HEADER CALCIUM-BINDING PROTEIN 17-JUN-99 1QIW TITLE CALMODULIN COMPLEXED WITH N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-( TITLE 2 3,4-BIS-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 ORGAN: BRAIN; SOURCE 5 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 1 28-MAR-00 1QIW 0 JRNL AUTH V.HARMAT,Z.S.BOCSKEI,G.NARAY-SZABO,I.BATA, JRNL AUTH 2 A.S.CSUTOR,I.HERMECZ,P.ARANYI,B.SZABO,K.LILIOM, JRNL AUTH 3 B.G.VERTESSY,J.OVADI JRNL TITL A NEW POTENT CALMODULIN ANTAGONIST WITH JRNL TITL 2 ARYLALKYLAMINE STRUCTURE: CRYSTALLOGRAPHIC, JRNL TITL 3 SPECTROSCOPIC AND FUNCTIONAL STUDIES JRNL REF J.MOL.BIOL. V. 297 747 2000 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.G.VERTESSY,Z.S.BOCSKEI,V.HARMAT,G.NARAY-SZABO, REMARK 1 AUTH 2 J.OVADI REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY DIFFRACTION REMARK 1 TITL 2 ANALYSIS OF CA2+-CALMODULIN-DRUG AND REMARK 1 TITL 3 APOCALMODULIN-DRUG COMPLEXES REMARK 1 REF PROTEINS: STRUCT.,FUNCT., V. 28 131 1997 REMARK 1 REF 2 GENET. REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 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 ASTM NSBIEW US ISSN 1072-8368 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 ASTM BICHAW US ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. 2.3 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 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 69.24 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 (%) : 5.5 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) : 2.3 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.4 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 24.39 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 370 REMARK 3 BIN R VALUE (WORKING SET) : 0.105 REMARK 3 BIN FREE R VALUE : 0.280 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) : 26.7 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.8 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -7.008 REMARK 3 B22 (A**2) : -12.279 REMARK 3 B33 (A**2) : -14.919 REMARK 3 B12 (A**2) : -0.196 REMARK 3 B13 (A**2) : -1.001 REMARK 3 B23 (A**2) : -2.453 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.263 REMARK 3 ESD FROM SIGMAA (A) : 0.0962 REMARK 3 LOW RESOLUTION CUTOFF (A) : 2.7 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.423 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.410 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 : RESTRAINTS REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : 0.098 ; 25 REMARK 3 GROUP 1 B-FACTOR (A**2) : 6.00 ; 5 REMARK 3 GROUP 2 POSITIONAL (A) : 0.499 ; 20 REMARK 3 GROUP 2 B-FACTOR (A**2) : 7.14 ; 8 REMARK 3 GROUP 3 POSITIONAL (A) : 0.078 ; 50 REMARK 3 GROUP 3 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 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : CA.TOP REMARK 3 TOPOLOGY FILE 3 : AAA.TOP REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED SIDE CHAIN ATOMS OF REMARK 3 RESIDUES A2, A7, A47, A78, A79, A86, A114, A123, B6, B13, REMARK 3 B69, B77, B82, B84, B123, B127 AND 146 AS WELL AS REMARK 3 TRIMETHYL-LYSINES A115, B115 ARE NOT PRESENT IN THE STRUCTURE REMARK 3 TEMPERATURE FACTORS FOR THE ATOMS IN THE CENTRAL REGIONS REMARK 3 (A73-A80, B75-B82),ATOMS AT THE ENDS OF THE POLIPEPTIDE REMARK 3 CHAINS (A144-A146, B4-B7, B144) AS WELL AS FOR SOME SURFACE REMARK 3 RESIDUES (A45, A84, A107, A112, B107, B119, B126) ARE REMARK 3 UNUSUALLY HIGH, INDICATING FLEXIBILITY IN THESE PARTS OF REMARK 3 THE STRUCTURE. REMARK 3 THE C-TERMINAL RESIDUES FOR BOTH CHAINS A AND B WERE NOT REMARK 3 SEEN IN THE DENSITY MAPS REMARK 4 REMARK 4 1QIW COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 6-JUL-1999. REMARK 100 THE EBI ID CODE IS EBI-2825. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-APR-1996 REMARK 200 TEMPERATURE (KELVIN) : 298 REMARK 200 PH : 6.0 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 REMARK 200 OPTICS : NORMAL FOCUS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU R-AXIS IIC 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) : 2.30 REMARK 200 RESOLUTION RANGE LOW (A) : 54.23 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 69.24 REMARK 200 DATA REDUNDANCY : 1.7 REMARK 200 R MERGE (I) : 0.137 REMARK 200 R SYM (I) : 0.093 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.1 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 : 1.4 REMARK 200 R MERGE FOR SHELL (I) : 0.705 REMARK 200 R SYM FOR SHELL (I) : 0.513 REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.3 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 REMARK 200 MODELS REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.185 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED BY REMARK 280 HANGING DROP TECHNIQUE. 50 MM PH=6.0 SODIUM CACODYLATE/HCL REMARK 280 BUFFER, 10 MM MGCL2, 10 MM CACL2, 2MM DPD AND 30% PEG 8000 REMARK 280 THE CRYSTAL COULD NOT BE REPRODUCED. 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 295 REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY. REMARK 295 REMARK 295 APPLIED TO TRANSFORMED TO REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD REMARK 295 SSS REMARK 295 M 1 A 11 .. 144 B 11 .. 144 0.356 REMARK 295 REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS REMARK 295 REMARK 295 REMARK: THE TRANSFORMATION RELATES CHAIN B TO CHAIN A REMARK 285 THE MATRIX WAS CALCULATED FOR THE ATOMS RESTRAINED DURING THE REMARK 295 REFINEMENT (RESIDUES 11-38, 45-68, 84-112, 118-144 WITH REMARK 295 THE EXCEPTION OF SIDE CHAINS WITH DIFFERENT CONFORMATIONS REMARK 295 BETWEEN THE TWO CHAINS) REMARK 300 REMARK 300 BIOMOLECULE REMARK 300 THE ASYMMETRIC UNIT CONTAINS 2 REMARK 300 INDEPENDENT COPIES OF THE MOLECULAR COMPLEX REMARK 300 REMARK 300 BIOLOGICAL UNIT: MONOMER 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 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 470 DPD A 153 O3 C41 C42 C43 C44 O4 C51 C52 C53 C54 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASN B 97 OD1 - CG - ND2 ANGL. DEV. = -8.2 DEGREES REMARK 500 ASN B 97 CB - CG - ND2 ANGL. DEV. = 9.6 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 REMARK 500 OD1 ASP B 93 OD1 ASN B 97 2.19 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: A1 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: A2 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: A3 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: A4 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: B1 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: B2 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: B3 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 800 SITE_IDENTIFIER: B4 REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE REMARK 800 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LIN RELATED DB: PDB REMARK 900 RELATED ID: 1QIV RELATED DB: PDB REMARK 900 DBREF 1QIW A 1 148 SWS P02593 CALM_HUMAN 1 148 DBREF 1QIW B 1 148 SWS 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 CA B 149 1 HET CA B 150 1 HET CA B 151 1 HET CA B 152 1 HET DPD A 153 28 HET DPD A 154 38 HET DPD B 154 38 HETNAM CA CALCIUM ION HETNAM DPD N-(3,3-DIPHENYLPROPYL)-N'-[1-R-(3,4-BIS-BUTOXYPHENYL)ETHYL]- HETNAM 2 DPD PROPYLENEDIAMINE FORMUL 3 CA 8(CA1 2+) FORMUL 4 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 CA CA A 149 CD GLU A 31 LINK CA CA A 149 CG ASP A 22 LINK CA CA A 149 O THR A 26 LINK CA CA A 149 OD1 ASP A 20 LINK CA CA A 149 OD1 ASP A 22 LINK CA CA A 149 OD1 ASP A 24 LINK CA CA A 149 OD2 ASP A 22 LINK CA CA A 149 OE1 GLU A 31 LINK CA CA A 149 OE2 GLU A 31 LINK CA CA A 150 CD GLU A 67 LINK CA CA A 150 CG ASP A 58 LINK CA CA A 150 O THR A 62 LINK CA CA A 150 OD1 ASN A 60 LINK CA CA A 150 OD1 ASP A 56 LINK CA CA A 150 OD1 ASP A 58 LINK CA CA A 150 OE1 GLU A 67 LINK CA CA A 150 OE2 GLU A 67 LINK CA CA A 151 CD GLU A 104 LINK CA CA A 151 O TYR A 99 LINK CA CA A 151 OD1 ASN A 97 LINK CA CA A 151 OD1 ASP A 93 LINK CA CA A 151 OD1 ASP A 95 LINK CA CA A 151 OE1 GLU A 104 LINK CA CA A 151 OE2 GLU A 104 LINK CA CA A 152 CD GLU A 140 LINK CA CA A 152 CG ASP A 129 LINK CA CA A 152 CG ASP A 131 LINK CA CA A 152 CG ASP A 133 LINK CA CA A 152 O GLN A 135 LINK CA CA A 152 OD1 ASP A 129 LINK CA CA A 152 OD1 ASP A 131 LINK CA CA A 152 OD1 ASP A 133 LINK CA CA A 152 OD2 ASP A 131 LINK CA CA A 152 OD2 ASP A 133 LINK CA CA A 152 OE1 GLU A 140 LINK CA CA A 152 OE2 GLU A 140 LINK CA CA B 149 CD GLU B 31 LINK CA CA B 149 CG ASP B 22 LINK CA CA B 149 O THR B 26 LINK CA CA B 149 OD1 ASP B 20 LINK CA CA B 149 OD1 ASP B 22 LINK CA CA B 149 OD1 ASP B 24 LINK CA CA B 149 OD2 ASP B 22 LINK CA CA B 149 OE1 GLU B 31 LINK CA CA B 149 OE2 GLU B 31 LINK CA CA B 150 CD GLU B 67 LINK CA CA B 150 CG ASP B 58 LINK CA CA B 150 O THR B 62 LINK CA CA B 150 OD1 ASN B 60 LINK CA CA B 150 OD1 ASP B 56 LINK CA CA B 150 OD1 ASP B 58 LINK CA CA B 150 OE1 GLU B 67 LINK CA CA B 150 OE2 GLU B 67 LINK CA CA B 151 CD GLU B 104 LINK CA CA B 151 CG ASN B 97 LINK CA CA B 151 O TYR B 99 LINK CA CA B 151 OD1 ASN B 97 LINK CA CA B 151 OD1 ASP B 93 LINK CA CA B 151 OD1 ASP B 95 LINK CA CA B 151 OE1 GLU B 104 LINK CA CA B 151 OE2 GLU B 104 LINK CA CA B 152 CD GLU B 140 LINK CA CA B 152 CG ASP B 131 LINK CA CA B 152 CG ASP B 133 LINK CA CA B 152 O GLN B 135 LINK CA CA B 152 OD1 ASP B 129 LINK CA CA B 152 OD1 ASP B 131 LINK CA CA B 152 OD1 ASP B 133 LINK CA CA B 152 OD2 ASP B 131 LINK CA CA B 152 OD2 ASP B 133 LINK CA CA B 152 OE1 GLU B 140 LINK CA CA B 152 OE2 GLU B 140 SITE 1 A1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26 SITE 2 A1 5 GLU A 31 SITE 1 A2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62 SITE 2 A2 5 GLU A 67 SITE 1 A3 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99 SITE 2 A3 5 GLU A 104 SITE 1 A4 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135 SITE 2 A4 5 GLU A 140 SITE 1 B1 5 ASP B 20 ASP B 22 ASP B 24 THR B 26 SITE 2 B1 5 GLU B 31 SITE 1 B2 5 ASP B 56 ASP B 58 ASN B 60 THR B 62 SITE 2 B2 5 GLU B 67 SITE 1 B3 5 ASP B 93 ASP B 95 ASN B 97 TYR B 99 SITE 2 B3 5 GLU B 104 SITE 1 B4 5 ASP B 129 ASP B 131 ASP B 133 GLN B 135 SITE 2 B4 5 GLU B 140 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