HEADER CALCIUM-BINDING PROTEIN 02-JUN-96 1NCX
TITLE TROPONIN C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: SKELETAL;
SOURCE 6 TISSUE: SKELETAL MUSCLE
KEYWDS MUSCLE PROTEIN, CALCIUM-BINDING PROTEIN, DUPLICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SUNDARALINGAM,S.T.RAO
REVDAT 3 14-FEB-24 1NCX 1 REMARK LINK
REVDAT 2 24-FEB-09 1NCX 1 VERSN
REVDAT 1 07-DEC-96 1NCX 0
JRNL AUTH S.T.RAO,K.A.SATYSHUR,M.L.GREASER,M.SUNDARALINGAM
JRNL TITL X-RAY STRUCTURES OF MN, CD AND TB METAL COMPLEXES OF
JRNL TITL 2 TROPONIN C.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 52 916 1996
JRNL REFN ISSN 0907-4449
JRNL PMID 15299599
JRNL DOI 10.1107/S0907444996006166
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.A.SATYSHUR,D.PYZALSKA,S.T.RAO,M.GREASER,M.SUNDARALINGAM
REMARK 1 TITL STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN-C AT 1.78
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 50 40 1994
REMARK 1 REFN ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.A.SATYSHUR,S.T.RAO,D.PYZALSKA,W.DRENDEL,M.GREASER,
REMARK 1 AUTH 2 M.SUNDARALINGAM
REMARK 1 TITL REFINED STRUCTURE OF CHICKEN SKELETAL MUSCLE TROPONIN C IN
REMARK 1 TITL 2 THE TWO-CALCIUM STATE AT 2-A RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 263 1628 1988
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.SUNDARALINGAM,R.BERGSTROM,G.STRASBURG,S.T.RAO,
REMARK 1 AUTH 2 P.ROYCHOWDHURY,M.GREASER,B.C.WANG
REMARK 1 TITL MOLECULAR STRUCTURE OF TROPONIN C FROM CHICKEN SKELETAL
REMARK 1 TITL 2 MUSCLE AT 3-ANGSTROM RESOLUTION
REMARK 1 REF SCIENCE V. 227 945 1985
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.M.STRASBURG,M.L.GREASER,M.SUNDARALINGAM
REMARK 1 TITL X-RAY DIFFRACTION STUDIES OF TROPONIN-C CRYSTALS FROM RABBIT
REMARK 1 TITL 2 AND CHICKEN SKELETAL MUSCLES
REMARK 1 REF J.BIOL.CHEM. V. 255 3806 1980
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.M.WILKINSON
REMARK 1 TITL THE AMINO ACID SEQUENCE OF TROPONIN C FROM CHICKEN SKELETAL
REMARK 1 TITL 2 MUSCLE
REMARK 1 REF FEBS LETT. V. 70 254 1976
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 12762
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1271
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.018 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.049 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.005 ; 0.010
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.005 ; 0.010
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.042 ; 5.000
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 1.800 ; 5.000
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.900 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.900 ; 6.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.900 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.900 ; 6.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NCX 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_1000175240.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IN-HOUSE SOFTWARE
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29532
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 8.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.06000
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.53333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 20.26667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 20.26667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.53333
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 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 OD2 ASP A 152 O HOH A 319 1.86
REMARK 500 ND2 ASN A 100 O HOH A 375 1.88
REMARK 500 O LYS A 156 O GLN A 162 1.97
REMARK 500 O HOH A 241 O HOH A 263 1.97
REMARK 500 OD1 ASP A 89 O HOH A 372 2.04
REMARK 500 OE1 GLU A 97 O HOH A 375 2.06
REMARK 500 OD1 ASP A 152 O HOH A 291 2.09
REMARK 500 O HOH A 284 O HOH A 364 2.09
REMARK 500 O HOH A 281 O HOH A 363 2.11
REMARK 500 OD2 ASP A 30 O HOH A 339 2.11
REMARK 500 OD1 ASP A 66 O HOH A 197 2.19
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 HOH A 363 O HOH A 364 2664 2.00
REMARK 500 O HOH A 203 O HOH A 322 3565 2.04
REMARK 500 OE2 GLU A 63 OD2 ASP A 140 2665 2.16
REMARK 500 NZ LYS A 40 NZ LYS A 143 2665 2.18
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 127 CD GLU A 127 OE2 -0.067
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 ARG A 11 NH1 - CZ - NH2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 PHE A 22 CZ - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG A 47 CD - NE - CZ ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG A 47 NH1 - CZ - NH2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 GLU A 64 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ASP A 74 CB - CG - OD1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 PHE A 75 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 GLU A 77 CG - CD - OE1 ANGL. DEV. = 13.4 DEGREES
REMARK 500 PHE A 78 CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 84 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 89 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 GLU A 96 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 GLU A 97 OE1 - CD - OE2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 GLU A 97 CG - CD - OE2 ANGL. DEV. = 14.2 DEGREES
REMARK 500 CYS A 101 CA - CB - SG ANGL. DEV. = 14.1 DEGREES
REMARK 500 ASP A 106 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ILE A 115 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 ILE A 115 N - CA - CB ANGL. DEV. = 16.0 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 HIS A 128 CA - CB - CG ANGL. DEV. = -11.1 DEGREES
REMARK 500 GLU A 132 OE1 - CD - OE2 ANGL. DEV. = 12.9 DEGREES
REMARK 500 ASP A 142 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 148 CD - NE - CZ ANGL. DEV. = 21.9 DEGREES
REMARK 500 ARG A 148 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 PHE A 151 CB - CG - CD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 152 CB - CG - OD1 ANGL. DEV. = -9.0 DEGREES
REMARK 500 ASP A 152 CB - CG - OD2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 GLN A 162 CA - C - O ANGL. DEV. = -14.2 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 30 -81.45 -83.36
REMARK 500 ALA A 31 -53.86 93.45
REMARK 500 ASP A 66 44.22 -105.28
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 CD A 163 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 106 OD1
REMARK 620 2 ASN A 108 OD1 81.4
REMARK 620 3 ASP A 110 OD1 85.6 77.5
REMARK 620 4 PHE A 112 O 86.1 155.6 80.7
REMARK 620 5 GLU A 117 OE1 115.4 122.7 151.4 81.6
REMARK 620 6 GLU A 117 OE2 97.7 74.4 150.8 128.4 50.2
REMARK 620 7 HOH A 176 O 162.1 92.2 76.7 93.4 82.1 96.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 164 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 142 OD1
REMARK 620 2 ASN A 144 OD1 81.3
REMARK 620 3 ASP A 146 OD1 83.7 79.4
REMARK 620 4 ARG A 148 O 87.5 156.4 78.8
REMARK 620 5 GLU A 153 OE2 89.8 74.6 153.9 126.3
REMARK 620 6 GLU A 153 OE1 113.5 121.4 153.7 82.1 50.6
REMARK 620 7 HOH A 209 O 162.8 92.9 79.3 91.8 104.4 83.4
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 CD A 163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 225
DBREF 1NCX A 1 162 UNP P02588 TNNC2_CHICK 1 162
SEQRES 1 A 162 ALA SER MET THR ASP GLN GLN ALA GLU ALA ARG ALA PHE
SEQRES 2 A 162 LEU SER GLU GLU MET ILE ALA GLU PHE LYS ALA ALA PHE
SEQRES 3 A 162 ASP MET PHE ASP ALA ASP GLY GLY GLY ASP ILE SER THR
SEQRES 4 A 162 LYS GLU LEU GLY THR VAL MET ARG MET LEU GLY GLN ASN
SEQRES 5 A 162 PRO THR LYS GLU GLU LEU ASP ALA ILE ILE GLU GLU VAL
SEQRES 6 A 162 ASP GLU ASP GLY SER GLY THR ILE ASP PHE GLU GLU PHE
SEQRES 7 A 162 LEU VAL MET MET VAL ARG GLN MET LYS GLU ASP ALA LYS
SEQRES 8 A 162 GLY LYS SER GLU GLU GLU LEU ALA ASN CYS PHE ARG ILE
SEQRES 9 A 162 PHE ASP LYS ASN ALA ASP GLY PHE ILE ASP ILE GLU GLU
SEQRES 10 A 162 LEU GLY GLU ILE LEU ARG ALA THR GLY GLU HIS VAL THR
SEQRES 11 A 162 GLU GLU ASP ILE GLU ASP LEU MET LYS ASP SER ASP LYS
SEQRES 12 A 162 ASN ASN ASP GLY ARG ILE ASP PHE ASP GLU PHE LEU LYS
SEQRES 13 A 162 MET MET GLU GLY VAL GLN
HET CD A 163 1
HET CD A 164 1
HET SO4 A 225 5
HETNAM CD CADMIUM ION
HETNAM SO4 SULFATE ION
FORMUL 2 CD 2(CD 2+)
FORMUL 4 SO4 O4 S 2-
FORMUL 5 HOH *155(H2 O)
HELIX 1 1 MET A 3 PHE A 13 1 11
HELIX 2 2 GLU A 16 PHE A 29 1 14
HELIX 3 3 THR A 39 MET A 48 5 10
HELIX 4 4 LYS A 55 VAL A 65 1 11
HELIX 5 5 PHE A 75 PHE A 105 1 31
HELIX 6 6 ILE A 115 THR A 125 1 11
HELIX 7 7 GLU A 131 SER A 141 1 11
HELIX 8 8 PHE A 151 GLU A 159 1 9
SHEET 1 A 2 ASP A 36 SER A 38 0
SHEET 2 A 2 THR A 72 ASP A 74 -1 N ILE A 73 O ILE A 37
LINK OD1 ASP A 106 CD CD A 163 1555 1555 2.03
LINK OD1 ASN A 108 CD CD A 163 1555 1555 2.33
LINK OD1 ASP A 110 CD CD A 163 1555 1555 2.29
LINK O PHE A 112 CD CD A 163 1555 1555 2.32
LINK OE1 GLU A 117 CD CD A 163 1555 1555 2.47
LINK OE2 GLU A 117 CD CD A 163 1555 1555 2.51
LINK OD1 ASP A 142 CD CD A 164 1555 1555 2.11
LINK OD1 ASN A 144 CD CD A 164 1555 1555 2.37
LINK OD1 ASP A 146 CD CD A 164 1555 1555 2.30
LINK O ARG A 148 CD CD A 164 1555 1555 2.32
LINK OE2 GLU A 153 CD CD A 164 1555 1555 2.63
LINK OE1 GLU A 153 CD CD A 164 1555 1555 2.40
LINK CD CD A 163 O HOH A 176 1555 1555 2.23
LINK CD CD A 164 O HOH A 209 1555 1555 2.25
SITE 1 AC1 6 ASP A 106 ASN A 108 ASP A 110 PHE A 112
SITE 2 AC1 6 GLU A 117 HOH A 176
SITE 1 AC2 6 ASP A 142 ASN A 144 ASP A 146 ARG A 148
SITE 2 AC2 6 GLU A 153 HOH A 209
SITE 1 AC3 7 GLY A 43 THR A 44 ARG A 47 LYS A 55
SITE 2 AC3 7 HOH A 234 HOH A 306 HOH A 325
CRYST1 66.700 66.700 60.800 90.00 90.00 120.00 P 32 2 1 6
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 0.014993 0.008656 0.000000 0.00000
SCALE2 0.000000 0.017312 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016447 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
