HEADER HYDROLASE 12-MAY-04 1WDA
TITLE CRYSTAL STRUCTURE OF HUMAN PEPTIDYLARGININE DEIMINASE TYPE4 (PAD4) IN
TITLE 2 COMPLEX WITH BENZOYL-L-ARGININE AMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-ARGININE DEIMINASE TYPE IV;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PEPTIDYLARGININE DEIMINASE IV, HL-60 PAD;
COMPND 5 EC: 3.5.3.15;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1
KEYWDS POST-TRANSLATIONAL ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.ARITA,H.HASHIMOTO,T.SHIMIZU,K.NAKASHIMA,M.YAMADA,M.SATO
REVDAT 6 10-NOV-21 1WDA 1 REMARK SEQADV LINK
REVDAT 5 13-JUL-11 1WDA 1 VERSN
REVDAT 4 12-MAY-09 1WDA 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1WDA 1 VERSN
REVDAT 2 10-AUG-04 1WDA 1 JRNL
REVDAT 1 13-JUL-04 1WDA 0
JRNL AUTH K.ARITA,H.HASHIMOTO,T.SHIMIZU,K.NAKASHIMA,M.YAMADA,M.SATO
JRNL TITL STRUCTURAL BASIS FOR CA(2+)-INDUCED ACTIVATION OF HUMAN PAD4
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 777 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15247907
JRNL DOI 10.1038/NSMB799
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 32646
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3661
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2303
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 251
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4946
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.64000
REMARK 3 B22 (A**2) : 7.10000
REMARK 3 B33 (A**2) : -5.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -5.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.328
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.240
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.175
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.245
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
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): 5071 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4555 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6890 ; 1.593 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10653 ; 1.013 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 623 ; 7.110 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 771 ; 0.152 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5582 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 976 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1007 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5370 ; 0.236 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 3157 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 164 ; 0.189 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 16 ; 0.118 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 5 ; 0.096 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 44 ; 0.209 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.335 ; 0.200
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): 3140 ; 0.708 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5102 ; 1.292 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1931 ; 1.681 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1788 ; 2.777 ; 4.500
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 : 1
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 4 A 1066
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3116 33.5791 0.6208
REMARK 3 T TENSOR
REMARK 3 T11: 0.1126 T22: 0.0208
REMARK 3 T33: 0.1671 T12: 0.0045
REMARK 3 T13: 0.0417 T23: 0.0550
REMARK 3 L TENSOR
REMARK 3 L11: 1.0511 L22: 0.1171
REMARK 3 L33: 3.2482 L12: 0.0652
REMARK 3 L13: 1.3197 L23: 0.3315
REMARK 3 S TENSOR
REMARK 3 S11: -0.0170 S12: 0.1882 S13: 0.1140
REMARK 3 S21: 0.0020 S22: -0.0655 S23: -0.0571
REMARK 3 S31: 0.0947 S32: 0.4565 S33: 0.0825
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 1WDA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000023454.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9000
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36718
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 42.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
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) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEGMME2000, PH 8.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 73.06650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.02250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 73.06650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.02250
REMARK 290 SMTRY3 4 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: DIMERIC
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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 -6
REMARK 465 PRO A -5
REMARK 465 LEU A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 PRO A -1
REMARK 465 GLN A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLN A 3
REMARK 465 ASP A 36
REMARK 465 CYS A 37
REMARK 465 ALA A 53
REMARK 465 HIS A 54
REMARK 465 SER A 55
REMARK 465 PRO A 56
REMARK 465 PRO A 57
REMARK 465 ALA A 58
REMARK 465 LYS A 59
REMARK 465 LYS A 60
REMARK 465 LYS A 61
REMARK 465 SER A 62
REMARK 465 THR A 63
REMARK 465 GLY A 64
REMARK 465 SER A 65
REMARK 465 SER A 66
REMARK 465 VAL A 127
REMARK 465 LYS A 128
REMARK 465 PRO A 129
REMARK 465 THR A 130
REMARK 465 ARG A 131
REMARK 465 ALA A 132
REMARK 465 VAL A 133
REMARK 465 LYS A 134
REMARK 465 ASP A 135
REMARK 465 ARG A 218
REMARK 465 GLY A 219
REMARK 465 LYS A 220
REMARK 465 LEU A 221
REMARK 465 SER A 222
REMARK 465 SER A 223
REMARK 465 LYS A 224
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 137 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 377 CG CD CE NZ
REMARK 480 LYS A 519 CG CD CE NZ
REMARK 480 LYS A 520 CG CD CE NZ
REMARK 480 LYS A 521 CG CD CE NZ
REMARK 480 LYS A 527 CG CD CE NZ
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 981 O HOH A 1002 1.92
REMARK 500 O HOH A 1052 O HOH A 1054 1.93
REMARK 500 O PRO A 601 O HOH A 964 2.08
REMARK 500 NH2 ARG A 137 O GLN A 286 2.17
REMARK 500 O ARG A 484 O HOH A 952 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 519 CB LYS A 519 CG -0.486
REMARK 500 LYS A 520 CB LYS A 520 CG -0.226
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 51 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 137 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ASP A 248 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 344 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 388 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 VAL A 412 CB - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 ARG A 427 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 432 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 439 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 GLN A 455 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASP A 473 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 483 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 632 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
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 ARG A 137 33.91 -78.67
REMARK 500 LEU A 159 -73.67 -31.32
REMARK 500 PHE A 261 97.37 -162.35
REMARK 500 GLN A 306 -31.86 -131.80
REMARK 500 ILE A 313 94.10 -65.37
REMARK 500 PHE A 314 -160.78 -163.66
REMARK 500 GLU A 315 -34.52 -35.18
REMARK 500 GLU A 317 -36.32 -149.63
REMARK 500 ARG A 374 -146.39 -92.87
REMARK 500 GLN A 455 51.80 35.10
REMARK 500 VAL A 456 -10.01 -147.10
REMARK 500 ALA A 458 87.06 -18.75
REMARK 500 ARG A 484 66.84 19.39
REMARK 500 LYS A 485 -24.84 107.39
REMARK 500 LYS A 522 106.47 -57.69
REMARK 500 LYS A 574 -121.86 -136.70
REMARK 500 LEU A 592 74.63 -118.38
REMARK 500 GLU A 642 -149.55 -140.51
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 901 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 153 OD1
REMARK 620 2 ASP A 155 OD1 79.9
REMARK 620 3 ASP A 157 OD2 166.6 90.8
REMARK 620 4 ASP A 165 OD2 98.3 81.8 89.7
REMARK 620 5 ASP A 176 OD1 88.8 159.3 102.8 82.7
REMARK 620 6 ASP A 179 OD2 105.4 86.7 64.1 151.3 113.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 902 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 155 OD2
REMARK 620 2 ASP A 157 OD2 82.2
REMARK 620 3 ASP A 157 OD1 77.6 45.5
REMARK 620 4 ASP A 179 OD2 82.8 77.1 120.9
REMARK 620 5 ASP A 179 OD1 106.6 122.2 167.0 49.1
REMARK 620 6 ASP A 388 OD1 106.3 140.4 97.5 141.5 93.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 904 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 165 O
REMARK 620 2 ASP A 168 OD1 86.2
REMARK 620 3 GLU A 170 O 169.1 83.1
REMARK 620 4 HOH A1059 O 85.7 79.2 94.4
REMARK 620 5 HOH A1066 O 81.4 152.7 109.2 75.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 900 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 349 OE1
REMARK 620 2 GLU A 353 OE1 138.4
REMARK 620 3 PHE A 407 O 90.4 100.6
REMARK 620 4 LEU A 410 O 147.5 74.1 82.9
REMARK 620 5 GLU A 411 OE1 79.0 135.3 102.6 71.6
REMARK 620 6 HOH A 919 O 68.4 73.6 81.7 140.8 147.2
REMARK 620 7 HOH A 942 O 95.2 73.6 173.9 93.7 80.9 98.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 903 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 351 OE1
REMARK 620 2 ASP A 369 OD1 89.7
REMARK 620 3 ASP A 369 OD2 118.0 40.4
REMARK 620 4 SER A 370 O 90.9 89.7 115.4
REMARK 620 5 ASN A 373 OD1 105.4 162.4 122.3 99.0
REMARK 620 6 HOH A1065 O 173.8 85.5 59.9 85.1 80.0
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 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BAG A 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WD8 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, CALCIUM FREE FORM
REMARK 900 RELATED ID: 1WD9 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, CALCIUM BOUND FORM
DBREF 1WDA A 1 663 UNP Q9UM07 PADI4_HUMAN 1 663
SEQADV 1WDA GLY A -6 UNP Q9UM07 EXPRESSION TAG
SEQADV 1WDA PRO A -5 UNP Q9UM07 EXPRESSION TAG
SEQADV 1WDA LEU A -4 UNP Q9UM07 EXPRESSION TAG
SEQADV 1WDA GLY A -3 UNP Q9UM07 EXPRESSION TAG
SEQADV 1WDA SER A -2 UNP Q9UM07 EXPRESSION TAG
SEQADV 1WDA PRO A -1 UNP Q9UM07 EXPRESSION TAG
SEQADV 1WDA GLN A 0 UNP Q9UM07 EXPRESSION TAG
SEQADV 1WDA ALA A 645 UNP Q9UM07 CYS 645 ENGINEERED MUTATION
SEQRES 1 A 670 GLY PRO LEU GLY SER PRO GLN MET ALA GLN GLY THR LEU
SEQRES 2 A 670 ILE ARG VAL THR PRO GLU GLN PRO THR HIS ALA VAL CYS
SEQRES 3 A 670 VAL LEU GLY THR LEU THR GLN LEU ASP ILE CYS SER SER
SEQRES 4 A 670 ALA PRO GLU ASP CYS THR SER PHE SER ILE ASN ALA SER
SEQRES 5 A 670 PRO GLY VAL VAL VAL ASP ILE ALA HIS SER PRO PRO ALA
SEQRES 6 A 670 LYS LYS LYS SER THR GLY SER SER THR TRP PRO LEU ASP
SEQRES 7 A 670 PRO GLY VAL GLU VAL THR LEU THR MET LYS ALA ALA SER
SEQRES 8 A 670 GLY SER THR GLY ASP GLN LYS VAL GLN ILE SER TYR TYR
SEQRES 9 A 670 GLY PRO LYS THR PRO PRO VAL LYS ALA LEU LEU TYR LEU
SEQRES 10 A 670 THR ALA VAL GLU ILE SER LEU CYS ALA ASP ILE THR ARG
SEQRES 11 A 670 THR GLY LYS VAL LYS PRO THR ARG ALA VAL LYS ASP GLN
SEQRES 12 A 670 ARG THR TRP THR TRP GLY PRO CYS GLY GLN GLY ALA ILE
SEQRES 13 A 670 LEU LEU VAL ASN CYS ASP ARG ASP ASN LEU GLU SER SER
SEQRES 14 A 670 ALA MET ASP CYS GLU ASP ASP GLU VAL LEU ASP SER GLU
SEQRES 15 A 670 ASP LEU GLN ASP MET SER LEU MET THR LEU SER THR LYS
SEQRES 16 A 670 THR PRO LYS ASP PHE PHE THR ASN HIS THR LEU VAL LEU
SEQRES 17 A 670 HIS VAL ALA ARG SER GLU MET ASP LYS VAL ARG VAL PHE
SEQRES 18 A 670 GLN ALA THR ARG GLY LYS LEU SER SER LYS CYS SER VAL
SEQRES 19 A 670 VAL LEU GLY PRO LYS TRP PRO SER HIS TYR LEU MET VAL
SEQRES 20 A 670 PRO GLY GLY LYS HIS ASN MET ASP PHE TYR VAL GLU ALA
SEQRES 21 A 670 LEU ALA PHE PRO ASP THR ASP PHE PRO GLY LEU ILE THR
SEQRES 22 A 670 LEU THR ILE SER LEU LEU ASP THR SER ASN LEU GLU LEU
SEQRES 23 A 670 PRO GLU ALA VAL VAL PHE GLN ASP SER VAL VAL PHE ARG
SEQRES 24 A 670 VAL ALA PRO TRP ILE MET THR PRO ASN THR GLN PRO PRO
SEQRES 25 A 670 GLN GLU VAL TYR ALA CYS SER ILE PHE GLU ASN GLU ASP
SEQRES 26 A 670 PHE LEU LYS SER VAL THR THR LEU ALA MET LYS ALA LYS
SEQRES 27 A 670 CYS LYS LEU THR ILE CYS PRO GLU GLU GLU ASN MET ASP
SEQRES 28 A 670 ASP GLN TRP MET GLN ASP GLU MET GLU ILE GLY TYR ILE
SEQRES 29 A 670 GLN ALA PRO HIS LYS THR LEU PRO VAL VAL PHE ASP SER
SEQRES 30 A 670 PRO ARG ASN ARG GLY LEU LYS GLU PHE PRO ILE LYS ARG
SEQRES 31 A 670 VAL MET GLY PRO ASP PHE GLY TYR VAL THR ARG GLY PRO
SEQRES 32 A 670 GLN THR GLY GLY ILE SER GLY LEU ASP SER PHE GLY ASN
SEQRES 33 A 670 LEU GLU VAL SER PRO PRO VAL THR VAL ARG GLY LYS GLU
SEQRES 34 A 670 TYR PRO LEU GLY ARG ILE LEU PHE GLY ASP SER CYS TYR
SEQRES 35 A 670 PRO SER ASN ASP SER ARG GLN MET HIS GLN ALA LEU GLN
SEQRES 36 A 670 ASP PHE LEU SER ALA GLN GLN VAL GLN ALA PRO VAL LYS
SEQRES 37 A 670 LEU TYR SER ASP TRP LEU SER VAL GLY HIS VAL ASP GLU
SEQRES 38 A 670 PHE LEU SER PHE VAL PRO ALA PRO ASP ARG LYS GLY PHE
SEQRES 39 A 670 ARG LEU LEU LEU ALA SER PRO ARG SER CYS TYR LYS LEU
SEQRES 40 A 670 PHE GLN GLU GLN GLN ASN GLU GLY HIS GLY GLU ALA LEU
SEQRES 41 A 670 LEU PHE GLU GLY ILE LYS LYS LYS LYS GLN GLN LYS ILE
SEQRES 42 A 670 LYS ASN ILE LEU SER ASN LYS THR LEU ARG GLU HIS ASN
SEQRES 43 A 670 SER PHE VAL GLU ARG CYS ILE ASP TRP ASN ARG GLU LEU
SEQRES 44 A 670 LEU LYS ARG GLU LEU GLY LEU ALA GLU SER ASP ILE ILE
SEQRES 45 A 670 ASP ILE PRO GLN LEU PHE LYS LEU LYS GLU PHE SER LYS
SEQRES 46 A 670 ALA GLU ALA PHE PHE PRO ASN MET VAL ASN MET LEU VAL
SEQRES 47 A 670 LEU GLY LYS HIS LEU GLY ILE PRO LYS PRO PHE GLY PRO
SEQRES 48 A 670 VAL ILE ASN GLY ARG CYS CYS LEU GLU GLU LYS VAL CYS
SEQRES 49 A 670 SER LEU LEU GLU PRO LEU GLY LEU GLN CYS THR PHE ILE
SEQRES 50 A 670 ASN ASP PHE PHE THR TYR HIS ILE ARG HIS GLY GLU VAL
SEQRES 51 A 670 HIS ALA GLY THR ASN VAL ARG ARG LYS PRO PHE SER PHE
SEQRES 52 A 670 LYS TRP TRP ASN MET VAL PRO
HET CA A 900 1
HET CA A 901 1
HET CA A 902 1
HET CA A 903 1
HET CA A 904 1
HET SO4 A 905 5
HET SO4 A 906 5
HET SO4 A 907 5
HET BAG A 801 20
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM BAG N-[(E)-2-AMINO-1-(3-{[AMINO(IMINO)METHYL]AMINO}PROPYL)-
HETNAM 2 BAG 2-HYDROXYVINYL]BENZAMIDE
HETSYN BAG BENZOYL-L-ARGININE AMIDE
FORMUL 2 CA 5(CA 2+)
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 10 BAG C13 H19 N5 O2
FORMUL 11 HOH *159(H2 O)
HELIX 1 1 MET A 164 ASP A 168 5 5
HELIX 2 2 ASP A 173 MET A 180 5 8
HELIX 3 3 ASP A 192 THR A 195 5 4
HELIX 4 4 GLU A 207 ASP A 209 5 3
HELIX 5 5 GLU A 317 LYS A 331 1 15
HELIX 6 6 PRO A 338 MET A 343 1 6
HELIX 7 7 ARG A 374 LYS A 377 5 4
HELIX 8 8 GLU A 378 ARG A 383 1 6
HELIX 9 9 SER A 402 GLY A 408 5 7
HELIX 10 10 HIS A 444 GLN A 454 1 11
HELIX 11 11 HIS A 471 GLU A 474 5 4
HELIX 12 12 PRO A 494 GLU A 507 1 14
HELIX 13 13 ILE A 526 ASN A 532 1 7
HELIX 14 14 ASN A 532 GLY A 558 1 27
HELIX 15 15 ALA A 560 SER A 562 5 3
HELIX 16 16 GLU A 575 SER A 577 5 3
HELIX 17 17 CYS A 611 GLU A 614 1 4
HELIX 18 18 PRO A 622 GLY A 624 5 3
HELIX 19 19 TYR A 636 HIS A 640 5 5
HELIX 20 20 LYS A 657 MET A 661 5 5
SHEET 1 A 4 THR A 5 ARG A 8 0
SHEET 2 A 4 THR A 25 ASP A 28 1 O ASP A 28 N ILE A 7
SHEET 3 A 4 VAL A 76 MET A 80 -1 O VAL A 76 N LEU A 27
SHEET 4 A 4 VAL A 48 ASP A 51 -1 N VAL A 49 O THR A 79
SHEET 1 B 5 THR A 15 VAL A 20 0
SHEET 2 B 5 VAL A 104 CYS A 118 1 O THR A 111 N CYS A 19
SHEET 3 B 5 GLN A 90 TYR A 97 -1 N TYR A 96 O VAL A 104
SHEET 4 B 5 SER A 32 ALA A 44 -1 N SER A 41 O SER A 95
SHEET 5 B 5 TRP A 68 PRO A 69 -1 O TRP A 68 N PHE A 40
SHEET 1 C 6 THR A 15 VAL A 20 0
SHEET 2 C 6 VAL A 104 CYS A 118 1 O THR A 111 N CYS A 19
SHEET 3 C 6 SER A 174 THR A 189 -1 O THR A 184 N CYS A 118
SHEET 4 C 6 GLY A 243 ALA A 253 -1 O PHE A 249 N MET A 183
SHEET 5 C 6 VAL A 211 GLN A 215 -1 N PHE A 214 O TYR A 250
SHEET 6 C 6 SER A 226 LEU A 229 -1 O SER A 226 N GLN A 215
SHEET 1 D 5 ALA A 148 LEU A 150 0
SHEET 2 D 5 ALA A 282 VAL A 293 1 O ARG A 292 N LEU A 150
SHEET 3 D 5 LEU A 264 ASP A 273 -1 N ILE A 265 O PHE A 291
SHEET 4 D 5 HIS A 197 VAL A 203 -1 N THR A 198 O LEU A 272
SHEET 5 D 5 SER A 235 TYR A 237 -1 O HIS A 236 N LEU A 201
SHEET 1 E 4 ILE A 297 MET A 298 0
SHEET 2 E 4 MET A 352 ALA A 359 -1 O TYR A 356 N ILE A 297
SHEET 3 E 4 LYS A 362 ASP A 369 -1 O PHE A 368 N GLU A 353
SHEET 4 E 4 GLY A 390 THR A 393 1 O GLY A 390 N PRO A 365
SHEET 1 F 3 LYS A 333 ILE A 336 0
SHEET 2 F 3 PRO A 305 ALA A 310 1 N VAL A 308 O THR A 335
SHEET 3 F 3 THR A 647 ARG A 651 -1 O ASN A 648 N TYR A 309
SHEET 1 G 3 LEU A 410 VAL A 412 0
SHEET 2 G 3 ILE A 428 ASP A 432 -1 O LEU A 429 N GLU A 411
SHEET 3 G 3 VAL A 460 TYR A 463 1 O LEU A 462 N ASP A 432
SHEET 1 H 2 VAL A 416 VAL A 418 0
SHEET 2 H 2 LYS A 421 TYR A 423 -1 O LYS A 421 N VAL A 418
SHEET 1 I 3 LEU A 476 PRO A 480 0
SHEET 2 I 3 PHE A 487 SER A 493 -1 O LEU A 490 N SER A 477
SHEET 3 I 3 ILE A 564 PRO A 568 1 O ILE A 565 N LEU A 489
SHEET 1 J 2 LEU A 513 LEU A 514 0
SHEET 2 J 2 GLN A 524 LYS A 525 -1 O GLN A 524 N LEU A 514
SHEET 1 K 2 PHE A 571 LEU A 573 0
SHEET 2 K 2 ALA A 579 ALA A 581 -1 O GLU A 580 N LYS A 572
SHEET 1 L 3 LEU A 590 LEU A 592 0
SHEET 2 L 3 HIS A 595 PRO A 599 -1 O GLY A 597 N LEU A 590
SHEET 3 L 3 GLN A 626 ILE A 630 1 O ILE A 630 N ILE A 598
SHEET 1 M 2 VAL A 605 ILE A 606 0
SHEET 2 M 2 ARG A 609 CYS A 610 -1 O ARG A 609 N ILE A 606
LINK OD1 ASN A 153 CA CA A 901 1555 1555 2.40
LINK OD1 ASP A 155 CA CA A 901 1555 1555 2.36
LINK OD2 ASP A 155 CA CA A 902 1555 1555 2.44
LINK OD2 ASP A 157 CA CA A 901 1555 1555 2.93
LINK OD2 ASP A 157 CA CA A 902 1555 1555 2.29
LINK OD1 ASP A 157 CA CA A 902 1555 1555 2.97
LINK OD2 ASP A 165 CA CA A 901 1555 1555 2.25
LINK O ASP A 165 CA CA A 904 1555 1555 2.32
LINK OD1 ASP A 168 CA CA A 904 1555 1555 2.45
LINK O GLU A 170 CA CA A 904 1555 1555 2.26
LINK OD1 ASP A 176 CA CA A 901 1555 1555 2.42
LINK OD2 ASP A 179 CA CA A 901 1555 1555 2.42
LINK OD2 ASP A 179 CA CA A 902 1555 1555 2.31
LINK OD1 ASP A 179 CA CA A 902 1555 1555 2.78
LINK OE1 GLN A 349 CA CA A 900 1555 1555 2.27
LINK OE1 GLU A 351 CA CA A 903 1555 1555 2.52
LINK OE1 GLU A 353 CA CA A 900 1555 1555 2.55
LINK OD1 ASP A 369 CA CA A 903 1555 1555 2.30
LINK OD2 ASP A 369 CA CA A 903 1555 1555 3.34
LINK O SER A 370 CA CA A 903 1555 1555 2.30
LINK OD1 ASN A 373 CA CA A 903 1555 1555 2.50
LINK OD1 ASP A 388 CA CA A 902 1555 1555 2.75
LINK O PHE A 407 CA CA A 900 1555 1555 2.24
LINK O LEU A 410 CA CA A 900 1555 1555 2.44
LINK OE1 GLU A 411 CA CA A 900 1555 1555 2.58
LINK CA CA A 900 O HOH A 919 1555 1555 2.40
LINK CA CA A 900 O HOH A 942 1555 1555 2.38
LINK CA CA A 903 O HOH A1065 1555 1555 2.57
LINK CA CA A 904 O HOH A1059 1555 1555 2.24
LINK CA CA A 904 O HOH A1066 1555 1555 2.31
SITE 1 AC1 7 GLN A 349 GLU A 353 PHE A 407 LEU A 410
SITE 2 AC1 7 GLU A 411 HOH A 919 HOH A 942
SITE 1 AC2 6 ASN A 153 ASP A 155 ASP A 157 ASP A 165
SITE 2 AC2 6 ASP A 176 ASP A 179
SITE 1 AC3 4 ASP A 155 ASP A 157 ASP A 179 ASP A 388
SITE 1 AC4 5 GLU A 351 ASP A 369 SER A 370 ASN A 373
SITE 2 AC4 5 HOH A1065
SITE 1 AC5 5 ASP A 165 ASP A 168 GLU A 170 HOH A1059
SITE 2 AC5 5 HOH A1066
SITE 1 AC6 3 SER A 402 GLY A 403 ARG A 441
SITE 1 AC7 4 ARG A 495 SER A 496 LYS A 499 LYS A 615
SITE 1 AC8 2 LYS A 525 ASN A 528
SITE 1 AC9 12 TRP A 347 GLN A 349 ASP A 350 ARG A 374
SITE 2 AC9 12 GLY A 408 HIS A 471 ASP A 473 ASN A 588
SITE 3 AC9 12 ARG A 639 HIS A 640 ALA A 645 HOH A 941
CRYST1 146.133 60.045 115.406 90.00 124.23 90.00 C 1 2 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 0.006843 0.000000 0.004656 0.00000
SCALE2 0.000000 0.016654 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010480 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
