HEADER METAL BINDING PROTEIN 26-FEB-14 2MLF
TITLE NMR STRUCTURE OF THE DILATED CARDIOMYOPATHY MUTATION G159D IN TROPONIN
TITLE 2 C BOUND TO THE ANCHORING REGION OF TROPONIN I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C, SLOW SKELETAL AND CARDIAC MUSCLES;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: UNP RESIDUES 91-161;
COMPND 5 SYNONYM: TN-C;
COMPND 6 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: BL21(DE3)PLYSS
KEYWDS TROPONIN C, METAL BINDING PROTEIN, DILATED CARDIOMYOPATHY, G159D, EF-
KEYWDS 2 HAND
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR O.K.BARYSHNIKOVA,I.M.ROBERTSON,P.MERCIER,B.D.SYKES
REVDAT 3 14-JUN-23 2MLF 1 REMARK SEQADV LINK
REVDAT 2 09-DEC-15 2MLF 1 JRNL
REVDAT 1 12-MAR-14 2MLF 0
JRNL AUTH O.K.BARYSHNIKOVA,I.M.ROBERTSON,P.MERCIER,B.D.SYKES
JRNL TITL THE DILATED CARDIOMYOPATHY G159D MUTATION IN CARDIAC
JRNL TITL 2 TROPONIN C WEAKENS THE ANCHORING INTERACTION WITH TROPONIN
JRNL TITL 3 I.
JRNL REF BIOCHEMISTRY V. 47 10950 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18803402
JRNL DOI 10.1021/BI801165C
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA, PROCHECKNMR, TALOS, X-PLOR NIH, CYANA
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA),
REMARK 3 LASKOWSKI AND MACARTHUR (PROCHECKNMR), CORNILESCU,
REMARK 3 DELAGLIO AND BAX (TALOS), SCHWIETERS, KUSZEWSKI,
REMARK 3 TJANDRA AND CLORE (X-PLOR NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MLF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000103756.
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 : 0.12
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM [U-95% 13C; U-95% 15N]
REMARK 210 CCTNC, 2 MM CALCIUM, 0.2 MM DSS,
REMARK 210 100 MM POTASSIUM CHLORIDE, 5 MM
REMARK 210 SODIUM AZIDE, 10 MM IMIDAZOLE,
REMARK 210 1.2 MM TROPONIN I(34-71), 90%
REMARK 210 H2O/10% D2O; 0.5 MM [U-95% 13C;
REMARK 210 U-95% 15N] CCTNC, 2 MM CALCIUM,
REMARK 210 0.2 MM DSS, 100 MM POTASSIUM
REMARK 210 CHLORIDE, 5 MM SODIUM AZIDE, 0.5
REMARK 210 MM IMIDAZOLE, 1.2 MM TROPONIN
REMARK 210 I(34-71), 9.5 MM [U-2H]
REMARK 210 IMIDAZOLE, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HCCH-TOCSY;
REMARK 210 3D CBCA(CO)NH; 3D HNCACB; 3D
REMARK 210 H(CCO)NH; 3D C(CO)NH; 3D 1H-13C
REMARK 210 NOESY; 3D 1H-15N NOESY; 3D 1H-
REMARK 210 15N TOCSY; 3D HNHA; 3D HNHB; 2D
REMARK 210 DQF-COSY; 2D 1H-1H NOESY; 2D 13C-
REMARK 210 15N FILTERED 1H-1H TOCSY; 2D 13C-
REMARK 210 15N FILTERED 1H-1H NOESY; 2D 13C
REMARK 210 EDITED,FILTERED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, NMRDRAW, NMRPIPE,
REMARK 210 NMRVIEW, TALOS, VNMRJ
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 MET C 103 HZ1 LYS C 106 1.44
REMARK 500 OE2 GLU C 135 HZ2 LYS C 138 1.48
REMARK 500 O ASP C 105 HZ2 LYS C 106 1.53
REMARK 500 HZ2 LYS C 142 OE1 GLU C 155 1.54
REMARK 500 OD1 ASP C 115 HZ2 LYS C 118 1.54
REMARK 500 HZ3 LYS C 92 OD1 ASP C 159 1.56
REMARK 500 HZ2 LYS C 92 OE1 GLU C 161 1.58
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 1 GLU C 116 CD GLU C 116 OE2 -0.081
REMARK 500 1 GLU C 152 CD GLU C 152 OE1 -0.071
REMARK 500 1 GLU C 152 CD GLU C 152 OE2 -0.082
REMARK 500 2 GLU C 116 CD GLU C 116 OE2 -0.085
REMARK 500 2 GLU C 152 CD GLU C 152 OE1 -0.067
REMARK 500 2 GLU C 152 CD GLU C 152 OE2 -0.087
REMARK 500 3 GLU C 116 CD GLU C 116 OE2 -0.088
REMARK 500 3 GLU C 152 CD GLU C 152 OE1 -0.067
REMARK 500 3 GLU C 152 CD GLU C 152 OE2 -0.078
REMARK 500 4 GLU C 116 CD GLU C 116 OE1 -0.072
REMARK 500 4 GLU C 116 CD GLU C 116 OE2 -0.088
REMARK 500 4 GLU C 152 CD GLU C 152 OE2 -0.079
REMARK 500 5 GLU C 116 CD GLU C 116 OE1 -0.082
REMARK 500 5 GLU C 116 CD GLU C 116 OE2 -0.082
REMARK 500 5 GLU C 152 CD GLU C 152 OE1 -0.080
REMARK 500 5 GLU C 152 CD GLU C 152 OE2 -0.077
REMARK 500 6 GLU C 116 CD GLU C 116 OE1 -0.066
REMARK 500 6 GLU C 116 CD GLU C 116 OE2 -0.104
REMARK 500 6 GLU C 152 CD GLU C 152 OE1 -0.072
REMARK 500 6 GLU C 152 CD GLU C 152 OE2 -0.096
REMARK 500 7 GLU C 116 CD GLU C 116 OE1 -0.071
REMARK 500 7 GLU C 116 CD GLU C 116 OE2 -0.084
REMARK 500 7 GLU C 152 CD GLU C 152 OE1 -0.078
REMARK 500 7 GLU C 152 CD GLU C 152 OE2 -0.071
REMARK 500 8 GLU C 116 CD GLU C 116 OE1 -0.093
REMARK 500 8 GLU C 116 CD GLU C 116 OE2 -0.078
REMARK 500 8 GLU C 152 CD GLU C 152 OE1 -0.078
REMARK 500 8 GLU C 152 CD GLU C 152 OE2 -0.081
REMARK 500 9 GLU C 116 CD GLU C 116 OE1 -0.083
REMARK 500 9 GLU C 116 CD GLU C 116 OE2 -0.075
REMARK 500 9 GLU C 152 CD GLU C 152 OE2 -0.069
REMARK 500 10 GLU C 116 CD GLU C 116 OE1 -0.067
REMARK 500 10 GLU C 116 CD GLU C 116 OE2 -0.077
REMARK 500 10 GLU C 152 CD GLU C 152 OE1 -0.076
REMARK 500 10 GLU C 152 CD GLU C 152 OE2 -0.096
REMARK 500 11 GLU C 116 CD GLU C 116 OE1 -0.072
REMARK 500 11 GLU C 116 CD GLU C 116 OE2 -0.082
REMARK 500 11 GLU C 152 CD GLU C 152 OE2 -0.090
REMARK 500 12 GLU C 116 CD GLU C 116 OE2 -0.086
REMARK 500 12 GLU C 152 CD GLU C 152 OE1 -0.087
REMARK 500 12 GLU C 152 CD GLU C 152 OE2 -0.076
REMARK 500 13 GLU C 116 CD GLU C 116 OE1 -0.074
REMARK 500 13 GLU C 116 CD GLU C 116 OE2 -0.090
REMARK 500 13 GLU C 152 CD GLU C 152 OE1 -0.082
REMARK 500 13 GLU C 152 CD GLU C 152 OE2 -0.083
REMARK 500 14 GLU C 116 CD GLU C 116 OE1 -0.067
REMARK 500 14 GLU C 116 CD GLU C 116 OE2 -0.078
REMARK 500 14 GLU C 152 CD GLU C 152 OE1 -0.086
REMARK 500 14 GLU C 152 CD GLU C 152 OE2 -0.085
REMARK 500 15 GLU C 116 CD GLU C 116 OE1 -0.079
REMARK 500
REMARK 500 THIS ENTRY HAS 72 BOND DEVIATIONS.
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 159 -71.93 -91.67
REMARK 500 1 VAL C 160 71.64 43.29
REMARK 500 2 ASP C 159 -57.06 57.44
REMARK 500 2 VAL C 160 91.52 40.44
REMARK 500 4 LYS C 92 48.80 -142.51
REMARK 500 4 GLU C 126 -72.71 -77.59
REMARK 500 4 ILE C 128 171.60 61.30
REMARK 500 4 GLU C 130 -64.63 63.43
REMARK 500 5 GLU C 130 49.58 -72.81
REMARK 500 5 ASP C 131 -63.02 -144.60
REMARK 500 6 LYS C 92 -78.60 -133.95
REMARK 500 6 SER C 93 -63.70 -180.00
REMARK 500 6 GLU C 126 -112.33 41.61
REMARK 500 6 LYS C 158 -73.00 -60.14
REMARK 500 7 LYS C 92 39.40 -146.85
REMARK 500 7 GLU C 130 -56.69 68.18
REMARK 500 7 ASN C 143 -125.84 -96.59
REMARK 500 7 ASN C 144 33.28 -141.91
REMARK 500 8 GLU C 130 -27.98 -172.36
REMARK 500 9 LYS C 92 61.04 -154.37
REMARK 500 9 THR C 124 70.25 -151.60
REMARK 500 9 GLU C 126 -92.35 -93.50
REMARK 500 10 LYS C 92 -35.84 -137.96
REMARK 500 10 ASP C 159 60.34 -108.24
REMARK 500 11 GLU C 126 -124.08 -82.09
REMARK 500 12 THR C 124 57.90 -159.12
REMARK 500 12 ASP C 131 -62.52 -145.86
REMARK 500 13 THR C 129 -166.77 -77.22
REMARK 500 14 ASP C 159 77.63 -112.39
REMARK 500 16 ALA C 108 13.87 59.24
REMARK 500 16 GLU C 126 -81.92 59.79
REMARK 500 16 ASP C 141 63.57 -113.14
REMARK 500 16 ASN C 144 92.49 -64.36
REMARK 500 17 ASP C 159 49.90 -83.42
REMARK 500 19 VAL C 160 -32.64 -137.57
REMARK 500 20 VAL C 160 -54.00 -153.08
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 102 0.28 SIDE CHAIN
REMARK 500 1 ARG C 147 0.29 SIDE CHAIN
REMARK 500 2 ARG C 102 0.33 SIDE CHAIN
REMARK 500 2 ARG C 147 0.17 SIDE CHAIN
REMARK 500 3 ARG C 102 0.26 SIDE CHAIN
REMARK 500 3 ARG C 147 0.26 SIDE CHAIN
REMARK 500 4 ARG C 102 0.32 SIDE CHAIN
REMARK 500 4 ARG C 147 0.29 SIDE CHAIN
REMARK 500 5 ARG C 102 0.29 SIDE CHAIN
REMARK 500 5 ARG C 147 0.32 SIDE CHAIN
REMARK 500 6 ARG C 102 0.33 SIDE CHAIN
REMARK 500 6 ARG C 147 0.28 SIDE CHAIN
REMARK 500 7 ARG C 102 0.29 SIDE CHAIN
REMARK 500 7 ARG C 147 0.26 SIDE CHAIN
REMARK 500 8 ARG C 102 0.31 SIDE CHAIN
REMARK 500 8 ARG C 147 0.31 SIDE CHAIN
REMARK 500 9 ARG C 102 0.26 SIDE CHAIN
REMARK 500 9 ARG C 147 0.25 SIDE CHAIN
REMARK 500 10 ARG C 102 0.24 SIDE CHAIN
REMARK 500 11 ARG C 102 0.28 SIDE CHAIN
REMARK 500 11 ARG C 147 0.29 SIDE CHAIN
REMARK 500 12 ARG C 102 0.24 SIDE CHAIN
REMARK 500 12 ARG C 147 0.28 SIDE CHAIN
REMARK 500 13 ARG C 102 0.17 SIDE CHAIN
REMARK 500 13 ARG C 147 0.26 SIDE CHAIN
REMARK 500 14 ARG C 102 0.28 SIDE CHAIN
REMARK 500 14 ARG C 147 0.31 SIDE CHAIN
REMARK 500 15 ARG C 102 0.30 SIDE CHAIN
REMARK 500 15 ARG C 147 0.33 SIDE CHAIN
REMARK 500 16 ARG C 102 0.31 SIDE CHAIN
REMARK 500 16 ARG C 147 0.32 SIDE CHAIN
REMARK 500 17 ARG C 102 0.29 SIDE CHAIN
REMARK 500 17 ARG C 147 0.30 SIDE CHAIN
REMARK 500 18 ARG C 102 0.28 SIDE CHAIN
REMARK 500 18 ARG C 147 0.11 SIDE CHAIN
REMARK 500 19 ARG C 102 0.28 SIDE CHAIN
REMARK 500 19 ARG C 147 0.32 SIDE CHAIN
REMARK 500 20 ARG C 102 0.28 SIDE CHAIN
REMARK 500 20 ARG C 147 0.29 SIDE CHAIN
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 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 105 OD2
REMARK 620 2 ASP C 105 OD1 39.6
REMARK 620 3 ASP C 109 OD1 98.9 67.4
REMARK 620 4 ASP C 109 OD2 99.2 105.1 64.9
REMARK 620 5 GLU C 116 OE2 157.5 135.6 95.0 102.7
REMARK 620 6 GLU C 116 OE1 96.1 78.8 99.8 159.8 63.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 141 OD1
REMARK 620 2 ASP C 145 OD2 108.5
REMARK 620 3 ASP C 145 OD1 75.5 62.9
REMARK 620 4 ARG C 147 O 127.0 98.9 78.4
REMARK 620 5 GLU C 152 OE1 127.9 103.4 156.6 85.7
REMARK 620 6 GLU C 152 OE2 76.2 91.0 131.9 148.7 63.0
REMARK 620 N 1 2 3 4 5
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19817 RELATED DB: BMRB
REMARK 900 RELATED ID: 2MLE RELATED DB: PDB
DBREF 2MLF C 91 161 UNP P63316 TNNC1_HUMAN 91 161
SEQADV 2MLF MET C 90 UNP P63316 INITIATING METHIONINE
SEQADV 2MLF ASP C 159 UNP P63316 GLY 159 ENGINEERED MUTATION
SEQRES 1 C 72 MET GLY LYS SER GLU GLU GLU LEU SER ASP LEU PHE ARG
SEQRES 2 C 72 MET PHE ASP LYS ASN ALA ASP GLY TYR ILE ASP LEU ASP
SEQRES 3 C 72 GLU LEU LYS ILE MET LEU GLN ALA THR GLY GLU THR ILE
SEQRES 4 C 72 THR GLU ASP ASP ILE GLU GLU LEU MET LYS ASP GLY ASP
SEQRES 5 C 72 LYS ASN ASN ASP GLY ARG ILE ASP TYR ASP GLU PHE LEU
SEQRES 6 C 72 GLU PHE MET LYS ASP VAL GLU
HET CA C 201 1
HET CA C 202 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 SER C 93 ASP C 105 1 13
HELIX 2 2 LEU C 114 GLY C 125 1 12
HELIX 3 3 THR C 129 ASP C 141 1 13
HELIX 4 4 TYR C 150 MET C 157 1 8
SHEET 1 A 2 TYR C 111 ASP C 113 0
SHEET 2 A 2 ARG C 147 ASP C 149 -1 O ILE C 148 N ILE C 112
LINK OD2 ASP C 105 CA CA C 202 1555 1555 1.86
LINK OD1 ASP C 105 CA CA C 202 1555 1555 3.14
LINK OD1 ASP C 109 CA CA C 202 1555 1555 1.89
LINK OD2 ASP C 109 CA CA C 202 1555 1555 1.93
LINK OE2 GLU C 116 CA CA C 202 1555 1555 1.92
LINK OE1 GLU C 116 CA CA C 202 1555 1555 1.94
LINK OD1 ASP C 141 CA CA C 201 1555 1555 2.52
LINK OD2 ASP C 145 CA CA C 201 1555 1555 1.92
LINK OD1 ASP C 145 CA CA C 201 1555 1555 1.95
LINK O ARG C 147 CA CA C 201 1555 1555 1.98
LINK OE1 GLU C 152 CA CA C 201 1555 1555 1.88
LINK OE2 GLU C 152 CA CA C 201 1555 1555 2.00
SITE 1 AC1 4 ASP C 141 ASP C 145 ARG C 147 GLU C 152
SITE 1 AC2 4 ASP C 105 ASP C 109 TYR C 111 GLU C 116
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
