HEADER HYDROLASE 11-MAY-10 3MZ2
TITLE CRYSTAL STRUCTURE OF A GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE
TITLE 2 (BDI_3922) FROM PARABACTEROIDES DISTASONIS ATCC 8503 AT 1.55 A
TITLE 3 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARABACTEROIDES DISTASONIS;
SOURCE 3 ORGANISM_TAXID: 435591;
SOURCE 4 STRAIN: ATCC 8503 / DSM 20701 / NCTC 11152;
SOURCE 5 GENE: BDI_3922;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 4 01-FEB-23 3MZ2 1 REMARK SEQADV
REVDAT 3 17-JUL-19 3MZ2 1 REMARK LINK
REVDAT 2 08-NOV-17 3MZ2 1 REMARK
REVDAT 1 07-JUL-10 3MZ2 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A GLYCEROPHOSPHORYL DIESTER
JRNL TITL 2 PHOSPHODIESTERASE (BDI_3922) FROM PARABACTEROIDES DISTASONIS
JRNL TITL 3 ATCC 8503 AT 1.55 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 77315
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3882
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5409
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 291
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4532
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 141
REMARK 3 SOLVENT ATOMS : 529
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : -0.95000
REMARK 3 B33 (A**2) : 0.54000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.34000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.410
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5152 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3589 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7052 ; 1.592 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8847 ; 0.938 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 699 ; 6.129 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;33.904 ;24.378
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 934 ;13.113 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;14.262 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 769 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5736 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1017 ; 0.001 ; 0.020
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): 3051 ; 0.824 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1205 ; 0.283 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5054 ; 1.402 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2101 ; 2.535 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1931 ; 4.029 ; 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 : 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 32 A 316
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6200 44.0050 29.3100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0483 T22: 0.0296
REMARK 3 T33: 0.0057 T12: 0.0011
REMARK 3 T13: -0.0178 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.5359 L22: 1.0119
REMARK 3 L33: 0.5092 L12: -0.0829
REMARK 3 L13: 0.0275 L23: -0.1997
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: -0.0133 S13: 0.0006
REMARK 3 S21: -0.0689 S22: -0.0113 S23: -0.0547
REMARK 3 S31: 0.0074 S32: 0.0456 S33: 0.0146
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 : B 32 B 316
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5420 61.7710 53.7330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0366 T22: 0.0262
REMARK 3 T33: 0.0111 T12: 0.0024
REMARK 3 T13: -0.0266 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.3552 L22: 0.8603
REMARK 3 L33: 0.5643 L12: -0.0040
REMARK 3 L13: -0.0568 L23: -0.0288
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: 0.0244 S13: 0.0180
REMARK 3 S21: 0.0204 S22: 0.0066 S23: -0.0233
REMARK 3 S31: 0.0170 S32: 0.0012 S33: 0.0006
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL U FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL U FACTORS. 4. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 5. X-RAY FLUORESCENCE EXCITATION AND WAVELENGTH
REMARK 3 SCANS AND ANOMALOUS DIFFERENCE FOURIERS SUPPORT THE MODELING OF
REMARK 3 NA IONS. 6. SODIUM (NA), SULPHATE (SO4) IONS, A PEG-4000 (PE4)
REMARK 3 FRAGMENT AND PEG-200 (PG4) MOLECULES FROM THE CRYSTALLIZATION/
REMARK 3 CRYOPROTECTION SOLUTION ARE MODELED
REMARK 4
REMARK 4 3MZ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000059173.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91837,0.97925,0.97895
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77355
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 47.615
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : 0.61000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHENIX, SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27.0000% POLYETHYLENE GLYCOL 4000,
REMARK 280 0.3000M AMMONIUM SULFATE, 0.1M SODIUM ACETATE PH 4.0, NANODROP,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 45.24050
REMARK 290 SMTRY3 2 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 300 REMARK: CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A
REMARK 300 MONOMER AS THE SIGNIFICANT OLIGOMERIZATION STATE.
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
REMARK 350 TOTAL BURIED SURFACE AREA: 5090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 0
REMARK 465 GLU A 26
REMARK 465 GLU A 27
REMARK 465 LEU A 28
REMARK 465 GLU A 29
REMARK 465 TYR A 30
REMARK 465 LYS A 31
REMARK 465 GLY B 0
REMARK 465 GLU B 26
REMARK 465 GLU B 27
REMARK 465 LEU B 28
REMARK 465 GLU B 29
REMARK 465 TYR B 30
REMARK 465 LYS B 31
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 LYS A 67 CD CE NZ
REMARK 470 ARG A 142 NE CZ NH1 NH2
REMARK 470 LYS A 200 CE NZ
REMARK 470 LYS A 213 CG CD CE NZ
REMARK 470 LYS B 67 CG CD CE NZ
REMARK 470 GLU B 124 CD OE1 OE2
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 MSE A 254 CG - SE - CE ANGL. DEV. = -14.0 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 PHE A 103 124.61 -170.79
REMARK 500 LYS A 164 -101.26 -117.78
REMARK 500 LYS A 164 -99.38 -119.23
REMARK 500 SER A 262 -99.26 -118.67
REMARK 500 LYS B 164 -102.12 -113.32
REMARK 500 SER B 262 -99.64 -122.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 17
REMARK 610 PG4 A 19
REMARK 610 PG4 A 21
REMARK 610 PG4 A 23
REMARK 610 PG4 B 15
REMARK 610 PG4 B 16
REMARK 610 PG4 B 18
REMARK 610 PG4 B 20
REMARK 610 PG4 B 22
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 NA B 1 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PE4 B 14 O6
REMARK 620 2 PE4 B 14 O5 59.8
REMARK 620 3 PE4 B 14 O1 73.7 133.5
REMARK 620 4 PE4 B 14 O4 111.8 54.2 165.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 19
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 21
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 23
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 B 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 16
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 18
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 20
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 22
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 396626 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT (RESIDUES 26-316) WAS EXPRESSED WITH A PURIFICATION
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3MZ2 A 26 316 UNP A6LIT8 A6LIT8_PARD8 26 316
DBREF 3MZ2 B 26 316 UNP A6LIT8 A6LIT8_PARD8 26 316
SEQADV 3MZ2 GLY A 0 UNP A6LIT8 EXPRESSION TAG
SEQADV 3MZ2 GLY B 0 UNP A6LIT8 EXPRESSION TAG
SEQRES 1 A 292 GLY GLU GLU LEU GLU TYR LYS GLY MSE ASN THR LEU GLN
SEQRES 2 A 292 ILE SER ASN VAL ASP ASP LEU ILE SER PHE TYR GLN TYR
SEQRES 3 A 292 ALA ASP ASP ARG ILE PRO LEU ILE SER GLY HIS ARG GLY
SEQRES 4 A 292 GLY ARG GLY LYS GLY TYR PRO GLU ASN SER MSE GLU THR
SEQRES 5 A 292 PHE GLU ASN THR LEU SER TYR THR PRO ALA THR PHE GLU
SEQRES 6 A 292 ILE ASP PRO ARG LEU THR LYS ASP SER VAL ILE VAL LEU
SEQRES 7 A 292 PHE HIS ASP ASP THR LEU GLU ARG THR SER ASN GLY THR
SEQRES 8 A 292 GLY LYS VAL SER ASP TYR THR TRP GLU GLU LEU GLN ASN
SEQRES 9 A 292 PHE ARG LEU LYS ASP PRO GLU GLY ASN ILE THR ASN TYR
SEQRES 10 A 292 ARG ILE PRO THR LEU GLU GLU ALA ILE ARG TRP ALA ARG
SEQRES 11 A 292 GLY LYS THR ILE LEU ILE LEU ASP LYS LYS ASP VAL PRO
SEQRES 12 A 292 MSE GLU ARG THR ALA GLN LEU ILE THR ASP MSE GLN ALA
SEQRES 13 A 292 GLU PRO TYR VAL MSE ILE THR VAL HIS ASP GLY ALA SER
SEQRES 14 A 292 ALA ARG PHE PHE TYR GLU LYS ASN PRO ASN PHE MSE PHE
SEQRES 15 A 292 GLU ALA PHE VAL LYS THR LYS GLU ALA VAL GLN ASP TYR
SEQRES 16 A 292 GLU ASP ASN GLY ILE PRO TRP SER HIS ILE MSE ALA TYR
SEQRES 17 A 292 VAL GLY PRO LYS ILE THR PRO GLU VAL ARG GLU VAL ILE
SEQRES 18 A 292 ASP MSE LEU HIS GLU ARG GLY VAL MSE CYS MSE ILE SER
SEQRES 19 A 292 THR ALA PRO SER ASP ASP LYS LEU SER THR PRO GLU SER
SEQRES 20 A 292 ARG ALA GLU ALA TYR ARG MSE ILE ILE ARG GLN GLY VAL
SEQRES 21 A 292 ASP ILE ILE GLU SER ASP ARG PRO ILE GLU VAL ALA GLU
SEQRES 22 A 292 ALA ILE SER SER LEU ILE PRO VAL SER SER SER LYS GLY
SEQRES 23 A 292 LYS PHE PHE SER THR LEU
SEQRES 1 B 292 GLY GLU GLU LEU GLU TYR LYS GLY MSE ASN THR LEU GLN
SEQRES 2 B 292 ILE SER ASN VAL ASP ASP LEU ILE SER PHE TYR GLN TYR
SEQRES 3 B 292 ALA ASP ASP ARG ILE PRO LEU ILE SER GLY HIS ARG GLY
SEQRES 4 B 292 GLY ARG GLY LYS GLY TYR PRO GLU ASN SER MSE GLU THR
SEQRES 5 B 292 PHE GLU ASN THR LEU SER TYR THR PRO ALA THR PHE GLU
SEQRES 6 B 292 ILE ASP PRO ARG LEU THR LYS ASP SER VAL ILE VAL LEU
SEQRES 7 B 292 PHE HIS ASP ASP THR LEU GLU ARG THR SER ASN GLY THR
SEQRES 8 B 292 GLY LYS VAL SER ASP TYR THR TRP GLU GLU LEU GLN ASN
SEQRES 9 B 292 PHE ARG LEU LYS ASP PRO GLU GLY ASN ILE THR ASN TYR
SEQRES 10 B 292 ARG ILE PRO THR LEU GLU GLU ALA ILE ARG TRP ALA ARG
SEQRES 11 B 292 GLY LYS THR ILE LEU ILE LEU ASP LYS LYS ASP VAL PRO
SEQRES 12 B 292 MSE GLU ARG THR ALA GLN LEU ILE THR ASP MSE GLN ALA
SEQRES 13 B 292 GLU PRO TYR VAL MSE ILE THR VAL HIS ASP GLY ALA SER
SEQRES 14 B 292 ALA ARG PHE PHE TYR GLU LYS ASN PRO ASN PHE MSE PHE
SEQRES 15 B 292 GLU ALA PHE VAL LYS THR LYS GLU ALA VAL GLN ASP TYR
SEQRES 16 B 292 GLU ASP ASN GLY ILE PRO TRP SER HIS ILE MSE ALA TYR
SEQRES 17 B 292 VAL GLY PRO LYS ILE THR PRO GLU VAL ARG GLU VAL ILE
SEQRES 18 B 292 ASP MSE LEU HIS GLU ARG GLY VAL MSE CYS MSE ILE SER
SEQRES 19 B 292 THR ALA PRO SER ASP ASP LYS LEU SER THR PRO GLU SER
SEQRES 20 B 292 ARG ALA GLU ALA TYR ARG MSE ILE ILE ARG GLN GLY VAL
SEQRES 21 B 292 ASP ILE ILE GLU SER ASP ARG PRO ILE GLU VAL ALA GLU
SEQRES 22 B 292 ALA ILE SER SER LEU ILE PRO VAL SER SER SER LYS GLY
SEQRES 23 B 292 LYS PHE PHE SER THR LEU
MODRES 3MZ2 MSE A 33 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 74 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 168 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 178 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 185 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 205 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 230 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 247 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 254 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 256 MET SELENOMETHIONINE
MODRES 3MZ2 MSE A 278 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 33 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 74 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 168 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 178 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 185 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 205 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 230 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 247 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 254 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 256 MET SELENOMETHIONINE
MODRES 3MZ2 MSE B 278 MET SELENOMETHIONINE
HET MSE A 33 8
HET MSE A 74 8
HET MSE A 168 13
HET MSE A 178 13
HET MSE A 185 8
HET MSE A 205 8
HET MSE A 230 8
HET MSE A 247 13
HET MSE A 254 13
HET MSE A 256 13
HET MSE A 278 8
HET MSE B 33 8
HET MSE B 74 8
HET MSE B 168 8
HET MSE B 178 13
HET MSE B 185 8
HET MSE B 205 8
HET MSE B 230 8
HET MSE B 247 13
HET MSE B 254 8
HET MSE B 256 13
HET MSE B 278 13
HET SO4 A 2 5
HET SO4 A 5 5
HET SO4 A 7 5
HET SO4 A 8 5
HET SO4 A 9 5
HET PG4 A 17 7
HET PG4 A 19 8
HET PG4 A 21 7
HET PG4 A 23 6
HET NA B 1 1
HET SO4 B 3 5
HET SO4 B 4 5
HET SO4 B 6 5
HET SO4 B 10 5
HET SO4 B 11 5
HET SO4 B 12 5
HET SO4 B 13 5
HET PE4 B 14 16
HET PG4 B 15 7
HET PG4 B 16 7
HET PG4 B 18 8
HET PG4 B 20 7
HET PG4 B 22 7
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM NA SODIUM ION
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 1 MSE 22(C5 H11 N O2 SE)
FORMUL 3 SO4 12(O4 S 2-)
FORMUL 8 PG4 9(C8 H18 O5)
FORMUL 12 NA NA 1+
FORMUL 20 PE4 C16 H34 O8
FORMUL 26 HOH *529(H2 O)
HELIX 1 1 ASN A 40 TYR A 48 1 9
HELIX 2 2 ARG A 62 GLY A 64 5 3
HELIX 3 3 SER A 73 THR A 84 1 12
HELIX 4 4 LYS A 117 TYR A 121 5 5
HELIX 5 5 THR A 122 GLN A 127 1 6
HELIX 6 6 THR A 145 ARG A 154 1 10
HELIX 7 7 PRO A 167 MSE A 178 1 12
HELIX 8 8 ASP A 190 ASN A 201 1 12
HELIX 9 9 THR A 212 ASN A 222 1 11
HELIX 10 10 PRO A 225 SER A 227 5 3
HELIX 11 11 THR A 238 ARG A 251 1 14
HELIX 12 12 SER A 262 LEU A 266 5 5
HELIX 13 13 THR A 268 GLN A 282 1 15
HELIX 14 14 ARG A 291 SER A 300 1 10
HELIX 15 15 SER A 301 ILE A 303 5 3
HELIX 16 16 LYS A 309 LYS A 311 5 3
HELIX 17 17 ASN B 40 TYR B 48 1 9
HELIX 18 18 ARG B 62 GLY B 64 5 3
HELIX 19 19 SER B 73 THR B 84 1 12
HELIX 20 20 LYS B 117 TYR B 121 5 5
HELIX 21 21 THR B 122 GLN B 127 1 6
HELIX 22 22 THR B 145 ARG B 154 1 10
HELIX 23 23 PRO B 167 MSE B 178 1 12
HELIX 24 24 ASP B 190 ASN B 201 1 12
HELIX 25 25 THR B 212 ASN B 222 1 11
HELIX 26 26 PRO B 225 SER B 227 5 3
HELIX 27 27 THR B 238 ARG B 251 1 14
HELIX 28 28 SER B 262 LEU B 266 5 5
HELIX 29 29 THR B 268 GLN B 282 1 15
HELIX 30 30 ARG B 291 SER B 300 1 10
HELIX 31 31 SER B 301 ILE B 303 5 3
HELIX 32 32 LYS B 309 LYS B 311 5 3
SHEET 1 A 2 MSE A 33 LEU A 36 0
SHEET 2 A 2 PHE A 313 LEU A 316 -1 O LEU A 316 N MSE A 33
SHEET 1 B 9 LEU A 57 GLY A 60 0
SHEET 2 B 9 THR A 87 ILE A 90 1 O THR A 87 N GLY A 60
SHEET 3 B 9 LEU A 159 LEU A 161 1 O ILE A 160 N PHE A 88
SHEET 4 B 9 VAL A 184 VAL A 188 1 O MSE A 185 N LEU A 159
SHEET 5 B 9 PHE A 206 PHE A 209 1 O GLU A 207 N VAL A 188
SHEET 6 B 9 ILE A 229 GLY A 234 1 O MSE A 230 N ALA A 208
SHEET 7 B 9 CYS A 255 SER A 258 1 O MSE A 256 N ALA A 231
SHEET 8 B 9 ILE A 286 SER A 289 1 O GLU A 288 N ILE A 257
SHEET 9 B 9 LEU A 57 GLY A 60 1 N SER A 59 O ILE A 287
SHEET 1 C 2 PRO A 92 LEU A 94 0
SHEET 2 C 2 ILE A 100 LEU A 102 -1 O VAL A 101 N ARG A 93
SHEET 1 D 2 MSE B 33 LEU B 36 0
SHEET 2 D 2 PHE B 313 LEU B 316 -1 O LEU B 316 N MSE B 33
SHEET 1 E 9 LEU B 57 GLY B 60 0
SHEET 2 E 9 THR B 87 ILE B 90 1 O THR B 87 N GLY B 60
SHEET 3 E 9 LEU B 159 LEU B 161 1 O ILE B 160 N ILE B 90
SHEET 4 E 9 VAL B 184 VAL B 188 1 O MSE B 185 N LEU B 159
SHEET 5 E 9 PHE B 206 PHE B 209 1 O GLU B 207 N VAL B 188
SHEET 6 E 9 ILE B 229 GLY B 234 1 O TYR B 232 N ALA B 208
SHEET 7 E 9 CYS B 255 SER B 258 1 O MSE B 256 N VAL B 233
SHEET 8 E 9 ILE B 286 SER B 289 1 O GLU B 288 N ILE B 257
SHEET 9 E 9 LEU B 57 GLY B 60 1 N SER B 59 O ILE B 287
SHEET 1 F 2 PRO B 92 LEU B 94 0
SHEET 2 F 2 ILE B 100 LEU B 102 -1 O VAL B 101 N ARG B 93
LINK C GLY A 32 N MSE A 33 1555 1555 1.33
LINK C MSE A 33 N ASN A 34 1555 1555 1.32
LINK C SER A 73 N MSE A 74 1555 1555 1.33
LINK C MSE A 74 N GLU A 75 1555 1555 1.32
LINK C PRO A 167 N MSE A 168 1555 1555 1.33
LINK C MSE A 168 N GLU A 169 1555 1555 1.33
LINK C ASP A 177 N MSE A 178 1555 1555 1.33
LINK C MSE A 178 N GLN A 179 1555 1555 1.34
LINK C VAL A 184 N MSE A 185 1555 1555 1.33
LINK C MSE A 185 N ILE A 186 1555 1555 1.32
LINK C PHE A 204 N MSE A 205 1555 1555 1.32
LINK C MSE A 205 N PHE A 206 1555 1555 1.34
LINK C ILE A 229 N MSE A 230 1555 1555 1.34
LINK C MSE A 230 N ALA A 231 1555 1555 1.34
LINK C ASP A 246 N MSE A 247 1555 1555 1.34
LINK C MSE A 247 N LEU A 248 1555 1555 1.32
LINK C VAL A 253 N MSE A 254 1555 1555 1.33
LINK C MSE A 254 N CYS A 255 1555 1555 1.33
LINK C CYS A 255 N MSE A 256 1555 1555 1.31
LINK C MSE A 256 N ILE A 257 1555 1555 1.33
LINK C ARG A 277 N MSE A 278 1555 1555 1.33
LINK C MSE A 278 N ILE A 279 1555 1555 1.34
LINK C GLY B 32 N MSE B 33 1555 1555 1.34
LINK C MSE B 33 N ASN B 34 1555 1555 1.33
LINK C SER B 73 N MSE B 74 1555 1555 1.33
LINK C MSE B 74 N GLU B 75 1555 1555 1.33
LINK C PRO B 167 N MSE B 168 1555 1555 1.33
LINK C MSE B 168 N GLU B 169 1555 1555 1.34
LINK C ASP B 177 N MSE B 178 1555 1555 1.33
LINK C MSE B 178 N GLN B 179 1555 1555 1.34
LINK C VAL B 184 N MSE B 185 1555 1555 1.33
LINK C MSE B 185 N ILE B 186 1555 1555 1.31
LINK C PHE B 204 N MSE B 205 1555 1555 1.32
LINK C MSE B 205 N PHE B 206 1555 1555 1.33
LINK C ILE B 229 N MSE B 230 1555 1555 1.34
LINK C MSE B 230 N ALA B 231 1555 1555 1.34
LINK C ASP B 246 N MSE B 247 1555 1555 1.32
LINK C MSE B 247 N LEU B 248 1555 1555 1.33
LINK C VAL B 253 N MSE B 254 1555 1555 1.33
LINK C MSE B 254 N CYS B 255 1555 1555 1.32
LINK C CYS B 255 N MSE B 256 1555 1555 1.33
LINK C MSE B 256 N ILE B 257 1555 1555 1.33
LINK C ARG B 277 N MSE B 278 1555 1555 1.34
LINK C MSE B 278 N ILE B 279 1555 1555 1.32
LINK NA NA B 1 O6 PE4 B 14 1555 1555 2.68
LINK NA NA B 1 O5 PE4 B 14 1555 1555 2.81
LINK NA NA B 1 O1 PE4 B 14 1555 1555 3.01
LINK NA NA B 1 O4 PE4 B 14 1555 1555 3.07
SITE 1 AC1 6 HIS A 61 ARG A 62 HIS A 104 HOH A 347
SITE 2 AC1 6 HOH A 356 HOH A 501
SITE 1 AC2 3 MSE A 247 GLU A 250 ARG A 251
SITE 1 AC3 7 LYS A 163 PRO A 167 MSE A 168 HOH A 397
SITE 2 AC3 7 HOH A 425 HOH A 500 HOH A 504
SITE 1 AC4 7 ARG A 65 ASP A 264 LYS A 265 ARG A 291
SITE 2 AC4 7 HOH A 375 HOH A 438 HOH A 569
SITE 1 AC5 6 ARG A 62 ARG A 65 LYS A 265 HOH A 319
SITE 2 AC5 6 HOH A 325 LYS B 117
SITE 1 AC6 4 ARG A 54 LEU A 302 HOH A 510 HOH A 554
SITE 1 AC7 1 LYS A 236
SITE 1 AC8 4 PRO A 56 THR A 84 ALA A 296 HOH A 363
SITE 1 AC9 5 ILE A 38 ARG A 154 GLN A 179 TYR A 183
SITE 2 AC9 5 ARG B 154
SITE 1 BC1 1 PE4 B 14
SITE 1 BC2 7 HIS B 61 ARG B 62 HIS B 104 HOH B 335
SITE 2 BC2 7 HOH B 351 HOH B 501 HOH B 553
SITE 1 BC3 8 LYS A 117 ARG B 62 ARG B 65 LYS B 265
SITE 2 BC3 8 HOH B 372 HOH B 375 HOH B 539 HOH B 559
SITE 1 BC4 4 LYS B 163 PRO B 167 MSE B 168 HOH B 345
SITE 1 BC5 3 MSE B 247 GLU B 250 ARG B 251
SITE 1 BC6 7 ARG B 65 ASP B 264 LYS B 265 ARG B 291
SITE 2 BC6 7 HOH B 386 HOH B 440 HOH B 536
SITE 1 BC7 3 GLU B 135 ARG B 291 HOH B 471
SITE 1 BC8 3 ARG B 93 LYS B 164 HOH B 394
SITE 1 BC9 5 NA B 1 ASP B 97 SER B 98 TRP B 123
SITE 2 BC9 5 ARG B 170
SITE 1 CC1 2 PG4 B 16 LYS B 236
SITE 1 CC2 2 PG4 B 15 LYS B 236
SITE 1 CC3 2 ASP A 221 HOH B 463
SITE 1 CC4 7 ILE B 55 PRO B 56 LEU B 57 THR B 84
SITE 2 CC4 7 ALA B 296 SER B 300 HOH B 420
SITE 1 CC5 6 PRO A 202 GLU B 109 SER B 112 ASN B 113
SITE 2 CC5 6 GLY B 114 LYS B 132
CRYST1 53.577 90.481 60.373 90.00 111.95 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 0.018665 0.000000 0.007524 0.00000
SCALE2 0.000000 0.011052 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017859 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
