HEADER HYDROLASE 05-FEB-10 3LPA
TITLE CRYSTAL STRUCTURE OF A SUBTILISIN-LIKE PROTEASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACIDIC EXTRACELLULAR SUBTILISIN-LIKE PROTEASE APRV2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 131-470;
COMPND 5 EC: 3.4.21.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DICHELOBACTER NODOSUS;
SOURCE 3 ORGANISM_TAXID: 246195;
SOURCE 4 STRAIN: VCS1703A;
SOURCE 5 GENE: APRV2, DNO_1167;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI(DE3)LYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PROTEASE, SUBTILASE, VIRULENCE FACTOR, HYDROLASE, SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.J.PORTER,W.WONG,J.C.WHISSTOCK,J.I.ROOD,R.M.KENNAN
REVDAT 3 01-NOV-23 3LPA 1 REMARK LINK
REVDAT 2 15-DEC-10 3LPA 1 JRNL
REVDAT 1 08-DEC-10 3LPA 0
JRNL AUTH R.M.KENNAN,W.WONG,O.P.DHUNGYEL,X.HAN,D.WONG,D.PARKER,
JRNL AUTH 2 C.J.ROSADO,R.H.P.LAW,S.MCGOWAN,S.B.REEVE,V.LEVINA,
JRNL AUTH 3 G.A.POWERS,R.N.PIKE,S.P.BOTTOMLEY,A.I.SMITH,I.MARSH,
JRNL AUTH 4 R.J.WHITTINGTON,J.C.WHISSTOCK,C.J.PORTER,J.I.ROOD
JRNL TITL THE SUBTILISIN-LIKE PROTEASE APRV2 IS REQUIRED FOR VIRULENCE
JRNL TITL 2 AND USES A NOVEL DISULPHIDE-TETHERED EXOSITE TO BIND
JRNL TITL 3 SUBSTRATES
JRNL REF PLOS PATHOG. V. 6 01210 2010
JRNL REFN ISSN 1553-7366
JRNL PMID 21124876
JRNL DOI 10.1371/JOURNAL.PPAT.1001210
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 17664
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 915
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1166
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2495
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 154
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : -0.01000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : -0.03000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.241
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.193
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.231
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2550 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3483 ; 1.343 ; 1.925
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 339 ; 6.163 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;37.145 ;24.602
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 356 ;13.743 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;19.354 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 387 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2002 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1676 ; 0.947 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2671 ; 1.488 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 874 ; 1.091 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 812 ; 1.622 ; 3.000
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9701 -10.7657 -16.7273
REMARK 3 T TENSOR
REMARK 3 T11: 0.1096 T22: 0.0634
REMARK 3 T33: 0.0605 T12: 0.0212
REMARK 3 T13: 0.0034 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 1.4949 L22: 0.4840
REMARK 3 L33: 0.0465 L12: 0.6117
REMARK 3 L13: 0.0920 L23: 0.1323
REMARK 3 S TENSOR
REMARK 3 S11: -0.0311 S12: -0.0100 S13: 0.0350
REMARK 3 S21: -0.0577 S22: 0.0133 S23: -0.0237
REMARK 3 S31: 0.0103 S32: 0.0103 S33: 0.0178
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 209 A 341
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5628 -7.8338 -4.1872
REMARK 3 T TENSOR
REMARK 3 T11: 0.0687 T22: 0.1823
REMARK 3 T33: 0.0368 T12: -0.0126
REMARK 3 T13: 0.0075 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 1.8370 L22: 0.6158
REMARK 3 L33: 0.4849 L12: 0.5158
REMARK 3 L13: 0.0276 L23: -0.0819
REMARK 3 S TENSOR
REMARK 3 S11: 0.1517 S12: -0.5081 S13: 0.0947
REMARK 3 S21: -0.0087 S22: -0.1666 S23: 0.0459
REMARK 3 S31: -0.0113 S32: -0.1057 S33: 0.0148
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3LPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057560.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17666
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.659
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.26500
REMARK 200 R SYM FOR SHELL (I) : 0.26500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3LPC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, SODIUM CACODYLATE, PEG
REMARK 280 8000, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 ARG A 17 CD NE CZ NH1 NH2
REMARK 470 ARG A 48 NE CZ NH1 NH2
REMARK 470 ARG A 99 NE CZ NH1 NH2
REMARK 470 ARG A 120 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 145 OD1 OD2
REMARK 470 ASP A 308 CG OD1 OD2
REMARK 470 ARG A 320 CG CD NE CZ NH1 NH2
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 PHE A 15 -22.09 -141.72
REMARK 500 ASN A 34 25.75 48.57
REMARK 500 ASP A 41 -151.45 -162.32
REMARK 500 ALA A 114 45.17 -153.85
REMARK 500 ARG A 120 -42.39 66.59
REMARK 500 ALA A 127 72.39 -113.31
REMARK 500 ARG A 263 -88.50 -111.23
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 361 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 5 OD1
REMARK 620 2 ASP A 49 OD1 156.5
REMARK 620 3 ASP A 49 OD2 150.0 51.8
REMARK 620 4 VAL A 116 O 98.0 83.8 95.2
REMARK 620 5 ASN A 119 OD1 78.7 78.4 130.1 81.3
REMARK 620 6 ILE A 121 O 86.6 88.2 85.3 169.3 90.2
REMARK 620 7 VAL A 123 O 79.6 123.7 76.0 81.0 149.7 109.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 360 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 59 OD2
REMARK 620 2 ASP A 69 OD2 85.2
REMARK 620 3 ASP A 74 OD2 113.0 106.7
REMARK 620 4 ASP A 74 OD1 81.3 66.4 49.8
REMARK 620 5 ASP A 76 O 90.4 175.4 76.6 114.6
REMARK 620 6 HOH A 373 O 95.4 91.8 146.8 158.1 87.0
REMARK 620 7 HOH A 398 O 164.5 81.1 78.0 99.6 103.0 78.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 362 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 69 OD2
REMARK 620 2 ASP A 69 OD1 52.3
REMARK 620 3 ASP A 71 OD1 93.7 81.3
REMARK 620 4 ASP A 71 O 122.4 70.1 77.5
REMARK 620 5 GLY A 72 O 158.5 149.2 92.4 79.1
REMARK 620 6 ASP A 74 OD1 70.8 122.2 94.2 164.3 88.2
REMARK 620 7 HOH A 347 O 96.5 103.0 169.4 94.8 78.9 91.5
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 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 362
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LPC RELATED DB: PDB
REMARK 900 RELATED ID: 3LPD RELATED DB: PDB
DBREF 3LPA A 2 341 UNP A5EXI3 A5EXI3_DICNV 131 470
SEQRES 1 A 340 ALA PRO ASN ASP GLN HIS TYR ARG GLU GLN TRP HIS TYR
SEQRES 2 A 340 PHE ASP ARG TYR GLY VAL LYS ALA ASP LYS VAL TRP ASP
SEQRES 3 A 340 MET GLY PHE THR GLY GLN ASN VAL VAL VAL ALA VAL VAL
SEQRES 4 A 340 ASP THR GLY ILE LEU HIS HIS ARG ASP LEU ASN ALA ASN
SEQRES 5 A 340 VAL LEU PRO GLY TYR ASP PHE ILE SER ASN SER GLN ILE
SEQRES 6 A 340 SER LEU ASP GLY ASP GLY ARG ASP ALA ASP PRO PHE ASP
SEQRES 7 A 340 GLU GLY ASP TRP PHE ASP ASN TRP ALA CYS GLY GLY TYR
SEQRES 8 A 340 PRO ASP PRO ARG LYS GLU ARG SER ASP SER SER TRP HIS
SEQRES 9 A 340 GLY SER HIS VAL ALA GLY THR ILE ALA ALA VAL THR ASN
SEQRES 10 A 340 ASN ARG ILE GLY VAL ALA GLY VAL ALA TYR GLY ALA LYS
SEQRES 11 A 340 VAL VAL PRO VAL ARG ALA LEU GLY ARG CYS GLY GLY TYR
SEQRES 12 A 340 ASP SER ASP ILE SER ASP GLY LEU TYR TRP ALA ALA GLY
SEQRES 13 A 340 GLY ARG ILE ALA GLY ILE PRO GLU ASN ARG ASN PRO ALA
SEQRES 14 A 340 LYS VAL ILE ASN MET SER LEU GLY SER ASP GLY GLN CYS
SEQRES 15 A 340 SER TYR ASN ALA GLN THR MET ILE ASP ARG ALA THR ARG
SEQRES 16 A 340 LEU GLY ALA LEU VAL VAL VAL ALA ALA GLY ASN GLU ASN
SEQRES 17 A 340 GLN ASN ALA SER ASN THR TRP PRO THR SER CYS ASN ASN
SEQRES 18 A 340 VAL LEU SER VAL GLY ALA THR THR SER ARG GLY ILE ARG
SEQRES 19 A 340 ALA SER PHE SER ASN TYR GLY VAL ASP VAL ASP LEU ALA
SEQRES 20 A 340 ALA PRO GLY GLN ASP ILE LEU SER THR VAL ASP SER GLY
SEQRES 21 A 340 THR ARG ARG PRO VAL SER ASP ALA TYR SER PHE MET ALA
SEQRES 22 A 340 GLY THR SER MET ALA THR PRO HIS VAL SER GLY VAL ALA
SEQRES 23 A 340 ALA LEU VAL ILE SER ALA ALA ASN SER VAL ASN LYS ASN
SEQRES 24 A 340 LEU THR PRO ALA GLU LEU LYS ASP VAL LEU VAL SER THR
SEQRES 25 A 340 THR SER PRO PHE ASN GLY ARG LEU ASP ARG ALA LEU GLY
SEQRES 26 A 340 SER GLY ILE VAL ASP ALA GLU ALA ALA VAL ASN SER VAL
SEQRES 27 A 340 LEU GLY
HET CA A 360 1
HET CA A 361 1
HET CA A 362 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 3(CA 2+)
FORMUL 5 HOH *154(H2 O)
HELIX 1 1 HIS A 7 GLU A 10 5 4
HELIX 2 2 GLN A 11 ASP A 16 1 6
HELIX 3 3 LYS A 21 ASP A 27 1 7
HELIX 4 4 LEU A 50 VAL A 54 5 5
HELIX 5 5 ASN A 63 LEU A 68 1 6
HELIX 6 6 ASP A 94 GLU A 98 5 5
HELIX 7 7 TRP A 104 ALA A 115 1 12
HELIX 8 8 TYR A 144 GLY A 157 1 14
HELIX 9 9 SER A 184 LEU A 197 1 14
HELIX 10 10 ASN A 211 SER A 213 5 3
HELIX 11 11 GLY A 275 VAL A 297 1 23
HELIX 12 12 THR A 302 THR A 313 1 12
HELIX 13 13 ASP A 331 GLY A 341 1 11
SHEET 1 A 7 TYR A 58 ASP A 59 0
SHEET 2 A 7 LYS A 131 ARG A 136 1 O ARG A 136 N TYR A 58
SHEET 3 A 7 VAL A 36 ASP A 41 1 N VAL A 37 O LYS A 131
SHEET 4 A 7 VAL A 172 MET A 175 1 O ASN A 174 N ALA A 38
SHEET 5 A 7 LEU A 200 ALA A 204 1 O VAL A 202 N MET A 175
SHEET 6 A 7 LEU A 224 THR A 229 1 O LEU A 224 N VAL A 203
SHEET 7 A 7 LEU A 247 PRO A 250 1 O LEU A 247 N GLY A 227
SHEET 1 B 2 SER A 179 ASP A 180 0
SHEET 2 B 2 THR A 215 TRP A 216 -1 O TRP A 216 N SER A 179
SHEET 1 C 2 ILE A 254 ASP A 259 0
SHEET 2 C 2 ASP A 268 MET A 273 -1 O ALA A 269 N VAL A 258
SSBOND 1 CYS A 89 CYS A 141 1555 1555 2.03
SSBOND 2 CYS A 183 CYS A 220 1555 1555 2.02
LINK OD1 ASP A 5 CA CA A 361 1555 1555 2.18
LINK OD1 ASP A 49 CA CA A 361 1555 1555 2.45
LINK OD2 ASP A 49 CA CA A 361 1555 1555 2.63
LINK OD2 ASP A 59 CA CA A 360 1555 1555 2.32
LINK OD2 ASP A 69 CA CA A 360 1555 1555 2.40
LINK OD2 ASP A 69 CA CA A 362 1555 1555 2.44
LINK OD1 ASP A 69 CA CA A 362 1555 1555 2.52
LINK OD1 ASP A 71 CA CA A 362 1555 1555 2.37
LINK O ASP A 71 CA CA A 362 1555 1555 2.50
LINK O GLY A 72 CA CA A 362 1555 1555 2.20
LINK OD2 ASP A 74 CA CA A 360 1555 1555 2.51
LINK OD1 ASP A 74 CA CA A 360 1555 1555 2.68
LINK OD1 ASP A 74 CA CA A 362 1555 1555 2.37
LINK O ASP A 76 CA CA A 360 1555 1555 2.30
LINK O VAL A 116 CA CA A 361 1555 1555 2.32
LINK OD1 ASN A 119 CA CA A 361 1555 1555 2.41
LINK O ILE A 121 CA CA A 361 1555 1555 2.44
LINK O VAL A 123 CA CA A 361 1555 1555 2.48
LINK O HOH A 347 CA CA A 362 1555 1555 2.35
LINK CA CA A 360 O HOH A 373 1555 1555 2.16
LINK CA CA A 360 O HOH A 398 1555 1555 2.36
CISPEP 1 CYS A 89 GLY A 90 0 -29.09
CISPEP 2 TYR A 92 PRO A 93 0 8.21
CISPEP 3 TRP A 216 PRO A 217 0 6.57
SITE 1 AC1 6 ASP A 59 ASP A 69 ASP A 74 ASP A 76
SITE 2 AC1 6 HOH A 373 HOH A 398
SITE 1 AC2 6 ASP A 5 ASP A 49 VAL A 116 ASN A 119
SITE 2 AC2 6 ILE A 121 VAL A 123
SITE 1 AC3 5 ASP A 69 ASP A 71 GLY A 72 ASP A 74
SITE 2 AC3 5 HOH A 347
CRYST1 43.059 45.980 47.243 97.79 115.24 113.86 P 1 1
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 0.023224 0.010272 0.015918 0.00000
SCALE2 0.000000 0.023781 0.009541 0.00000
SCALE3 0.000000 0.000000 0.025215 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
