HEADER STRUCTURAL PROTEIN 12-JAN-00 1DTL
TITLE CRYSTAL STRUCTURE OF CALCIUM-SATURATED (3CA2+) CARDIAC TROPONIN C
TITLE 2 COMPLEXED WITH THE CALCIUM SENSITIZER BEPRIDIL AT 2.15 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARDIAC TROPONIN C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: HEART;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: BL21(DE3)PLYSS
KEYWDS HELIX-TURN-HELIX, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LI,M.L.LOVE,J.A.PUTKEY,C.COHEN
REVDAT 4 09-AUG-23 1DTL 1 REMARK
REVDAT 3 03-NOV-21 1DTL 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1DTL 1 VERSN
REVDAT 1 12-MAY-00 1DTL 0
JRNL AUTH Y.LI,M.L.LOVE,J.A.PUTKEY,C.COHEN
JRNL TITL BEPRIDIL OPENS THE REGULATORY N-TERMINAL LOBE OF CARDIAC
JRNL TITL 2 TROPONIN C.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 5140 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10792039
JRNL DOI 10.1073/PNAS.090098997
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 500.00
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) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 7829
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 405
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 846
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 34
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 : 1181
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 123
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.19300
REMARK 3 B22 (A**2) : 1.09700
REMARK 3 B33 (A**2) : 1.09700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 1.450
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : BEPRIDIL.PAR2
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DTL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010355.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-98
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.935
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7998
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.830
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.12
REMARK 200 R MERGE FOR SHELL (I) : 0.12600
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRIES 1AVS AND 1TN4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350 MONODISPERSE, MAGNESIUM
REMARK 280 CHLORIDE, CALCIUM CHLORIDE, HEPES, BEPRIDIL, HCL, PH 7.2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 18.13500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.02000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.02000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.02000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.13500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.02000
REMARK 290 SMTRY3 4 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 MET A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 3
REMARK 465 ILE A 4
REMARK 465 ASP A 87
REMARK 465 ASP A 88
REMARK 465 SER A 89
REMARK 465 LYS A 90
REMARK 465 GLY A 91
REMARK 465 GLY A 125
REMARK 465 GLU A 126
REMARK 465 GLU A 161
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 122 CG CD OE1 NE2
REMARK 470 THR A 124 CB OG1 CG2
REMARK 470 VAL A 160 O CB CG1 CG2
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 OD1 71.1
REMARK 620 3 SER A 69 OG 95.4 83.3
REMARK 620 4 THR A 71 O 90.7 154.0 80.1
REMARK 620 5 GLU A 76 OE1 109.4 125.0 146.7 77.9
REMARK 620 6 GLU A 76 OE2 79.6 75.2 158.4 120.7 52.4
REMARK 620 7 HOH A 414 O 165.7 95.1 86.0 103.5 75.3 93.8
REMARK 620 N 1 2 3 4 5 6
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 77.4
REMARK 620 3 ASP A 109 OD1 80.6 80.1
REMARK 620 4 TYR A 111 O 78.2 150.6 80.0
REMARK 620 5 GLU A 116 OE1 122.3 128.6 144.2 78.9
REMARK 620 6 GLU A 116 OE2 99.7 81.9 161.5 118.4 50.1
REMARK 620 7 HOH A 408 O 161.3 87.6 85.9 112.2 75.9 89.0
REMARK 620 N 1 2 3 4 5 6
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 79.4
REMARK 620 3 ASP A 145 OD1 78.2 83.0
REMARK 620 4 ARG A 147 O 82.4 153.2 74.1
REMARK 620 5 GLU A 152 OE1 116.4 125.9 148.3 79.9
REMARK 620 6 GLU A 152 OE2 92.3 77.8 159.9 122.6 51.8
REMARK 620 7 HOH A 413 O 162.4 87.2 89.1 105.9 80.7 95.9
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 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 BEP A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEP A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEP A 206
DBREF 1DTL A 1 161 UNP P09860 TNNC1_CHICK 1 161
SEQADV 1DTL SER A 35 UNP P09860 CYS 35 ENGINEERED MUTATION
SEQADV 1DTL SER A 84 UNP P09860 CYS 84 ENGINEERED MUTATION
SEQADV 1DTL SER A 93 UNP P09860 THR 93 CONFLICT
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
HET CA A 201 1
HET CA A 202 1
HET CA A 203 1
HET BEP A 204 27
HET BEP A 205 27
HET BEP A 206 27
HETNAM CA CALCIUM ION
HETNAM BEP 1-ISOBUTOXY-2-PYRROLIDINO-3[N-BENZYLANILINO] PROPANE
HETSYN BEP BEPRIDIL
FORMUL 2 CA 3(CA 2+)
FORMUL 5 BEP 3(C24 H34 N2 O)
FORMUL 8 HOH *123(H2 O)
HELIX 1 1 ALA A 7 LEU A 12 5 6
HELIX 2 2 THR A 13 VAL A 28 1 16
HELIX 3 3 ALA A 31 SER A 35 5 5
HELIX 4 4 SER A 37 LEU A 48 1 12
HELIX 5 5 THR A 53 ASP A 65 1 13
HELIX 6 6 ASP A 73 LYS A 86 1 14
HELIX 7 7 LYS A 92 ASP A 105 1 14
HELIX 8 8 LEU A 114 LYS A 118 1 5
HELIX 9 9 ILE A 119 GLN A 122 5 4
HELIX 10 10 THR A 129 ASP A 141 1 13
HELIX 11 11 TYR A 150 GLY A 159 1 10
SHEET 1 A 2 TYR A 111 ASP A 113 0
SHEET 2 A 2 ARG A 147 ASP A 149 -1 N ILE A 148 O ILE A 112
LINK OD2 ASP A 65 CA CA A 201 1555 1555 2.32
LINK OD1 ASP A 67 CA CA A 201 1555 1555 2.34
LINK OG SER A 69 CA CA A 201 1555 1555 2.30
LINK O THR A 71 CA CA A 201 1555 1555 2.31
LINK OE1 GLU A 76 CA CA A 201 1555 1555 2.59
LINK OE2 GLU A 76 CA CA A 201 1555 1555 2.46
LINK OD1 ASP A 105 CA CA A 202 1555 1555 2.29
LINK OD1 ASN A 107 CA CA A 202 1555 1555 2.31
LINK OD1 ASP A 109 CA CA A 202 1555 1555 2.59
LINK O TYR A 111 CA CA A 202 1555 1555 2.44
LINK OE1 GLU A 116 CA CA A 202 1555 1555 2.70
LINK OE2 GLU A 116 CA CA A 202 1555 1555 2.56
LINK OD2 ASP A 141 CA CA A 203 1555 1555 2.51
LINK OD1 ASN A 143 CA CA A 203 1555 1555 2.48
LINK OD1 ASP A 145 CA CA A 203 1555 1555 2.53
LINK O ARG A 147 CA CA A 203 1555 1555 2.29
LINK OE1 GLU A 152 CA CA A 203 1555 1555 2.51
LINK OE2 GLU A 152 CA CA A 203 1555 1555 2.69
LINK CA CA A 201 O HOH A 414 1555 1555 2.26
LINK CA CA A 202 O HOH A 408 1555 1555 2.57
LINK CA CA A 203 O HOH A 413 1555 1555 2.37
SITE 1 AC1 6 ASP A 65 ASP A 67 SER A 69 THR A 71
SITE 2 AC1 6 GLU A 76 HOH A 414
SITE 1 AC2 6 ASP A 105 ASN A 107 ASP A 109 TYR A 111
SITE 2 AC2 6 GLU A 116 HOH A 408
SITE 1 AC3 6 ASP A 141 ASN A 143 ASP A 145 ARG A 147
SITE 2 AC3 6 GLU A 152 HOH A 413
SITE 1 AC4 7 PHE A 27 LEU A 41 MET A 45 MET A 60
SITE 2 AC4 7 MET A 80 GLU A 96 BEP A 205
SITE 1 AC5 10 PHE A 20 ALA A 23 MET A 81 LEU A 100
SITE 2 AC5 10 PHE A 104 LEU A 117 MET A 120 PHE A 156
SITE 3 AC5 10 MET A 157 BEP A 204
SITE 1 AC6 8 GLU A 14 MET A 45 GLN A 50 PRO A 52
SITE 2 AC6 8 GLU A 56 GLU A 96 ASP A 99 MET A 103
CRYST1 36.270 62.040 62.040 90.00 90.00 90.00 P 21 21 21 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 0.027571 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016119 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016119 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
