HEADER CALCIUM BINDING PROTEIN 16-OCT-08 3EWT
TITLE CRYSTAL STRUCTURE OF CALMODULIN COMPLEXED WITH A PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 6;
COMPND 8 CHAIN: E;
COMPND 9 FRAGMENT: HELIX(1+2) OF DEATH DOMAIN;
COMPND 10 SYNONYM: FASLG RECEPTOR, APOPTOSIS-MEDIATING SURFACE ANTIGEN FAS,
COMPND 11 APO-1 ANTIGEN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630;
SOURCE 14 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS CALMODULIN-PEPTIDE COMPLEX, FAS, DEATH DOMAIN, CALCIUM BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.JIANG,P.CAO,Y.GONG,H.J.YU,W.J.GUI,W.T.ZHANG
REVDAT 4 01-NOV-23 3EWT 1 REMARK
REVDAT 3 01-JAN-20 3EWT 1 SOURCE JRNL SEQADV
REVDAT 2 18-JUN-14 3EWT 1 JRNL VERSN
REVDAT 1 20-OCT-09 3EWT 0
JRNL AUTH P.CAO,W.ZHANG,W.GUI,Y.DONG,T.JIANG,Y.GONG
JRNL TITL STRUCTURAL INSIGHTS INTO THE MECHANISM OF CALMODULIN BINDING
JRNL TITL 2 TO DEATH RECEPTORS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 1604 2014
JRNL REFN ESSN 1399-0047
JRNL PMID 24914971
JRNL DOI 10.1107/S1399004714006919
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 6575
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 + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 312
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 475
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 18
REMARK 3 BIN FREE R VALUE : 0.4470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1227
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 44
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.73000
REMARK 3 B22 (A**2) : 0.73000
REMARK 3 B33 (A**2) : -1.09000
REMARK 3 B12 (A**2) : 0.36000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.491
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.278
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1239 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1667 ; 1.384 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 157 ; 5.293 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 65 ;37.661 ;26.308
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 224 ;20.238 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;16.376 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 189 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 940 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 682 ; 0.240 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 880 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 57 ; 0.128 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 21 ; 0.097 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 32 ; 0.268 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.185 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 783 ; 0.916 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1252 ; 1.499 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 456 ; 1.700 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 415 ; 3.023 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3EWT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049865.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6946
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 8.600
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : 0.04100
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1L7Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25%(W/V) PEG8000, 0.2M SODIUM ACETATE,
REMARK 280 0.1M SODIUM CACODYLATE, PH 5.5, EVAPORATION, TEMPERATURE 293K
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 116.28733
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 58.14367
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 58.14367
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 116.28733
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 626 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 627 LIES ON A SPECIAL POSITION.
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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 THR A 146
REMARK 465 ALA A 147
REMARK 465 LYS A 148
REMARK 465 GLN E 244
REMARK 465 VAL E 245
REMARK 465 LYS E 246
REMARK 465 GLY E 247
REMARK 465 PHE E 248
REMARK 465 VAL E 249
REMARK 465 ARG E 250
REMARK 465 LYS E 251
REMARK 465 ASN E 252
REMARK 465 GLY E 253
REMARK 465 VAL E 254
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 MET A 76 CG SD CE
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLU A 84 CG CD OE1 OE2
REMARK 470 GLU A 119 CG CD OE1 OE2
REMARK 470 GLU A 123 CG CD OE1 OE2
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 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 83.1
REMARK 620 3 ASP A 24 OD1 85.4 83.7
REMARK 620 4 THR A 26 O 81.7 158.5 80.0
REMARK 620 5 GLU A 31 OE1 107.6 126.0 148.1 73.4
REMARK 620 6 GLU A 31 OE2 99.8 76.4 158.6 121.2 49.8
REMARK 620 7 HOH A 607 O 162.8 80.6 87.5 112.4 86.5 81.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 602 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 78.9
REMARK 620 3 ASN A 60 OD1 87.0 75.5
REMARK 620 4 THR A 62 O 81.9 147.8 77.9
REMARK 620 5 GLU A 67 OE1 106.2 131.0 151.7 79.3
REMARK 620 6 GLU A 67 OE2 93.9 76.0 150.7 131.2 55.1
REMARK 620 7 HOH A 645 O 151.0 72.1 86.6 124.1 92.5 78.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 603 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 86.2
REMARK 620 3 ASN A 97 OD1 88.3 74.3
REMARK 620 4 TYR A 99 O 88.5 154.7 80.8
REMARK 620 5 GLU A 104 OE1 105.0 130.7 151.4 74.5
REMARK 620 6 GLU A 104 OE2 92.9 76.9 151.0 128.1 55.1
REMARK 620 7 HOH A 617 O 169.4 83.5 90.9 101.8 80.4 82.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 87.0
REMARK 620 3 ASP A 133 OD2 97.3 73.4
REMARK 620 4 GLN A 135 O 92.2 155.6 82.6
REMARK 620 5 GLU A 140 OE1 109.0 125.9 147.2 77.3
REMARK 620 6 GLU A 140 OE2 85.0 81.4 154.4 122.9 50.8
REMARK 620 7 HOH A 605 O 163.8 77.0 76.1 101.4 82.7 94.7
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EWV RELATED DB: PDB
DBREF 3EWT A 1 148 UNP P62158 CALM_HUMAN 2 149
DBREF 3EWT E 230 254 UNP P25445 TNR6_HUMAN 230 254
SEQADV 3EWT HIS A -5 UNP P62158 EXPRESSION TAG
SEQADV 3EWT HIS A -4 UNP P62158 EXPRESSION TAG
SEQADV 3EWT HIS A -3 UNP P62158 EXPRESSION TAG
SEQADV 3EWT HIS A -2 UNP P62158 EXPRESSION TAG
SEQADV 3EWT HIS A -1 UNP P62158 EXPRESSION TAG
SEQADV 3EWT HIS A 0 UNP P62158 EXPRESSION TAG
SEQRES 1 A 154 HIS HIS HIS HIS HIS HIS ALA ASP GLN LEU THR GLU GLU
SEQRES 2 A 154 GLN ILE ALA GLU PHE LYS GLU ALA PHE SER LEU PHE ASP
SEQRES 3 A 154 LYS ASP GLY ASP GLY THR ILE THR THR LYS GLU LEU GLY
SEQRES 4 A 154 THR VAL MET ARG SER LEU GLY GLN ASN PRO THR GLU ALA
SEQRES 5 A 154 GLU LEU GLN ASP MET ILE ASN GLU VAL ASP ALA ASP GLY
SEQRES 6 A 154 ASN GLY THR ILE ASP PHE PRO GLU PHE LEU THR MET MET
SEQRES 7 A 154 ALA ARG LYS MET LYS ASP THR ASP SER GLU GLU GLU ILE
SEQRES 8 A 154 ARG GLU ALA PHE ARG VAL PHE ASP LYS ASP GLY ASN GLY
SEQRES 9 A 154 TYR ILE SER ALA ALA GLU LEU ARG HIS VAL MET THR ASN
SEQRES 10 A 154 LEU GLY GLU LYS LEU THR ASP GLU GLU VAL ASP GLU MET
SEQRES 11 A 154 ILE ARG GLU ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN
SEQRES 12 A 154 TYR GLU GLU PHE VAL GLN MET MET THR ALA LYS
SEQRES 1 E 25 SER LYS TYR ILE THR THR ILE ALA GLY VAL MET THR LEU
SEQRES 2 E 25 SER GLN VAL LYS GLY PHE VAL ARG LYS ASN GLY VAL
HET CA A 601 1
HET CA A 602 1
HET CA A 603 1
HET CA A 604 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *44(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 28 LEU A 39 1 12
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 PHE A 65 ASP A 78 1 14
HELIX 5 5 SER A 81 ASP A 93 1 13
HELIX 6 6 SER A 101 LEU A 112 1 12
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 TYR A 138 MET A 145 1 8
HELIX 9 9 LYS E 231 SER E 243 1 13
SHEET 1 A 2 THR A 26 ILE A 27 0
SHEET 2 A 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 B 2 TYR A 99 ILE A 100 0
SHEET 2 B 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP A 20 CA CA A 601 1555 1555 2.19
LINK OD1 ASP A 22 CA CA A 601 1555 1555 2.32
LINK OD1 ASP A 24 CA CA A 601 1555 1555 2.37
LINK O THR A 26 CA CA A 601 1555 1555 2.35
LINK OE1 GLU A 31 CA CA A 601 1555 1555 2.64
LINK OE2 GLU A 31 CA CA A 601 1555 1555 2.56
LINK OD1 ASP A 56 CA CA A 602 1555 1555 2.31
LINK OD1 ASP A 58 CA CA A 602 1555 1555 2.41
LINK OD1 ASN A 60 CA CA A 602 1555 1555 2.55
LINK O THR A 62 CA CA A 602 1555 1555 2.37
LINK OE1 GLU A 67 CA CA A 602 1555 1555 2.39
LINK OE2 GLU A 67 CA CA A 602 1555 1555 2.33
LINK OD1 ASP A 93 CA CA A 603 1555 1555 2.28
LINK OD1 ASP A 95 CA CA A 603 1555 1555 2.37
LINK OD1 ASN A 97 CA CA A 603 1555 1555 2.35
LINK O TYR A 99 CA CA A 603 1555 1555 2.30
LINK OE1 GLU A 104 CA CA A 603 1555 1555 2.37
LINK OE2 GLU A 104 CA CA A 603 1555 1555 2.37
LINK OD1 ASP A 129 CA CA A 604 1555 1555 2.25
LINK OD1 ASP A 131 CA CA A 604 1555 1555 2.43
LINK OD2 ASP A 133 CA CA A 604 1555 1555 2.35
LINK O GLN A 135 CA CA A 604 1555 1555 2.36
LINK OE1 GLU A 140 CA CA A 604 1555 1555 2.60
LINK OE2 GLU A 140 CA CA A 604 1555 1555 2.46
LINK CA CA A 601 O HOH A 607 1555 1555 2.38
LINK CA CA A 602 O HOH A 645 1555 1555 2.33
LINK CA CA A 603 O HOH A 617 1555 1555 2.37
LINK CA CA A 604 O HOH A 605 1555 1555 2.53
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 GLU A 31 HOH A 607
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 GLU A 67 HOH A 645
SITE 1 AC3 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 6 GLU A 104 HOH A 617
SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 6 GLU A 140 HOH A 605
CRYST1 40.062 40.062 174.431 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 0.024961 0.014411 0.000000 0.00000
SCALE2 0.000000 0.028823 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005733 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
