HEADER HYDROLASE 07-AUG-02 1MDW
TITLE CRYSTAL STRUCTURE OF CALCIUM-BOUND PROTEASE CORE OF CALPAIN II REVEALS
TITLE 2 THE BASIS FOR INTRINSIC INACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALPAIN II, CATALYTIC SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PROTEASE CORE DOMAINS I AND II (RESIDUES 17-346);
COMPND 5 SYNONYM: CALCIUM-ACTIVATED NEUTRAL PROTEINASE, CANP, M-TYPE, M-
COMPND 6 CALPAIN, MILLIMOLAR-CALPAIN;
COMPND 7 EC: 3.4.22.17;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CALPAIN II;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24D
KEYWDS CALPAIN CYSTEINE PROTEASE FOLD, TWO COOPERATIVE CALCIUM SITES, HELIX
KEYWDS 2 INSTABILITY, TRYPTOPHAN-BASED ACTIVE SITE BLOCKAGE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.MOLDOVEANU,C.M.HOSFIELD,D.LIM,Z.JIA,P.L.DAVIES
REVDAT 4 14-FEB-24 1MDW 1 REMARK
REVDAT 3 27-OCT-21 1MDW 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1MDW 1 VERSN
REVDAT 1 29-APR-03 1MDW 0
JRNL AUTH T.MOLDOVEANU,C.M.HOSFIELD,D.LIM,Z.JIA,P.L.DAVIES
JRNL TITL CALPAIN SILENCING BY A REVERSIBLE INTRINSIC MECHANISM.
JRNL REF NAT.STRUCT.BIOL. V. 10 371 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 12665854
JRNL DOI 10.1038/NSB917
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.MOLDOVEANU,C.M.HOSFIELD,D.LIM,J.S.ELCE,Z.JIA,P.L.DAVIES
REMARK 1 TITL A CA(2+) SWITCH ALIGNS THE ACTIVE SITE OF CALPAIN
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 108 649 2002
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(02)00659-1
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.M.HOSFIELD,J.S.ELCE,P.L.DAVIES,Z.JIA
REMARK 1 TITL CRYSTAL STRUCTURE OF CALPAIN REVEALS THE STRUCTURAL BASIS
REMARK 1 TITL 2 FOR CA(2+)-DEPENDENT PROTEASE ACTIVITY AND A NOVEL MODE OF
REMARK 1 TITL 3 ENZYME ACTIVATION
REMARK 1 REF EMBO J. V. 18 6880 1999
REMARK 1 REFN ISSN 0261-4189
REMARK 1 DOI 10.1093/EMBOJ/18.24.6880
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 48591
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) : 0.207
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2437
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 5040
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 365
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MDW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016839.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-SEP-01
REMARK 200 TEMPERATURE (KELVIN) : 100
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48591
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 (%) : 93.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : 0.03500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.35600
REMARK 200 R SYM FOR SHELL (I) : 0.32600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG6000, 0.1M SODIUM ACETATE, 30MM
REMARK 280 CALCIUM CHLORIDE, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.30000
REMARK 290 SMTRY3 2 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE MONOMER OF THE DIMER IN THE
REMARK 300 ASSYMETRIC UNIT
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 GLY A 19
REMARK 465 SER A 20
REMARK 465 HIS A 21
REMARK 465 GLY A 198
REMARK 465 ALA A 199
REMARK 465 THR A 200
REMARK 465 THR A 201
REMARK 465 PRO A 345
REMARK 465 ASP A 346
REMARK 465 GLY B 19
REMARK 465 SER B 20
REMARK 465 HIS B 21
REMARK 465 GLU B 22
REMARK 465 GLY B 197
REMARK 465 GLY B 198
REMARK 465 ALA B 199
REMARK 465 THR B 200
REMARK 465 THR B 201
REMARK 465 ASP B 346
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 GLU A 22 CG CD OE1 OE2
REMARK 470 GLU A 41 CG CD OE1 OE2
REMARK 470 GLU A 202 CG CD OE1 OE2
REMARK 470 ILE A 211 CG1 CG2 CD1
REMARK 470 GLU A 310 CG CD OE1 OE2
REMARK 470 GLU B 41 CG CD OE1 OE2
REMARK 470 GLU B 202 CG CD OE1 OE2
REMARK 470 ILE B 211 CG1 CG2 CD1
REMARK 470 GLU B 310 CG CD OE1 OE2
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 O HOH A 349 O HOH A 444 0.00
REMARK 500 O HOH A 502 O HOH A 506 0.00
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 LEU A 28 19.93 56.67
REMARK 500 ASP A 48 109.23 -56.15
REMARK 500 LYS A 61 -80.76 -134.93
REMARK 500 ASP A 104 48.07 -108.96
REMARK 500 ASP A 128 33.38 -77.73
REMARK 500 GLN A 132 -88.19 -95.32
REMARK 500 ALA A 136 24.52 -145.32
REMARK 500 PHE A 167 -138.05 -99.35
REMARK 500 ALA A 269 119.78 -164.32
REMARK 500 VAL A 291 95.86 66.62
REMARK 500 ALA B 24 107.62 74.18
REMARK 500 LYS B 61 -80.88 -132.01
REMARK 500 ASP B 128 42.72 -101.76
REMARK 500 GLN B 132 -84.91 -111.76
REMARK 500 TYR B 146 49.37 35.20
REMARK 500 PHE B 167 -136.56 -97.44
REMARK 500 GLU B 205 -53.12 -28.11
REMARK 500 THR B 245 -71.81 -85.80
REMARK 500 ALA B 269 117.18 -167.10
REMARK 500 SER B 277 136.77 169.04
REMARK 500 VAL B 291 95.99 71.21
REMARK 500 TRP B 297 5.84 84.83
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 A 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 89 O
REMARK 620 2 GLY A 91 O 78.2
REMARK 620 3 ASP A 96 OD1 155.0 122.3
REMARK 620 4 ASP A 96 OD2 151.4 80.7 53.3
REMARK 620 5 GLU A 175 OE1 104.7 138.9 70.3 79.4
REMARK 620 6 GLU A 175 OE2 80.2 89.2 111.7 80.5 52.2
REMARK 620 7 HOH A 347 O 89.1 66.7 87.1 100.0 152.5 155.2
REMARK 620 8 HOH A 348 O 74.4 134.2 80.7 134.0 83.9 120.6 76.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 292 OE1
REMARK 620 2 GLU A 292 OE2 51.6
REMARK 620 3 ASP A 299 OD1 134.4 82.9
REMARK 620 4 ASP A 299 OD2 117.4 80.2 40.0
REMARK 620 5 GLN A 319 O 80.4 108.8 117.9 80.8
REMARK 620 6 ASP A 321 OD1 74.2 122.0 147.3 152.4 76.6
REMARK 620 7 GLU A 323 O 91.6 78.7 80.1 118.3 160.8 84.5
REMARK 620 8 HOH A 349 O 157.4 151.0 68.2 79.5 88.1 84.2 93.0
REMARK 620 9 HOH A 444 O 157.4 151.0 68.2 79.5 88.1 84.2 93.0 0.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 89 O
REMARK 620 2 GLY B 91 O 80.9
REMARK 620 3 ASP B 96 OD2 152.4 78.1
REMARK 620 4 ASP B 96 OD1 155.6 120.5 51.6
REMARK 620 5 GLU B 175 OE2 80.5 86.1 80.3 110.6
REMARK 620 6 GLU B 175 OE1 103.5 136.1 80.1 70.2 52.8
REMARK 620 7 HOH B 413 O 91.0 68.2 97.6 87.1 153.9 152.9
REMARK 620 8 HOH B 414 O 76.8 137.2 130.7 79.2 124.8 84.9 76.1
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 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 292 OE2
REMARK 620 2 GLU B 292 OE1 52.6
REMARK 620 3 ASP B 299 OD2 76.6 112.0
REMARK 620 4 ASP B 299 OD1 85.4 137.5 41.4
REMARK 620 5 GLN B 319 O 103.6 74.8 77.6 114.9
REMARK 620 6 ASP B 321 OD1 119.1 70.3 152.7 150.7 77.0
REMARK 620 7 GLU B 323 O 81.1 94.5 121.5 83.8 160.9 84.5
REMARK 620 8 HOH B 367 O 153.8 153.4 83.6 68.4 88.5 86.0 95.1
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KXR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CALCIUM-BOUND CALPAIN I REVEALS THE ACTIVATION
REMARK 900 MECHANISM OF CALPAINS
REMARK 900 RELATED ID: 1KFU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN M-CALPAIN FORM II
REMARK 900 RELATED ID: 1KFX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CALCIUM-FREE HUMAN CALPAIN II HETERODIMER -
REMARK 900 CRYSTAL FORM II
REMARK 900 RELATED ID: 1DFO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RAT M-CALPAIN
REMARK 900 RELATED ID: 1AJ5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RAT CALPAIN SMALL SUBUNIT DVI - APO
REMARK 900 RELATED ID: 1ALW RELATED DB: PDB
REMARK 900 INHIBITOR AND CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN
DBREF 1MDW A 19 346 UNP Q07009 CAN2_RAT 19 346
DBREF 1MDW B 19 346 UNP Q07009 CAN2_RAT 19 346
SEQADV 1MDW SER A 105 UNP Q07009 CYS 105 ENGINEERED MUTATION
SEQADV 1MDW SER B 105 UNP Q07009 CYS 105 ENGINEERED MUTATION
SEQRES 1 A 328 GLY SER HIS GLU ARG ALA ILE LYS TYR LEU ASN GLN ASP
SEQRES 2 A 328 TYR GLU THR LEU ARG ASN GLU CYS LEU GLU ALA GLY ALA
SEQRES 3 A 328 LEU PHE GLN ASP PRO SER PHE PRO ALA LEU PRO SER SER
SEQRES 4 A 328 LEU GLY PHE LYS GLU LEU GLY PRO TYR SER SER LYS THR
SEQRES 5 A 328 ARG GLY ILE GLU TRP LYS ARG PRO THR GLU ILE CYS ALA
SEQRES 6 A 328 ASP PRO GLN PHE ILE ILE GLY GLY ALA THR ARG THR ASP
SEQRES 7 A 328 ILE CYS GLN GLY ALA LEU GLY ASP SER TRP LEU LEU ALA
SEQRES 8 A 328 ALA ILE ALA SER LEU THR LEU ASN GLU GLU ILE LEU ALA
SEQRES 9 A 328 ARG VAL VAL PRO LEU ASP GLN SER PHE GLN GLU ASN TYR
SEQRES 10 A 328 ALA GLY ILE PHE HIS PHE GLN PHE TRP GLN TYR GLY GLU
SEQRES 11 A 328 TRP VAL GLU VAL VAL VAL ASP ASP ARG LEU PRO THR LYS
SEQRES 12 A 328 ASP GLY GLU LEU LEU PHE VAL HIS SER ALA GLU GLY SER
SEQRES 13 A 328 GLU PHE TRP SER ALA LEU LEU GLU LYS ALA TYR ALA LYS
SEQRES 14 A 328 ILE ASN GLY CYS TYR GLU ALA LEU SER GLY GLY ALA THR
SEQRES 15 A 328 THR GLU GLY PHE GLU ASP PHE THR GLY GLY ILE ALA GLU
SEQRES 16 A 328 TRP TYR GLU LEU ARG LYS PRO PRO PRO ASN LEU PHE LYS
SEQRES 17 A 328 ILE ILE GLN LYS ALA LEU GLU LYS GLY SER LEU LEU GLY
SEQRES 18 A 328 CYS SER ILE ASP ILE THR SER ALA ALA ASP SER GLU ALA
SEQRES 19 A 328 VAL THR TYR GLN LYS LEU VAL LYS GLY HIS ALA TYR SER
SEQRES 20 A 328 VAL THR GLY ALA GLU GLU VAL GLU SER SER GLY SER LEU
SEQRES 21 A 328 GLN LYS LEU ILE ARG ILE ARG ASN PRO TRP GLY GLN VAL
SEQRES 22 A 328 GLU TRP THR GLY LYS TRP ASN ASP ASN CYS PRO SER TRP
SEQRES 23 A 328 ASN THR VAL ASP PRO GLU VAL ARG ALA ASN LEU THR GLU
SEQRES 24 A 328 ARG GLN GLU ASP GLY GLU PHE TRP MET SER PHE SER ASP
SEQRES 25 A 328 PHE LEU ARG HIS TYR SER ARG LEU GLU ILE CYS ASN LEU
SEQRES 26 A 328 THR PRO ASP
SEQRES 1 B 328 GLY SER HIS GLU ARG ALA ILE LYS TYR LEU ASN GLN ASP
SEQRES 2 B 328 TYR GLU THR LEU ARG ASN GLU CYS LEU GLU ALA GLY ALA
SEQRES 3 B 328 LEU PHE GLN ASP PRO SER PHE PRO ALA LEU PRO SER SER
SEQRES 4 B 328 LEU GLY PHE LYS GLU LEU GLY PRO TYR SER SER LYS THR
SEQRES 5 B 328 ARG GLY ILE GLU TRP LYS ARG PRO THR GLU ILE CYS ALA
SEQRES 6 B 328 ASP PRO GLN PHE ILE ILE GLY GLY ALA THR ARG THR ASP
SEQRES 7 B 328 ILE CYS GLN GLY ALA LEU GLY ASP SER TRP LEU LEU ALA
SEQRES 8 B 328 ALA ILE ALA SER LEU THR LEU ASN GLU GLU ILE LEU ALA
SEQRES 9 B 328 ARG VAL VAL PRO LEU ASP GLN SER PHE GLN GLU ASN TYR
SEQRES 10 B 328 ALA GLY ILE PHE HIS PHE GLN PHE TRP GLN TYR GLY GLU
SEQRES 11 B 328 TRP VAL GLU VAL VAL VAL ASP ASP ARG LEU PRO THR LYS
SEQRES 12 B 328 ASP GLY GLU LEU LEU PHE VAL HIS SER ALA GLU GLY SER
SEQRES 13 B 328 GLU PHE TRP SER ALA LEU LEU GLU LYS ALA TYR ALA LYS
SEQRES 14 B 328 ILE ASN GLY CYS TYR GLU ALA LEU SER GLY GLY ALA THR
SEQRES 15 B 328 THR GLU GLY PHE GLU ASP PHE THR GLY GLY ILE ALA GLU
SEQRES 16 B 328 TRP TYR GLU LEU ARG LYS PRO PRO PRO ASN LEU PHE LYS
SEQRES 17 B 328 ILE ILE GLN LYS ALA LEU GLU LYS GLY SER LEU LEU GLY
SEQRES 18 B 328 CYS SER ILE ASP ILE THR SER ALA ALA ASP SER GLU ALA
SEQRES 19 B 328 VAL THR TYR GLN LYS LEU VAL LYS GLY HIS ALA TYR SER
SEQRES 20 B 328 VAL THR GLY ALA GLU GLU VAL GLU SER SER GLY SER LEU
SEQRES 21 B 328 GLN LYS LEU ILE ARG ILE ARG ASN PRO TRP GLY GLN VAL
SEQRES 22 B 328 GLU TRP THR GLY LYS TRP ASN ASP ASN CYS PRO SER TRP
SEQRES 23 B 328 ASN THR VAL ASP PRO GLU VAL ARG ALA ASN LEU THR GLU
SEQRES 24 B 328 ARG GLN GLU ASP GLY GLU PHE TRP MET SER PHE SER ASP
SEQRES 25 B 328 PHE LEU ARG HIS TYR SER ARG LEU GLU ILE CYS ASN LEU
SEQRES 26 B 328 THR PRO ASP
HET CA A 1 1
HET CA A 2 1
HET CA B 3 1
HET CA B 4 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *365(H2 O)
HELIX 1 1 LEU A 28 GLN A 30 5 3
HELIX 2 2 ASP A 31 GLY A 43 1 13
HELIX 3 3 LEU A 54 GLY A 59 1 6
HELIX 4 4 SER A 67 ARG A 71 5 5
HELIX 5 5 ARG A 77 CYS A 82 1 6
HELIX 6 6 THR A 93 ILE A 97 5 5
HELIX 7 7 ASP A 104 THR A 115 1 12
HELIX 8 8 ASN A 117 VAL A 125 1 9
HELIX 9 9 PHE A 176 ASN A 189 1 14
HELIX 10 10 CYS A 191 SER A 196 5 6
HELIX 11 11 PHE A 204 THR A 208 5 5
HELIX 12 12 ASN A 223 LYS A 234 1 12
HELIX 13 13 SER A 246 SER A 250 5 5
HELIX 14 14 CYS A 301 VAL A 307 5 7
HELIX 15 15 ASP A 308 THR A 316 1 9
HELIX 16 16 PHE A 328 TYR A 335 1 8
HELIX 17 17 LEU B 28 GLN B 30 5 3
HELIX 18 18 ASP B 31 GLY B 43 1 13
HELIX 19 19 LEU B 54 GLY B 59 1 6
HELIX 20 20 SER B 67 ARG B 71 5 5
HELIX 21 21 ARG B 77 CYS B 82 1 6
HELIX 22 22 THR B 93 ILE B 97 5 5
HELIX 23 23 ASP B 104 THR B 115 1 12
HELIX 24 24 ASN B 117 VAL B 125 1 9
HELIX 25 25 PHE B 176 GLY B 190 1 15
HELIX 26 26 CYS B 191 SER B 196 5 6
HELIX 27 27 PHE B 204 GLY B 209 1 6
HELIX 28 28 ASN B 223 LYS B 234 1 12
HELIX 29 29 SER B 246 SER B 250 5 5
HELIX 30 30 CYS B 301 VAL B 307 5 7
HELIX 31 31 ASP B 308 THR B 316 1 9
HELIX 32 32 PHE B 328 TYR B 335 1 8
SHEET 1 A 3 ILE A 25 LYS A 26 0
SHEET 2 A 3 GLU A 148 ASP A 155 1 O TRP A 149 N ILE A 25
SHEET 3 A 3 ILE A 138 GLN A 145 -1 N PHE A 143 O VAL A 150
SHEET 1 B 3 GLU A 74 LYS A 76 0
SHEET 2 B 3 LEU A 158 LYS A 161 -1 O LEU A 158 N LYS A 76
SHEET 3 B 3 GLU A 164 LEU A 165 -1 O GLU A 164 N LYS A 161
SHEET 1 C 6 ILE A 211 GLU A 216 0
SHEET 2 C 6 ARG A 337 ASN A 342 -1 O ILE A 340 N GLU A 213
SHEET 3 C 6 LEU A 237 SER A 241 -1 N GLY A 239 O GLU A 339
SHEET 4 C 6 TYR A 264 SER A 274 -1 O TYR A 264 N CYS A 240
SHEET 5 C 6 SER A 277 ARG A 285 -1 O LEU A 281 N GLU A 270
SHEET 6 C 6 GLU A 323 SER A 327 -1 O PHE A 324 N ILE A 284
SHEET 1 D 3 ILE B 25 LYS B 26 0
SHEET 2 D 3 GLU B 148 ASP B 155 1 O GLU B 151 N ILE B 25
SHEET 3 D 3 ILE B 138 GLN B 145 -1 N PHE B 143 O VAL B 150
SHEET 1 E 3 GLU B 74 LYS B 76 0
SHEET 2 E 3 LEU B 158 LYS B 161 -1 O THR B 160 N GLU B 74
SHEET 3 E 3 GLU B 164 LEU B 165 -1 O GLU B 164 N LYS B 161
SHEET 1 F 6 ILE B 211 GLU B 216 0
SHEET 2 F 6 ARG B 337 ASN B 342 -1 O ILE B 340 N GLU B 213
SHEET 3 F 6 LEU B 237 SER B 241 -1 N GLY B 239 O GLU B 339
SHEET 4 F 6 TYR B 264 GLU B 273 -1 O TYR B 264 N CYS B 240
SHEET 5 F 6 LEU B 278 ARG B 285 -1 O GLN B 279 N VAL B 272
SHEET 6 F 6 GLU B 323 SER B 327 -1 O PHE B 324 N ILE B 284
LINK CA CA A 1 O ILE A 89 1555 1555 2.38
LINK CA CA A 1 O GLY A 91 1555 1555 2.45
LINK CA CA A 1 OD1 ASP A 96 1555 1555 2.49
LINK CA CA A 1 OD2 ASP A 96 1555 1555 2.41
LINK CA CA A 1 OE1 GLU A 175 1555 1555 2.50
LINK CA CA A 1 OE2 GLU A 175 1555 1555 2.48
LINK CA CA A 1 O HOH A 347 1555 1555 2.45
LINK CA CA A 1 O HOH A 348 1555 1555 2.44
LINK CA CA A 2 OE1 GLU A 292 1555 1555 2.45
LINK CA CA A 2 OE2 GLU A 292 1555 1555 2.58
LINK CA CA A 2 OD1 ASP A 299 1555 1555 3.38
LINK CA CA A 2 OD2 ASP A 299 1555 1555 2.25
LINK CA CA A 2 O GLN A 319 1555 1555 2.36
LINK CA CA A 2 OD1 ASP A 321 1555 1555 2.57
LINK CA CA A 2 O GLU A 323 1555 1555 2.31
LINK CA CA A 2 O HOH A 349 1555 1555 2.30
LINK CA CA A 2 O HOH A 444 1555 1555 2.30
LINK CA CA B 3 O ILE B 89 1555 1555 2.38
LINK CA CA B 3 O GLY B 91 1555 1555 2.45
LINK CA CA B 3 OD2 ASP B 96 1555 1555 2.57
LINK CA CA B 3 OD1 ASP B 96 1555 1555 2.47
LINK CA CA B 3 OE2 GLU B 175 1555 1555 2.46
LINK CA CA B 3 OE1 GLU B 175 1555 1555 2.49
LINK CA CA B 3 O HOH B 413 1555 1555 2.29
LINK CA CA B 3 O HOH B 414 1555 1555 2.31
LINK CA CA B 4 OE2 GLU B 292 1555 1555 2.46
LINK CA CA B 4 OE1 GLU B 292 1555 1555 2.52
LINK CA CA B 4 OD2 ASP B 299 1555 1555 2.29
LINK CA CA B 4 OD1 ASP B 299 1555 1555 3.30
LINK CA CA B 4 O GLN B 319 1555 1555 2.49
LINK CA CA B 4 OD1 ASP B 321 1555 1555 2.53
LINK CA CA B 4 O GLU B 323 1555 1555 2.27
LINK CA CA B 4 O HOH B 367 1555 1555 2.39
SITE 1 AC1 6 ILE A 89 GLY A 91 ASP A 96 GLU A 175
SITE 2 AC1 6 HOH A 347 HOH A 348
SITE 1 AC2 7 GLU A 292 ASP A 299 GLN A 319 ASP A 321
SITE 2 AC2 7 GLU A 323 HOH A 349 HOH A 444
SITE 1 AC3 6 ILE B 89 GLY B 91 ASP B 96 GLU B 175
SITE 2 AC3 6 HOH B 413 HOH B 414
SITE 1 AC4 6 GLU B 292 ASP B 299 GLN B 319 ASP B 321
SITE 2 AC4 6 GLU B 323 HOH B 367
CRYST1 62.600 80.600 75.300 90.00 103.90 90.00 P 1 21 1 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 0.015974 0.000000 0.003953 0.00000
SCALE2 0.000000 0.012407 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013681 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
