE ALA GLU LEU GLN ASP
SEQRES 6 C 180 LEU ALA ARG GLN LEU HIS ALA ARG VAL ASP LYS VAL ASP
SEQRES 7 C 180 GLU GLU ARG TYR ASP ILE GLU ALA LYS VAL THR LYS ASN
SEQRES 8 C 180 ILE THR GLU ILE ALA ASP LEU THR GLN LYS ILE PHE ASP
SEQRES 9 C 180 LEU ARG GLY LYS PHE LYS ARG PRO THR LEU ARG ARG VAL
SEQRES 10 C 180 ARG ILE SER ALA ASP ALA MET MET GLN ALA LEU LEU GLY
SEQRES 11 C 180 ALA ARG ALA LYS GLU SER LEU ASP LEU ARG ALA HIS LEU
SEQRES 12 C 180 LYS GLN VAL LYS LYS GLU ASP THR GLU LYS GLU ASN ARG
SEQRES 13 C 180 GLU VAL GLY ASP TRP ARG LYS ASN ILE ASP ALA LEU SER
SEQRES 14 C 180 GLY MET GLU GLY ARG LYS LYS LYS PHE GLU SER
SEQRES 1 D 161 MET ASP ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR
SEQRES 2 D 161 GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE
SEQRES 3 D 161 PHE VAL LEU GLY ALA GLU ASP GLY SER ILE SER THR LYS
SEQRES 4 D 161 GLU LEU GLY LYS VAL MET ARG MET LEU GLY GLN ASN PRO
SEQRES 5 D 161 THR PRO GLU GLU LEU GLN GLU MET ILE ASP GLU VAL ASP
SEQRES 6 D 161 GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU
SEQRES 7 D 161 VAL MET MET VAL ARG SER MET LYS ASP ASP SER LYS GLY
SEQRES 8 D 161 LYS SER GLU GLU GLU LEU SER ASP LEU PHE ARG MET PHE
SEQRES 9 D 161 ASP LYS ASN ALA ASP GLY TYR ILE ASP LEU GLU GLU LEU
SEQRES 10 D 161 LYS ILE MET LEU GLN ALA THR GLY GLU THR ILE THR GLU
SEQRES 11 D 161 ASP ASP ILE GLU GLU LEU MET LYS ASP GLY ASP LYS ASN
SEQRES 12 D 161 ASN ASP GLY ARG ILE ASP TYR ASP GLU PHE LEU GLU PHE
SEQRES 13 D 161 MET LYS GLY VAL GLU
SEQRES 1 E 106 HIS PHE GLY GLY TYR ILE GLN LYS GLN ALA GLN THR GLU
SEQRES 2 E 106 ARG LYS SER GLY LYS ARG GLN THR GLU ARG GLU LYS LYS
SEQRES 3 E 106 LYS LYS ILE LEU ALA GLU ARG ARG LYS VAL LEU ALA ILE
SEQRES 4 E 106 ASP HIS LEU ASN GLU ASP GLN LEU ARG GLU LYS ALA LYS
SEQRES 5 E 106 GLU LEU TRP GLN THR ILE TYR ASN LEU GLU ALA GLU LYS
SEQRES 6 E 106 PHE ASP LEU GLN GLU LYS PHE LYS GLN GLN LYS TYR GLU
SEQRES 7 E 106 ILE ASN VAL LEU ARG ASN ARG ILE ASN ASP ASN GLN LYS
SEQRES 8 E 106 VAL SER LYS THR ARG GLY LYS ALA LYS VAL THR GLY ARG
SEQRES 9 E 106 TRP LYS
SEQRES 1 F 180 MET GLU PRO HIS ALA LYS LYS LYS SER LYS ILE SER ALA
SEQRES 2 F 180 SER ARG LYS LEU GLN LEU LYS THR LEU LEU LEU GLN ILE
SEQRES 3 F 180 ALA LYS GLN GLU LEU GLU ARG GLU ALA GLU GLU ARG ARG
SEQRES 4 F 180 GLY GLU LYS GLY ARG ALA LEU SER THR ARG ALA GLN PRO
SEQRES 5 F 180 LEU GLU LEU ALA GLY LEU GLY PHE ALA GLU LEU GLN ASP
SEQRES 6 F 180 LEU ALA ARG GLN LEU HIS ALA ARG VAL ASP LYS VAL ASP
SEQRES 7 F 180 GLU GLU ARG TYR ASP ILE GLU ALA LYS VAL THR LYS ASN
SEQRES 8 F 180 ILE THR GLU ILE ALA ASP LEU THR GLN LYS ILE PHE ASP
SEQRES 9 F 180 LEU ARG GLY LYS PHE LYS ARG PRO THR LEU ARG ARG VAL
SEQRES 10 F 180 ARG ILE SER ALA ASP ALA MET MET GLN ALA LEU LEU GLY
SEQRES 11 F 180 ALA ARG ALA LYS GLU SER LEU ASP LEU ARG ALA HIS LEU
SEQRES 12 F 180 LYS GLN VAL LYS LYS GLU ASP THR GLU LYS GLU ASN ARG
SEQRES 13 F 180 GLU VAL GLY ASP TRP ARG LYS ASN ILE ASP ALA LEU SER
SEQRES 14 F 180 GLY MET GLU GLY ARG LYS LYS LYS PHE GLU SER
HET CA A 201 1
HET CA A 202 1
HET CA A 203 1
HET CA D 201 1
HET CA D 202 1
HET CA D 203 1
HETNAM CA CALCIUM ION
FORMUL 7 CA 6(CA 2+)
HELIX 1 1 ASP A 3 GLN A 11 1 9
HELIX 2 2 THR A 13 VAL A 28 1 16
HELIX 3 3 SER A 37 ARG A 46 1 10
HELIX 4 4 MET A 47 GLY A 49 5 3
HELIX 5 5 THR A 53 GLU A 63 1 11
HELIX 6 6 ASP A 73 SER A 84 1 12
HELIX 7 7 SER A 93 ASP A 105 1 13
HELIX 8 8 LEU A 114 THR A 124 1 11
HELIX 9 9 THR A 129 ASP A 141 1 13
HELIX 10 10 TYR A 150 LYS A 158 1 9
HELIX 11 11 THR B 203 ASP B 222 1 20
HELIX 12 12 ASN B 225 ASN B 271 1 47
HELIX 13 13 SER C 42 ALA C 80 1 39
HELIX 14 14 GLU C 84 LEU C 88 5 5
HELIX 15 15 GLY C 89 ARG C 136 1 48
HELIX 16 16 SER C 150 GLY C 160 1 11
HELIX 17 17 ASP D 2 GLU D 10 1 9
HELIX 18 18 THR D 13 LEU D 29 1 17
HELIX 19 19 SER D 37 LEU D 48 1 12
HELIX 20 20 THR D 53 ASP D 65 1 13
HELIX 21 21 ASP D 73 LYS D 86 1 14
HELIX 22 22 SER D 93 ASP D 105 1 13
HELIX 23 23 LEU D 114 THR D 124 1 11
HELIX 24 24 THR D 129 ASP D 141 1 13
HELIX 25 25 ASP D 149 PHE D 156 1 8
HELIX 26 26 GLN E 202 ASP E 222 1 21
HELIX 27 27 ASN E 225 VAL E 274 1 50
HELIX 28 28 SER F 42 GLN F 81 1 40
HELIX 29 29 GLY F 89 ARG F 136 1 48
HELIX 30 30 SER F 150 GLY F 160 1 11
HELIX 31 31 GLY F 160 GLY F 189 1 30
SHEET 1 A 2 TYR A 111 ASP A 113 0
SHEET 2 A 2 ARG A 147 ASP A 149 -1 O ILE A 148 N ILE A 112
SHEET 1 B 2 ILE D 112 ASP D 113 0
SHEET 2 B 2 ARG D 147 ILE D 148 -1 O ILE D 148 N ILE D 112
LINK OD2 ASP A 65 CA CA A 201 1555 1555 2.95
LINK OD2 ASP A 67 CA CA A 201 1555 1555 2.08
LINK OD1 ASP A 67 CA CA A 201 1555 1555 3.17
LINK OG SER A 69 CA CA A 201 1555 1555 2.25
LINK O THR A 71 CA CA A 201 1555 1555 2.91
LINK OD2 ASP A 73 CA CA A 201 1555 1555 3.32
LINK OE1 GLU A 76 CA CA A 201 1555 1555 2.44
LINK OE2 GLU A 76 CA CA A 201 1555 1555 2.38
LINK OD1 ASP A 105 CA CA A 202 1555 1555 2.85
LINK OD1 ASN A 107 CA CA A 202 1555 1555 1.90
LINK ND2 ASN A 107 CA CA A 202 1555 1555 3.34
LINK OD1 ASP A 109 CA CA A 202 1555 1555 3.06
LINK OD2 ASP A 109 CA CA A 202 1555 1555 2.72
LINK O TYR A 111 CA CA A 202 1555 1555 2.54
LINK OE1 GLU A 116 CA CA A 202 1555 1555 2.17
LINK OE2 GLU A 116 CA CA A 202 1555 1555 2.17
LINK OD2 ASP A 141 CA CA A 203 1555 1555 2.04
LINK OD1 ASN A 143 CA CA A 203 1555 1555 2.27
LINK ND2 ASN A 143 CA CA A 203 1555 1555 2.73
LINK OD2 ASP A 145 CA CA A 203 1555 1555 3.16
LINK OD1 ASP A 145 CA CA A 203 1555 1555 2.75
LINK O ARG A 147 CA CA A 203 1555 1555 2.52
LINK OE1 GLU A 152 CA CA A 203 1555 1555 2.08
LINK OE2 GLU A 152 CA CA A 203 1555 1555 2.57
LINK OD2 ASP D 65 CA CA D 201 1555 1555 2.25
LINK OD2 ASP D 67 CA CA D 201 1555 1555 2.00
LINK OD1 ASP D 67 CA CA D 201 1555 1555 3.33
LINK OG SER D 69 CA CA D 201 1555 1555 2.50
LINK O THR D 71 CA CA D 201 1555 1555 2.78
LINK OD2 ASP D 73 CA CA D 201 1555 1555 3.01
LINK OE1 GLU D 76 CA CA D 201 1555 1555 2.16
LINK OE2 GLU D 76 CA CA D 201 1555 1555 2.41
LINK OD2 ASP D 105 CA CA D 202 1555 1555 2.50
LINK OD1 ASN D 107 CA CA D 202 1555 1555 2.24
LINK ND2 ASN D 107 CA CA D 202 1555 1555 2.79
LINK OD1 ASP D 109 CA CA D 202 1555 1555 2.16
LINK O TYR D 111 CA CA D 202 1555 1555 2.38
LINK OE1 GLU D 116 CA CA D 202 1555 1555 2.83
LINK OE2 GLU D 116 CA CA D 202 1555 1555 2.66
LINK OD2 ASP D 141 CA CA D 203 1555 1555 2.99
LINK OD1 ASN D 143 CA CA D 203 1555 1555 2.23
LINK ND2 ASN D 143 CA CA D 203 1555 1555 3.37
LINK OD1 ASP D 145 CA CA D 203 1555 1555 3.22
LINK OD2 ASP D 145 CA CA D 203 1555 1555 2.45
LINK O ARG D 147 CA CA D 203 1555 1555 2.35
LINK OE1 GLU D 152 CA CA D 203 1555 1555 2.55
LINK OE2 GLU D 152 CA CA D 203 1555 1555 2.53
SITE 1 AC1 6 ASP A 65 ASP A 67 SER A 69 THR A 71
SITE 2 AC1 6 ASP A 73 GLU A 76
SITE 1 AC2 6 ASP A 105 ASN A 107 ASP A 109 TYR A 111
SITE 2 AC2 6 ASP A 113 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
SITE 1 AC4 6 ASP D 65 ASP D 67 SER D 69 THR D 71
SITE 2 AC4 6 ASP D 73 GLU D 76
SITE 1 AC5 5 ASP D 105 ASN D 107 ASP D 109 TYR D 111
SITE 2 AC5 5 GLU D 116
SITE 1 AC6 5 ASP D 141 ASN D 143 ASP D 145 ARG D 147
SITE 2 AC6 5 GLU D 152
CRYST1 48.299 169.506 68.538 90.00 102.38 90.00 P 1 21 1 4
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 0.020704 0.000000 0.004545 0.00000
SCALE2 0.000000 0.005899 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014938 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
