HEADER HYDROLASE 07-FEB-03 1NX2
TITLE CALPAIN DOMAIN VI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM-DEPENDENT PROTEASE, SMALL SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN VI;
COMPND 5 SYNONYM: CALPAIN REGULATORY SUBUNIT, CALCIUM-ACTIVATED NEUTRAL
COMPND 6 PROTEINASE, CANP;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: CAPNS1 OR CAPN4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, CALCIUM BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR B.TODD,D.MOORE,C.C.S.DEIVANAYAGAM,G.-D.LIN,D.CHATTOPADHYAY,M.MAKI,
AUTHOR 2 K.K.W.WANG,S.V.L.NARAYANA
REVDAT 5 14-FEB-24 1NX2 1 REMARK LINK
REVDAT 4 02-MAY-12 1NX2 1 COMPND
REVDAT 3 13-JUL-11 1NX2 1 VERSN
REVDAT 2 24-FEB-09 1NX2 1 VERSN
REVDAT 1 19-AUG-03 1NX2 0
JRNL AUTH B.TODD,D.MOORE,C.C.S.DEIVANAYAGAM,G.-D.LIN,D.CHATTOPADHYAY,
JRNL AUTH 2 M.MAKI,K.K.W.WANG,S.V.L.NARAYANA
JRNL TITL A STRUCTURAL MODEL FOR THE INHIBITION OF CALPAIN BY
JRNL TITL 2 CALPASTATIN: CRYSTAL STRUCTURES OF THE NATIVE DOMAIN VI OF
JRNL TITL 3 CALPAIN AND ITS COMPLEXES WITH CALPASTATIN PEPTIDE AND A
JRNL TITL 4 SMALL MOLECULE INHIBITOR.
JRNL REF J.MOL.BIOL. V. 328 131 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12684003
JRNL DOI 10.1016/S0022-2836(03)00274-2
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
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 : 14531
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) : 0.221
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1453
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 : 1395
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 86
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) : NULL
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 1NX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018303.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : NULL
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
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 : 14531
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, BME, EDTA, CACL2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 25.92533
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 51.85067
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 51.85067
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 25.92533
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 25.92533
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 ASP A 135 OD1
REMARK 620 2 ASP A 223 OD1 125.1
REMARK 620 3 ASP A 223 OD2 76.5 51.9
REMARK 620 4 ASP A 225 OD1 77.5 71.7 73.5
REMARK 620 5 ASP A 225 OD2 93.0 102.7 126.5 53.1
REMARK 620 6 ASN A 226 ND2 157.7 74.4 125.2 102.0 70.3
REMARK 620 N 1 2 3 4 5
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 ASP A 150 OD1
REMARK 620 2 ASP A 152 OD1 82.4
REMARK 620 3 THR A 154 OG1 82.4 85.0
REMARK 620 4 LYS A 156 O 86.0 153.0 69.3
REMARK 620 5 GLU A 161 OE2 97.2 74.9 159.8 131.0
REMARK 620 6 GLU A 161 OE1 113.5 124.2 147.1 82.8 51.0
REMARK 620 7 HOH A 273 O 162.3 84.0 85.2 101.3 90.1 83.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 107 O
REMARK 620 2 ASP A 110 OD2 92.9
REMARK 620 3 GLU A 112 O 86.2 77.7
REMARK 620 4 GLU A 117 OE1 86.5 158.7 123.5
REMARK 620 5 GLU A 117 OE2 96.2 147.9 72.2 53.0
REMARK 620 6 HOH A 267 O 170.0 83.8 102.2 93.1 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 180 OD1
REMARK 620 2 ASP A 182 OD1 79.4
REMARK 620 3 SER A 184 OG 76.3 93.9
REMARK 620 4 THR A 186 O 74.7 149.3 64.3
REMARK 620 5 GLU A 191 OE1 109.3 125.4 140.8 79.4
REMARK 620 6 GLU A 191 OE2 100.2 73.0 166.9 127.4 52.4
REMARK 620 N 1 2 3 4 5
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 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NX0 RELATED DB: PDB
REMARK 900 RELATED ID: 1NX1 RELATED DB: PDB
REMARK 900 RELATED ID: 1NX3 RELATED DB: PDB
DBREF 1NX2 A 94 266 UNP P04574 CPNS1_PIG 94 266
SEQRES 1 A 173 GLU GLU VAL ARG GLN PHE ARG ARG LEU PHE ALA GLN LEU
SEQRES 2 A 173 ALA GLY ASP ASP MET GLU VAL SER ALA THR GLU LEU MET
SEQRES 3 A 173 ASN ILE LEU ASN LYS VAL VAL THR ARG HIS PRO ASP LEU
SEQRES 4 A 173 LYS THR ASP GLY PHE GLY ILE ASP THR CYS ARG SER MET
SEQRES 5 A 173 VAL ALA VAL MET ASP SER ASP THR THR GLY LYS LEU GLY
SEQRES 6 A 173 PHE GLU GLU PHE LYS TYR LEU TRP ASN ASN ILE LYS LYS
SEQRES 7 A 173 TRP GLN ALA ILE TYR LYS GLN PHE ASP VAL ASP ARG SER
SEQRES 8 A 173 GLY THR ILE GLY SER SER GLU LEU PRO GLY ALA PHE GLU
SEQRES 9 A 173 ALA ALA GLY PHE HIS LEU ASN GLU HIS LEU TYR SER MET
SEQRES 10 A 173 ILE ILE ARG ARG TYR SER ASP GLU GLY GLY ASN MET ASP
SEQRES 11 A 173 PHE ASP ASN PHE ILE SER CYS LEU VAL ARG LEU ASP ALA
SEQRES 12 A 173 MET PHE ARG ALA PHE LYS SER LEU ASP LYS ASP GLY THR
SEQRES 13 A 173 GLY GLN ILE GLN VAL ASN ILE GLN GLU TRP LEU GLN LEU
SEQRES 14 A 173 THR MET TYR SER
HET CA A 1 1
HET CA A 2 1
HET CA A 3 1
HET CA A 4 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 4(CA 2+)
FORMUL 6 HOH *86(H2 O)
HELIX 1 1 GLU A 94 GLY A 108 1 15
HELIX 2 2 ASP A 109 MET A 111 5 3
HELIX 3 3 SER A 114 THR A 127 1 14
HELIX 4 4 GLY A 138 ASP A 150 1 13
HELIX 5 5 GLY A 158 ASP A 180 1 23
HELIX 6 6 GLU A 191 ALA A 199 1 9
HELIX 7 7 ASN A 204 SER A 216 1 13
HELIX 8 8 ASP A 223 ASP A 245 1 23
HELIX 9 9 ASN A 255 TYR A 265 1 11
SHEET 1 A 2 ILE A 187 GLY A 188 0
SHEET 2 A 2 ASN A 221 MET A 222 -1 O MET A 222 N ILE A 187
LINK CA CA A 1 OD1 ASP A 135 1555 1555 2.28
LINK CA CA A 1 OD1 ASP A 223 1555 1555 2.70
LINK CA CA A 1 OD2 ASP A 223 1555 1555 2.20
LINK CA CA A 1 OD1 ASP A 225 1555 1555 2.42
LINK CA CA A 1 OD2 ASP A 225 1555 1555 2.48
LINK CA CA A 1 ND2 ASN A 226 1555 1555 2.46
LINK CA CA A 2 OD1 ASP A 150 1555 1555 2.25
LINK CA CA A 2 OD1 ASP A 152 1555 1555 2.20
LINK CA CA A 2 OG1 THR A 154 1555 1555 2.41
LINK CA CA A 2 O LYS A 156 1555 1555 2.33
LINK CA CA A 2 OE2 GLU A 161 1555 1555 2.70
LINK CA CA A 2 OE1 GLU A 161 1555 1555 2.36
LINK CA CA A 2 O HOH A 273 1555 1555 2.44
LINK CA CA A 3 O ALA A 107 1555 1555 2.24
LINK CA CA A 3 OD2 ASP A 110 1555 1555 2.45
LINK CA CA A 3 O GLU A 112 1555 1555 2.46
LINK CA CA A 3 OE1 GLU A 117 1555 1555 2.41
LINK CA CA A 3 OE2 GLU A 117 1555 1555 2.52
LINK CA CA A 3 O HOH A 267 1555 1555 2.42
LINK CA CA A 4 OD1 ASP A 180 1555 1555 2.33
LINK CA CA A 4 OD1 ASP A 182 1555 1555 2.26
LINK CA CA A 4 OG SER A 184 1555 1555 2.52
LINK CA CA A 4 O THR A 186 1555 1555 2.50
LINK CA CA A 4 OE1 GLU A 191 1555 1555 2.40
LINK CA CA A 4 OE2 GLU A 191 1555 1555 2.55
SITE 1 AC1 4 ASP A 135 ASP A 223 ASP A 225 ASN A 226
SITE 1 AC2 6 ASP A 150 ASP A 152 THR A 154 LYS A 156
SITE 2 AC2 6 GLU A 161 HOH A 273
SITE 1 AC3 5 ALA A 107 ASP A 110 GLU A 112 GLU A 117
SITE 2 AC3 5 HOH A 267
SITE 1 AC4 5 ASP A 180 ASP A 182 SER A 184 THR A 186
SITE 2 AC4 5 GLU A 191
CRYST1 78.673 78.673 77.776 90.00 90.00 120.00 P 31 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 0.012711 0.007339 0.000000 0.00000
SCALE2 0.000000 0.014677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012857 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
