HEADER CALCIUM-BINDING PROTEIN 17-JUN-99 1QIW
TITLE CALMODULIN COMPLEXED WITH N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-(3,4-BIS-
TITLE 2 BUTOXYPHENYL)-ETHYL]-PROPYLENEDIAMINE (DPD)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM
KEYWDS CALCIUM-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.HARMAT,Z.S.BOCSKEI,B.G.VERTESSY,J.OVADI,G.NARAY-SZABO
REVDAT 6 13-DEC-23 1QIW 1 REMARK LINK
REVDAT 5 08-MAY-19 1QIW 1 REMARK
REVDAT 4 05-JUL-17 1QIW 1 REMARK
REVDAT 3 24-MAR-09 1QIW 1 REMARK MASTER
REVDAT 2 24-FEB-09 1QIW 1 VERSN
REVDAT 1 28-MAR-00 1QIW 0
JRNL AUTH V.HARMAT,Z.S.BOCSKEI,G.NARAY-SZABO,I.BATA,A.S.CSUTOR,
JRNL AUTH 2 I.HERMECZ,P.ARANYI,B.SZABO,K.LILIOM,B.G.VERTESSY,J.OVADI
JRNL TITL A NEW POTENT CALMODULIN ANTAGONIST WITH ARYLALKYLAMINE
JRNL TITL 2 STRUCTURE: CRYSTALLOGRAPHIC, SPECTROSCOPIC AND FUNCTIONAL
JRNL TITL 3 STUDIES
JRNL REF J.MOL.BIOL. V. 297 747 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10731425
JRNL DOI 10.1006/JMBI.2000.3607
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.G.VERTESSY,Z.S.BOCSKEI,V.HARMATH,G.NARAY-SZABO,J.OVADI
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY DIFFRACTION ANALYSIS OF
REMARK 1 TITL 2 CA(2+)-CALMODULIN-DRUG AND APOCALMODULIN-DRUG COMPLEXES.
REMARK 1 REF PROTEINS: STRUCT.,FUNCT., V. 28 131 1997
REMARK 1 REF 2 GENET.
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 9144798
REMARK 1 DOI 10.1002/(SICI)1097-0134(199705)28:1<131::AID-PROT13>3.0.CO;2
REMARK 1 DOI 2 -K
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.VANDONSELAAR,R.A.HICKIE,J.W.QUAIL,L.T.J.DELBAERE
REMARK 1 TITL TRIFLUOPERAZINE-INDUCED CONFORMATIONAL CHANGE IN CA
REMARK 1 TITL 2 (2+)-CALMODULIN
REMARK 1 REF NAT.STRUCT.BIOL. V. 1 795 1994
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 7634090
REMARK 1 DOI 10.1038/NSB1194-795
REMARK 1 REFERENCE 3
REMARK 1 AUTH W.J.COOK,L.J.WALTER,M.R.WALTER
REMARK 1 TITL DRUG BINDING BY CALMODULIN: CRYSTAL STRUCTURE OF A
REMARK 1 TITL 2 CALMODULIN-TRIFLUOPERAZINE COMPLEX
REMARK 1 REF BIOCHEMISTRY V. 33 15259 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 7803388
REMARK 1 DOI 10.1021/BI00255A006
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 69.2
REMARK 3 NUMBER OF REFLECTIONS : 8711
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) : 0.232
REMARK 3 FREE R VALUE : 0.317
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.500
REMARK 3 FREE R VALUE TEST SET COUNT : 483
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.014
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 24.39
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 370
REMARK 3 BIN R VALUE (WORKING SET) : 0.1050
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.39
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 13
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.029
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2212
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 112
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.00800
REMARK 3 B22 (A**2) : -12.27900
REMARK 3 B33 (A**2) : -14.91900
REMARK 3 B12 (A**2) : -0.19600
REMARK 3 B13 (A**2) : -1.00100
REMARK 3 B23 (A**2) : -2.45300
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.10
REMARK 3 LOW RESOLUTION CUTOFF (A) : 2.70
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.232
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.25
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.506
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 0.078 ; 50
REMARK 3 GROUP 1 B-FACTOR (A**2) : 5.019 ; 10
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CA.PAR
REMARK 3 PARAMETER FILE 3 : AAA.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : CA.TOP
REMARK 3 TOPOLOGY FILE 3 : AAA.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED SIDE CHAIN ATOMS OF RESIDUES
REMARK 3 A2, A7, A47, A78, A79, A86, A114, A123, B6, B13, B69, B77, B82,
REMARK 3 B84, B123, B127 AND 146 AS WELL AS TRIMETHYL-LYSINES A115, B115
REMARK 3 ARE NOT PRESENT IN THE STRUCTURE TEMPERATURE FACTORS FOR THE
REMARK 3 ATOMS IN THE CENTRAL REGIONS (A73-A80, B75- B82),ATOMS AT THE
REMARK 3 ENDS OF THE POLIPEPTIDE CHAINS (A144-A146, B4-B7, B144) AS WELL
REMARK 3 AS FOR SOME SURFACE RESIDUES (A45, A84, A107, A112, B107, B119,
REMARK 3 B126) ARE UNUSUALLY HIGH, INDICATING FLEXIBILITY IN THESE PARTS
REMARK 3 OF THE STRUCTURE. THE C-TERMINAL RESIDUES FOR BOTH CHAINS A AND
REMARK 3 B WERE NOT SEEN IN THE DENSITY MAPS
REMARK 4
REMARK 4 1QIW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1290002825.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-96
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 6.00
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NORMAL FOCUS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU IMAGE PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BIOTEX
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8711
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 54.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 69.2
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.13700
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 25.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.40
REMARK 200 R MERGE FOR SHELL (I) : 0.70500
REMARK 200 R SYM FOR SHELL (I) : 0.51300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1LIN
REMARK 200
REMARK 200 REMARK: THE TWO DOMAINS OF 1LIN WERE USED SEPARATEDLY AS MODELS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED BY HANGING
REMARK 280 DROP TECHNIQUE. 50 MM PH=6.0 SODIUM CACODYLATE/HCL BUFFER, 10 MM
REMARK 280 MGCL2, 10 MM CACL2, 2MM DPD AND 30% PEG 8000 THE CRYSTAL COULD
REMARK 280 NOT BE REPRODUCED., PH 6.00, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 ALA A 1
REMARK 465 ALA A 147
REMARK 465 LYS A 148
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 GLN B 3
REMARK 465 ALA B 147
REMARK 465 LYS B 148
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 ASP A 2 CG OD1 OD2
REMARK 470 GLU A 7 CG CD OE1 OE2
REMARK 470 GLU A 47 CG CD OE1 OE2
REMARK 470 ASP A 78 CG OD1 OD2
REMARK 470 THR A 79 OG1 CG2
REMARK 470 ARG A 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 114 CG CD OE1 OE2
REMARK 470 GLU A 123 CG CD OE1 OE2
REMARK 470 GLU B 6 CG CD OE1 OE2
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 LEU B 69 CG CD1 CD2
REMARK 470 LYS B 77 CG CD CE NZ
REMARK 470 GLU B 82 CG CD OE1 OE2
REMARK 470 GLU B 84 CG CD OE1 OE2
REMARK 470 GLU B 123 CG CD OE1 OE2
REMARK 470 GLU B 127 CG CD OE1 OE2
REMARK 470 THR B 146 OG1 CG2
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 OD1 ASP B 93 OD1 ASN B 97 2.19
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 ASN A 42 89.94 -150.30
REMARK 500 ASP A 56 76.09 -67.46
REMARK 500 ALA A 73 26.51 -56.01
REMARK 500 ARG A 74 121.32 174.16
REMARK 500 MET A 76 40.86 32.58
REMARK 500 LYS A 77 121.28 -174.89
REMARK 500 ASN A 111 -17.24 -47.91
REMARK 500 GLU A 114 73.34 -155.34
REMARK 500 GLU B 6 -5.71 -54.18
REMARK 500 ASN B 42 79.48 -172.37
REMARK 500 ASP B 56 86.46 -65.64
REMARK 500 LYS B 75 81.34 -169.15
REMARK 500 ASP B 78 168.21 -47.25
REMARK 500 SER B 81 70.37 46.97
REMARK 500 ASN B 111 -13.34 -48.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 DPD A 153
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 149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 66.9
REMARK 620 3 ASP A 22 OD2 114.7 48.1
REMARK 620 4 ASP A 24 OD1 80.6 64.5 78.1
REMARK 620 5 THR A 26 O 90.2 144.9 147.6 86.5
REMARK 620 6 GLU A 31 OE1 107.7 134.9 112.5 160.4 76.0
REMARK 620 7 GLU A 31 OE2 98.2 80.1 68.1 142.2 131.2 55.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 77.4
REMARK 620 3 ASN A 60 OD1 78.3 64.0
REMARK 620 4 THR A 62 O 86.7 151.3 89.6
REMARK 620 5 GLU A 67 OE1 118.3 130.8 158.1 77.8
REMARK 620 6 GLU A 67 OE2 100.8 75.8 139.1 131.3 56.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 86.4
REMARK 620 3 ASN A 97 OD1 69.9 73.4
REMARK 620 4 TYR A 99 O 73.2 140.6 68.1
REMARK 620 5 GLU A 104 OE1 99.6 133.2 152.0 84.1
REMARK 620 6 GLU A 104 OE2 111.5 79.1 152.4 139.5 55.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 89.4
REMARK 620 3 ASP A 131 OD2 118.8 47.7
REMARK 620 4 ASP A 133 OD1 88.7 70.5 108.0
REMARK 620 5 ASP A 133 OD2 130.0 59.1 69.5 46.5
REMARK 620 6 GLN A 135 O 96.0 140.0 145.2 70.0 88.5
REMARK 620 7 GLU A 140 OE1 107.9 144.9 97.5 137.9 120.1 70.0
REMARK 620 8 GLU A 140 OE2 84.0 96.7 65.3 165.3 133.1 123.3 56.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 20 OD1
REMARK 620 2 ASP B 22 OD1 69.2
REMARK 620 3 ASP B 22 OD2 115.7 46.7
REMARK 620 4 ASP B 24 OD1 85.2 60.6 69.2
REMARK 620 5 THR B 26 O 88.5 145.7 147.3 92.9
REMARK 620 6 GLU B 31 OE1 108.7 133.9 112.1 162.3 77.0
REMARK 620 7 GLU B 31 OE2 86.2 78.7 78.8 138.8 127.0 55.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 56 OD1
REMARK 620 2 ASP B 58 OD1 74.2
REMARK 620 3 ASN B 60 OD1 80.6 72.4
REMARK 620 4 THR B 62 O 83.0 151.4 87.2
REMARK 620 5 GLU B 67 OE1 111.5 123.0 161.9 81.3
REMARK 620 6 GLU B 67 OE2 92.7 67.5 139.6 131.7 55.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 93 OD1
REMARK 620 2 ASP B 95 OD1 85.6
REMARK 620 3 ASN B 97 OD1 57.9 65.3
REMARK 620 4 ASN B 97 ND2 98.4 74.3 41.6
REMARK 620 5 TYR B 99 O 80.5 142.9 78.3 74.1
REMARK 620 6 GLU B 104 OE1 106.1 127.6 160.9 147.7 89.3
REMARK 620 7 GLU B 104 OE2 119.4 73.8 139.1 127.4 142.4 55.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 129 OD1
REMARK 620 2 ASP B 131 OD1 88.9
REMARK 620 3 ASP B 131 OD2 121.5 44.6
REMARK 620 4 ASP B 133 OD2 125.9 64.1 71.1
REMARK 620 5 ASP B 133 OD1 80.7 80.4 114.0 50.6
REMARK 620 6 GLN B 135 O 85.7 147.9 152.8 94.0 67.5
REMARK 620 7 GLU B 140 OE2 85.8 86.4 62.8 133.5 161.2 124.6
REMARK 620 8 GLU B 140 OE1 98.9 141.5 102.0 131.9 138.0 70.6 57.0
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 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPD A 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPD A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPD B 154
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LIN RELATED DB: PDB
REMARK 900 RELATED ID: 1QIV RELATED DB: PDB
DBREF 1QIW A 1 148 UNP P02593 CALM_HUMAN 1 148
DBREF 1QIW B 1 148 UNP P02593 CALM_HUMAN 1 148
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
SEQRES 1 B 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 B 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 B 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 B 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 B 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 B 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 B 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 B 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 B 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 B 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 B 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 B 148 MET MET THR ALA LYS
HET CA A 149 1
HET CA A 150 1
HET CA A 151 1
HET CA A 152 1
HET DPD A 153 28
HET DPD A 154 38
HET CA B 149 1
HET CA B 150 1
HET CA B 151 1
HET CA B 152 1
HET DPD B 154 38
HETNAM CA CALCIUM ION
HETNAM DPD N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-(2 3,4-BIS-
HETNAM 2 DPD BUTOXYPHENYL)-ETHYL]-PROPYLENEDIAMINE
FORMUL 3 CA 8(CA 2+)
FORMUL 7 DPD 3(C34 H48 N2 O2)
HELIX 1 1 THR A 5 SER A 17 1 13
HELIX 2 2 THR A 28 LEU A 39 1 12
HELIX 3 3 THR A 44 GLU A 54 1 11
HELIX 4 4 ASP A 64 ALA A 73 1 10
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 THR A 146 1 9
HELIX 9 9 ILE B 9 ASP B 20 1 12
HELIX 10 10 THR B 28 LEU B 39 1 12
HELIX 11 11 THR B 44 GLU B 54 1 11
HELIX 12 12 PHE B 65 ARG B 74 1 10
HELIX 13 13 GLU B 82 ASP B 93 1 12
HELIX 14 14 SER B 101 LEU B 112 1 12
HELIX 15 15 THR B 117 ASP B 129 1 13
HELIX 16 16 TYR B 138 THR B 146 1 9
SHEET 1 A 2 TYR A 99 ILE A 100 0
SHEET 2 A 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
SHEET 1 B 2 THR B 26 ILE B 27 0
SHEET 2 B 2 ILE B 63 ASP B 64 -1 O ILE B 63 N ILE B 27
SHEET 1 C 2 TYR B 99 ILE B 100 0
SHEET 2 C 2 VAL B 136 ASN B 137 -1 O VAL B 136 N ILE B 100
LINK OD1 ASP A 20 CA CA A 149 1555 1555 2.28
LINK OD1 ASP A 22 CA CA A 149 1555 1555 2.27
LINK OD2 ASP A 22 CA CA A 149 1555 1555 2.91
LINK OD1 ASP A 24 CA CA A 149 1555 1555 2.32
LINK O THR A 26 CA CA A 149 1555 1555 2.30
LINK OE1 GLU A 31 CA CA A 149 1555 1555 2.30
LINK OE2 GLU A 31 CA CA A 149 1555 1555 2.30
LINK OD1 ASP A 56 CA CA A 150 1555 1555 2.30
LINK OD1 ASP A 58 CA CA A 150 1555 1555 2.29
LINK OD1 ASN A 60 CA CA A 150 1555 1555 2.29
LINK O THR A 62 CA CA A 150 1555 1555 2.32
LINK OE1 GLU A 67 CA CA A 150 1555 1555 2.34
LINK OE2 GLU A 67 CA CA A 150 1555 1555 2.30
LINK OD1 ASP A 93 CA CA A 151 1555 1555 2.31
LINK OD1 ASP A 95 CA CA A 151 1555 1555 2.31
LINK OD1 ASN A 97 CA CA A 151 1555 1555 2.31
LINK O TYR A 99 CA CA A 151 1555 1555 2.31
LINK OE1 GLU A 104 CA CA A 151 1555 1555 2.32
LINK OE2 GLU A 104 CA CA A 151 1555 1555 2.32
LINK OD1 ASP A 129 CA CA A 152 1555 1555 2.31
LINK OD1 ASP A 131 CA CA A 152 1555 1555 2.92
LINK OD2 ASP A 131 CA CA A 152 1555 1555 2.31
LINK OD1 ASP A 133 CA CA A 152 1555 1555 2.30
LINK OD2 ASP A 133 CA CA A 152 1555 1555 3.01
LINK O GLN A 135 CA CA A 152 1555 1555 2.28
LINK OE1 GLU A 140 CA CA A 152 1555 1555 2.33
LINK OE2 GLU A 140 CA CA A 152 1555 1555 2.28
LINK OD1 ASP B 20 CA CA B 149 1555 1555 2.27
LINK OD1 ASP B 22 CA CA B 149 1555 1555 2.23
LINK OD2 ASP B 22 CA CA B 149 1555 1555 3.00
LINK OD1 ASP B 24 CA CA B 149 1555 1555 2.33
LINK O THR B 26 CA CA B 149 1555 1555 2.30
LINK OE1 GLU B 31 CA CA B 149 1555 1555 2.31
LINK OE2 GLU B 31 CA CA B 149 1555 1555 2.30
LINK OD1 ASP B 56 CA CA B 150 1555 1555 2.27
LINK OD1 ASP B 58 CA CA B 150 1555 1555 2.30
LINK OD1 ASN B 60 CA CA B 150 1555 1555 2.30
LINK O THR B 62 CA CA B 150 1555 1555 2.30
LINK OE1 GLU B 67 CA CA B 150 1555 1555 2.33
LINK OE2 GLU B 67 CA CA B 150 1555 1555 2.32
LINK OD1 ASP B 93 CA CA B 151 1555 1555 2.28
LINK OD1 ASP B 95 CA CA B 151 1555 1555 2.31
LINK OD1 ASN B 97 CA CA B 151 1555 1555 2.24
LINK ND2 ASN B 97 CA CA B 151 1555 1555 3.31
LINK O TYR B 99 CA CA B 151 1555 1555 2.30
LINK OE1 GLU B 104 CA CA B 151 1555 1555 2.31
LINK OE2 GLU B 104 CA CA B 151 1555 1555 2.31
LINK OD1 ASP B 129 CA CA B 152 1555 1555 2.30
LINK OD1 ASP B 131 CA CA B 152 1555 1555 2.32
LINK OD2 ASP B 131 CA CA B 152 1555 1555 3.12
LINK OD2 ASP B 133 CA CA B 152 1555 1555 2.73
LINK OD1 ASP B 133 CA CA B 152 1555 1555 2.29
LINK O GLN B 135 CA CA B 152 1555 1555 2.31
LINK OE2 GLU B 140 CA CA B 152 1555 1555 2.27
LINK OE1 GLU B 140 CA CA B 152 1555 1555 2.31
SITE 1 AC1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 5 GLU A 31
SITE 1 AC2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 5 GLU A 67
SITE 1 AC3 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 5 GLU A 104
SITE 1 AC4 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 5 GLU A 140
SITE 1 AC5 5 ASP B 20 ASP B 22 ASP B 24 THR B 26
SITE 2 AC5 5 GLU B 31
SITE 1 AC6 5 ASP B 56 ASP B 58 ASN B 60 THR B 62
SITE 2 AC6 5 GLU B 67
SITE 1 AC7 5 ASP B 93 ASP B 95 ASN B 97 TYR B 99
SITE 2 AC7 5 GLU B 104
SITE 1 AC8 5 ASP B 129 ASP B 131 ASP B 133 GLN B 135
SITE 2 AC8 5 GLU B 140
SITE 1 AC9 6 PHE A 19 LEU A 32 MET A 36 MET A 51
SITE 2 AC9 6 MET A 71 GLU A 84
SITE 1 BC1 8 GLU A 11 MET A 72 LEU A 105 MET A 124
SITE 2 BC1 8 GLU A 127 ALA A 128 MET A 144 MET A 145
SITE 1 BC2 10 GLN B 8 GLU B 11 PHE B 12 MET B 76
SITE 2 BC2 10 PHE B 92 LEU B 105 MET B 109 MET B 124
SITE 3 BC2 10 MET B 144 MET B 145
CRYST1 41.960 56.200 35.270 99.52 114.47 96.86 P 1 2
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 0.023832 0.002867 0.011868 0.00000
SCALE2 0.000000 0.017922 0.004387 0.00000
SCALE3 0.000000 0.000000 0.032070 0.00000
MTRIX1 1 -0.638671 0.193606 -0.744725 25.51900 1
MTRIX2 1 0.194159 -0.895966 -0.399434 72.21450 1
MTRIX3 1 -0.744581 -0.399702 0.534637 31.11850 1
(ATOM LINES ARE NOT SHOWN.)
END
