HEADER HYDROLASE 07-NOV-13 3WL4
TITLE N,N'-DIACETYLCHITOBIOSE DEACETYLASE (SE-DERIVATIVE) FROM PYROCOCCUS
TITLE 2 FURIOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 186497;
SOURCE 4 STRAIN: ATCC 43587 / DSM 3638 / JCM 8422 / VC1;
SOURCE 5 GENE: PF0354;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZN-DEPENDENT DEACETYLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.NAKAMURA,M.NIIYAMA,W.HASHIMOTO,K.UEGAKI
REVDAT 2 20-AUG-14 3WL4 1 JRNL
REVDAT 1 07-MAY-14 3WL4 0
JRNL AUTH S.MINE,M.NIIYAMA,W.HASHIMOTO,T.IKEGAMI,D.KOMA,T.OHMOTO,
JRNL AUTH 2 Y.FUKUDA,T.INOUE,Y.ABE,T.UEDA,J.MORITA,K.UEGAKI,T.NAKAMURA
JRNL TITL EXPRESSION FROM ENGINEERED ESCHERICHIA COLI CHROMOSOME AND
JRNL TITL 2 CRYSTALLOGRAPHIC STUDY OF ARCHAEAL N,N'-DIACETYLCHITOBIOSE
JRNL TITL 3 DEACETYLASE
JRNL REF FEBS J. V. 281 2584 2014
JRNL REFN ISSN 1742-464X
JRNL PMID 24702737
JRNL DOI 10.1111/FEBS.12805
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 136328
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7197
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) : 1.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.58
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9977
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 585
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 240
REMARK 3 SOLVENT ATOMS : 321
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.050
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.050
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.030
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.814
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4722 ; 0.040 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6268 ; 3.254 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 532 ; 6.051 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 218 ;34.832 ;23.578
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 792 ;11.918 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.339 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 656 ; 0.350 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3422 ; 0.018 ; 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): 2696 ; 1.749 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4364 ; 2.605 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2026 ; 4.560 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1904 ; 6.529 ; 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 : NULL
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 3WL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-NOV-13.
REMARK 100 THE RCSB ID CODE IS RCSB096471.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99522, 0.97910, 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 143526
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL (PH 8.0), 0.2M MGCL2,
REMARK 280 3.4M 1,6-HEXANEDIOL, 5MM CDCL2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.94700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.87837
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 67.00967
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 56.94700
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 32.87837
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 67.00967
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 56.94700
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 32.87837
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 67.00967
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.75673
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 134.01933
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 65.75673
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 134.01933
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 65.75673
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 134.01933
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 53670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 -56.94700
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 98.63510
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -113.89400
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
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 C2 HEZ A 316 O HOH A 532 1.95
REMARK 500 OD2 ASP B 265 O HOH B 556 2.06
REMARK 500 OD2 ASP A 265 O HOH A 564 2.11
REMARK 500 C6 HEZ B 313 O HOH B 536 2.17
REMARK 500 CE LYS A 180 O HOH A 499 2.17
REMARK 500 O5 TAM B 309 O HOH B 463 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 53 CB LYS A 53 CG 0.174
REMARK 500 TYR A 64 CD1 TYR A 64 CE1 0.091
REMARK 500 GLU A 93 CB GLU A 93 CG 0.129
REMARK 500 GLU A 94 CG GLU A 94 CD 0.152
REMARK 500 GLU A 94 CD GLU A 94 OE1 0.101
REMARK 500 PHE A 219 N PHE A 219 CA 0.124
REMARK 500 GLU A 225 CG GLU A 225 CD 0.115
REMARK 500 GLU B 3 CG GLU B 3 CD -0.094
REMARK 500 GLU B 38 CD GLU B 38 OE1 -0.073
REMARK 500 LYS B 53 CB LYS B 53 CG 0.173
REMARK 500 TYR B 64 CD1 TYR B 64 CE1 0.094
REMARK 500 ALA B 85 CA ALA B 85 CB 0.141
REMARK 500 ASN B 108 CG ASN B 108 ND2 -0.158
REMARK 500 LYS B 126 CD LYS B 126 CE -0.185
REMARK 500 GLU B 131 CD GLU B 131 OE2 -0.073
REMARK 500 GLN B 166 CB GLN B 166 CG -0.238
REMARK 500 TYR B 197 CD1 TYR B 197 CE1 0.103
REMARK 500 ILE B 198 CB ILE B 198 CG1 0.172
REMARK 500 ARG B 213 CZ ARG B 213 NH1 0.078
REMARK 500 GLU B 225 CG GLU B 225 CD 0.112
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 LEU A 16 CB - CG - CD1 ANGL. DEV. = -13.4 DEGREES
REMARK 500 ASP A 30 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 43 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 57 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TYR A 64 CB - CG - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLU A 92 OE1 - CD - OE2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ARG A 102 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP A 111 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 118 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 LYS A 126 CD - CE - NZ ANGL. DEV. = -14.1 DEGREES
REMARK 500 LYS A 130 CD - CE - NZ ANGL. DEV. = -14.0 DEGREES
REMARK 500 GLU A 131 OE1 - CD - OE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 153 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 153 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 PHE A 164 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 PHE A 164 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 PHE A 170 CB - CG - CD1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 LYS A 180 CD - CE - NZ ANGL. DEV. = 17.3 DEGREES
REMARK 500 ASP A 203 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 LYS A 210 CD - CE - NZ ANGL. DEV. = -15.0 DEGREES
REMARK 500 PHE A 230 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 232 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 THR A 235 CA - CB - CG2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 TYR A 246 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU B 15 CB - CG - CD2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 LEU B 16 CB - CG - CD1 ANGL. DEV. = -10.6 DEGREES
REMARK 500 PHE B 22 CG - CD1 - CE1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP B 43 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TYR B 64 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TYR B 64 CD1 - CE1 - CZ ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 89 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 GLU B 92 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 TYR B 109 CZ - CE2 - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP B 111 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG B 121 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 129 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 PHE B 137 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ASP B 150 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 152 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG B 153 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 PHE B 164 CB - CG - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 PHE B 164 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 PHE B 170 CB - CG - CD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ILE B 198 CA - CB - CG1 ANGL. DEV. = -11.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 55 ANGLE DEVIATIONS.
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 ASP A 42 -8.12 109.87
REMARK 500 MSE A 48 22.30 -153.86
REMARK 500 THR A 112 1.20 80.46
REMARK 500 ASP B 42 -7.91 106.44
REMARK 500 MSE B 48 23.98 -153.62
REMARK 500 PHE B 219 72.47 -119.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 121 0.10 SIDE CHAIN
REMARK 500 ARG B 121 0.10 SIDE CHAIN
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 B 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 265 OD1
REMARK 620 2 ASP B 265 OD2 54.9
REMARK 620 3 HOH B 555 O 107.7 94.0
REMARK 620 4 HOH B 556 O 105.4 50.5 80.8
REMARK 620 5 HOH B 554 O 98.4 150.5 107.7 151.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 265 OD1
REMARK 620 2 ASP A 265 OD2 53.6
REMARK 620 3 HOH A 565 O 110.7 95.0
REMARK 620 4 HOH A 564 O 105.3 51.9 80.0
REMARK 620 5 HOH A 563 O 99.9 150.9 107.1 149.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 302 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 225 OE2
REMARK 620 2 GLU B 225 OE1 53.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 302 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 225 OE2
REMARK 620 2 GLU A 225 OE1 53.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 301 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TAM B 309 N
REMARK 620 2 HIS B 151 NE2 153.2
REMARK 620 3 ASP B 43 OD2 99.9 93.9
REMARK 620 4 HIS B 40 ND1 104.7 97.6 91.5
REMARK 620 5 TAM B 309 O4 72.1 81.3 126.5 142.0
REMARK 620 6 TAM B 309 O6 74.4 93.9 171.3 83.7 58.6
REMARK 620 7 ASP B 43 OD1 80.5 90.0 52.8 144.0 73.9 131.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 301 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TAM A 309 N
REMARK 620 2 HIS A 151 NE2 155.0
REMARK 620 3 ASP A 43 OD2 100.0 94.2
REMARK 620 4 HIS A 40 ND1 103.9 96.3 91.1
REMARK 620 5 TAM A 309 O4 74.0 94.0 170.6 83.5
REMARK 620 6 ASP A 43 OD1 81.2 91.2 53.0 143.8 131.2
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 CD A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HE2 A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HE2 B 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 322
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WL3 RELATED DB: PDB
REMARK 900 RELATED ID: 3WE7 RELATED DB: PDB
DBREF 3WL4 A 2 267 UNP Q8U3V1 Q8U3V1_PYRFU 2 267
DBREF 3WL4 B 2 267 UNP Q8U3V1 Q8U3V1_PYRFU 2 267
SEQADV 3WL4 MSE A 1 UNP Q8U3V1 EXPRESSION TAG
SEQADV 3WL4 MSE B 1 UNP Q8U3V1 EXPRESSION TAG
SEQRES 1 A 267 MSE PHE GLU ASN VAL SER THR PHE GLU GLU ALA PHE ASN
SEQRES 2 A 267 LYS LEU LEU LYS GLU VAL LEU GLU PHE ASN LEU GLU ASN
SEQRES 3 A 267 PRO PHE GLU ASP ALA LYS LYS VAL ILE CYS ILE GLU PRO
SEQRES 4 A 267 HIS PRO ASP ASP CYS ALA ILE GLY MSE GLY GLY THR ILE
SEQRES 5 A 267 LYS LYS LEU SER ASP GLU GLY VAL GLU VAL ILE TYR ILE
SEQRES 6 A 267 CYS MSE THR ASP GLY TYR MSE GLY THR THR ASP GLU LYS
SEQRES 7 A 267 LEU SER GLY HIS GLU LEU ALA LEU ILE ARG ARG ARG GLU
SEQRES 8 A 267 GLU GLU GLU SER ALA LYS LEU LEU GLY VAL ARG LYS ILE
SEQRES 9 A 267 TYR TRP LEU ASN TYR ARG ASP THR GLU LEU PRO TYR SER
SEQRES 10 A 267 ARG GLU VAL ARG LYS ASP LEU VAL LYS ILE ILE ARG LYS
SEQRES 11 A 267 GLU LYS PRO ASP GLY VAL PHE ALA PRO ASP PRO TRP LEU
SEQRES 12 A 267 PRO TYR GLU SER HIS PRO ASP HIS ARG ARG THR GLY PHE
SEQRES 13 A 267 LEU ALA ILE GLU SER VAL ALA PHE SER GLN LEU PRO ASN
SEQRES 14 A 267 PHE SER ASN ILE ASP ILE ASP ILE GLY LEU LYS PRO HIS
SEQRES 15 A 267 SER VAL SER PHE ILE ALA LEU TYR TYR THR HIS LYS PRO
SEQRES 16 A 267 ASN TYR ILE VAL ASP ILE THR ASP LEU MSE GLU LEU LYS
SEQRES 17 A 267 LEU LYS ALA ILE ARG ALA HIS ARG SER GLN PHE THR ASP
SEQRES 18 A 267 ASP ILE TRP GLU THR TRP GLU PRO PHE LEU ARG THR VAL
SEQRES 19 A 267 THR MSE PHE TYR GLY GLU LYS ILE GLY VAL ARG TYR GLY
SEQRES 20 A 267 GLU GLY PHE ARG VAL MSE PRO GLY LEU PHE TYR HIS ILE
SEQRES 21 A 267 THR PRO PHE ALA ASP LEU ILE
SEQRES 1 B 267 MSE PHE GLU ASN VAL SER THR PHE GLU GLU ALA PHE ASN
SEQRES 2 B 267 LYS LEU LEU LYS GLU VAL LEU GLU PHE ASN LEU GLU ASN
SEQRES 3 B 267 PRO PHE GLU ASP ALA LYS LYS VAL ILE CYS ILE GLU PRO
SEQRES 4 B 267 HIS PRO ASP ASP CYS ALA ILE GLY MSE GLY GLY THR ILE
SEQRES 5 B 267 LYS LYS LEU SER ASP GLU GLY VAL GLU VAL ILE TYR ILE
SEQRES 6 B 267 CYS MSE THR ASP GLY TYR MSE GLY THR THR ASP GLU LYS
SEQRES 7 B 267 LEU SER GLY HIS GLU LEU ALA LEU ILE ARG ARG ARG GLU
SEQRES 8 B 267 GLU GLU GLU SER ALA LYS LEU LEU GLY VAL ARG LYS ILE
SEQRES 9 B 267 TYR TRP LEU ASN TYR ARG ASP THR GLU LEU PRO TYR SER
SEQRES 10 B 267 ARG GLU VAL ARG LYS ASP LEU VAL LYS ILE ILE ARG LYS
SEQRES 11 B 267 GLU LYS PRO ASP GLY VAL PHE ALA PRO ASP PRO TRP LEU
SEQRES 12 B 267 PRO TYR GLU SER HIS PRO ASP HIS ARG ARG THR GLY PHE
SEQRES 13 B 267 LEU ALA ILE GLU SER VAL ALA PHE SER GLN LEU PRO ASN
SEQRES 14 B 267 PHE SER ASN ILE ASP ILE ASP ILE GLY LEU LYS PRO HIS
SEQRES 15 B 267 SER VAL SER PHE ILE ALA LEU TYR TYR THR HIS LYS PRO
SEQRES 16 B 267 ASN TYR ILE VAL ASP ILE THR ASP LEU MSE GLU LEU LYS
SEQRES 17 B 267 LEU LYS ALA ILE ARG ALA HIS ARG SER GLN PHE THR ASP
SEQRES 18 B 267 ASP ILE TRP GLU THR TRP GLU PRO PHE LEU ARG THR VAL
SEQRES 19 B 267 THR MSE PHE TYR GLY GLU LYS ILE GLY VAL ARG TYR GLY
SEQRES 20 B 267 GLU GLY PHE ARG VAL MSE PRO GLY LEU PHE TYR HIS ILE
SEQRES 21 B 267 THR PRO PHE ALA ASP LEU ILE
MODRES 3WL4 MSE A 1 MET SELENOMETHIONINE
MODRES 3WL4 MSE A 48 MET SELENOMETHIONINE
MODRES 3WL4 MSE A 67 MET SELENOMETHIONINE
MODRES 3WL4 MSE A 72 MET SELENOMETHIONINE
MODRES 3WL4 MSE A 205 MET SELENOMETHIONINE
MODRES 3WL4 MSE A 236 MET SELENOMETHIONINE
MODRES 3WL4 MSE A 253 MET SELENOMETHIONINE
MODRES 3WL4 MSE B 1 MET SELENOMETHIONINE
MODRES 3WL4 MSE B 48 MET SELENOMETHIONINE
MODRES 3WL4 MSE B 67 MET SELENOMETHIONINE
MODRES 3WL4 MSE B 72 MET SELENOMETHIONINE
MODRES 3WL4 MSE B 205 MET SELENOMETHIONINE
MODRES 3WL4 MSE B 236 MET SELENOMETHIONINE
MODRES 3WL4 MSE B 253 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 48 8
HET MSE A 67 8
HET MSE A 72 8
HET MSE A 205 8
HET MSE A 236 8
HET MSE A 253 8
HET MSE B 1 8
HET MSE B 48 8
HET MSE B 67 8
HET MSE B 72 8
HET MSE B 205 8
HET MSE B 236 8
HET MSE B 253 8
HET CD A 301 1
HET CD A 302 1
HET CA A 303 1
HET CL A 304 1
HET CL A 305 1
HET CL A 306 1
HET CL A 307 1
HET TAM A 308 11
HET TAM A 309 11
HET HEZ A 310 8
HET HEZ A 311 8
HET HEZ A 312 8
HET HE2 A 313 7
HET HEZ A 314 8
HET HEZ A 315 8
HET HEZ A 316 8
HET HEZ A 317 8
HET HEZ A 318 8
HET HEZ A 319 8
HET CD B 301 1
HET CD B 302 1
HET CA B 303 1
HET CL B 304 1
HET CL B 305 1
HET CL B 306 1
HET CL B 307 1
HET TAM B 308 11
HET TAM B 309 11
HET HEZ B 310 8
HET HEZ B 311 8
HET HEZ B 312 8
HET HEZ B 313 8
HET HEZ B 314 8
HET HEZ B 315 8
HET HE2 B 316 7
HET HEZ B 317 8
HET HEZ B 318 8
HET HEZ B 319 8
HET HEZ B 320 8
HET HEZ B 321 8
HET HEZ B 322 8
HETNAM MSE SELENOMETHIONINE
HETNAM CD CADMIUM ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM TAM TRIS(HYDROXYETHYL)AMINOMETHANE
HETNAM HEZ HEXANE-1,6-DIOL
HETNAM HE2 HEXAN-1-OL
FORMUL 1 MSE 14(C5 H11 N O2 SE)
FORMUL 3 CD 4(CD 2+)
FORMUL 5 CA 2(CA 2+)
FORMUL 6 CL 8(CL 1-)
FORMUL 10 TAM 4(C7 H17 N O3)
FORMUL 12 HEZ 21(C6 H14 O2)
FORMUL 15 HE2 2(C6 H14 O)
FORMUL 44 HOH *321(H2 O)
HELIX 1 1 THR A 7 GLU A 18 1 12
HELIX 2 2 ASP A 42 GLU A 58 1 17
HELIX 3 3 SER A 80 GLY A 100 1 21
HELIX 4 4 SER A 117 LYS A 132 1 16
HELIX 5 5 HIS A 148 SER A 165 1 18
HELIX 6 6 SER A 171 ILE A 177 1 7
HELIX 7 7 LEU A 204 ALA A 214 1 11
HELIX 8 8 THR A 220 LYS A 241 1 22
HELIX 9 9 PRO A 254 HIS A 259 5 6
HELIX 10 10 PHE A 263 ILE A 267 5 5
HELIX 11 11 THR B 7 GLU B 18 1 12
HELIX 12 12 ASP B 42 GLU B 58 1 17
HELIX 13 13 SER B 80 GLY B 100 1 21
HELIX 14 14 SER B 117 LYS B 132 1 16
HELIX 15 15 HIS B 148 SER B 165 1 18
HELIX 16 16 SER B 171 ILE B 177 1 7
HELIX 17 17 LEU B 204 ALA B 214 1 11
HELIX 18 18 THR B 220 LYS B 241 1 22
HELIX 19 19 PRO B 254 HIS B 259 5 6
HELIX 20 20 PHE B 263 ILE B 267 5 5
SHEET 1 A 5 LYS A 103 TYR A 109 0
SHEET 2 A 5 GLU A 61 THR A 68 1 N CYS A 66 O TYR A 105
SHEET 3 A 5 LYS A 33 GLU A 38 1 N CYS A 36 O ILE A 63
SHEET 4 A 5 GLY A 135 PRO A 139 1 O PHE A 137 N ILE A 37
SHEET 5 A 5 PHE A 186 TYR A 190 1 O ALA A 188 N VAL A 136
SHEET 1 B 2 TYR A 197 ASP A 200 0
SHEET 2 B 2 GLY A 247 PHE A 250 -1 O GLU A 248 N VAL A 199
SHEET 1 C 5 LYS B 103 TYR B 109 0
SHEET 2 C 5 GLU B 61 THR B 68 1 N CYS B 66 O TYR B 105
SHEET 3 C 5 LYS B 33 GLU B 38 1 N CYS B 36 O ILE B 63
SHEET 4 C 5 GLY B 135 PRO B 139 1 O PHE B 137 N ILE B 37
SHEET 5 C 5 PHE B 186 TYR B 190 1 O ALA B 188 N VAL B 136
SHEET 1 D 2 TYR B 197 ASP B 200 0
SHEET 2 D 2 GLY B 247 PHE B 250 -1 O GLU B 248 N VAL B 199
LINK C MSE A 1 N PHE A 2 1555 1555 1.37
LINK C GLY A 47 N MSE A 48 1555 1555 1.35
LINK C MSE A 48 N GLY A 49 1555 1555 1.35
LINK C CYS A 66 N MSE A 67 1555 1555 1.34
LINK C MSE A 67 N THR A 68 1555 1555 1.36
LINK C TYR A 71 N MSE A 72 1555 1555 1.36
LINK C MSE A 72 N GLY A 73 1555 1555 1.33
LINK C LEU A 204 N MSE A 205 1555 1555 1.34
LINK C MSE A 205 N GLU A 206 1555 1555 1.35
LINK C THR A 235 N MSE A 236 1555 1555 1.35
LINK C MSE A 236 N PHE A 237 1555 1555 1.33
LINK C VAL A 252 N MSE A 253 1555 1555 1.36
LINK C MSE A 253 N PRO A 254 1555 1555 1.31
LINK C MSE B 1 N PHE B 2 1555 1555 1.37
LINK C GLY B 47 N MSE B 48 1555 1555 1.37
LINK C MSE B 48 N GLY B 49 1555 1555 1.35
LINK C CYS B 66 N MSE B 67 1555 1555 1.35
LINK C MSE B 67 N THR B 68 1555 1555 1.38
LINK C TYR B 71 N MSE B 72 1555 1555 1.33
LINK C MSE B 72 N GLY B 73 1555 1555 1.31
LINK C LEU B 204 N MSE B 205 1555 1555 1.34
LINK C MSE B 205 N GLU B 206 1555 1555 1.36
LINK C THR B 235 N MSE B 236 1555 1555 1.34
LINK C MSE B 236 N PHE B 237 1555 1555 1.35
LINK C VAL B 252 N MSE B 253 1555 1555 1.36
LINK C MSE B 253 N PRO B 254 1555 1555 1.32
LINK OD1 ASP B 265 CA CA B 303 1555 1555 2.22
LINK OD1 ASP A 265 CA CA A 303 1555 1555 2.24
LINK OE2 GLU B 225 CD CD B 302 1555 1555 2.24
LINK OE2 GLU A 225 CD CD A 302 1555 1555 2.25
LINK CD CD B 301 N TAM B 309 1555 1555 2.25
LINK CD CD A 301 N TAM A 309 1555 1555 2.27
LINK NE2 HIS A 151 CD CD A 301 1555 1555 2.29
LINK NE2 HIS B 151 CD CD B 301 1555 1555 2.29
LINK OD2 ASP A 43 CD CD A 301 1555 1555 2.29
LINK OD2 ASP B 43 CD CD B 301 1555 1555 2.32
LINK ND1 HIS B 40 CD CD B 301 1555 1555 2.33
LINK ND1 HIS A 40 CD CD A 301 1555 1555 2.34
LINK CD CD B 301 O4 TAM B 309 1555 1555 2.35
LINK OE1 GLU B 225 CD CD B 302 1555 1555 2.44
LINK CD CD B 301 O6 TAM B 309 1555 1555 2.45
LINK OE1 GLU A 225 CD CD A 302 1555 1555 2.46
LINK CD CD A 301 O4 TAM A 309 1555 1555 2.48
LINK OD2 ASP A 265 CA CA A 303 1555 1555 2.50
LINK OD2 ASP B 265 CA CA B 303 1555 1555 2.51
LINK OD1 ASP A 43 CD CD A 301 1555 1555 2.59
LINK OD1 ASP B 43 CD CD B 301 1555 1555 2.61
LINK CA CA B 303 O HOH B 555 1555 1555 2.27
LINK CA CA A 303 O HOH A 565 1555 1555 2.28
LINK CA CA A 303 O HOH A 564 1555 1555 2.30
LINK CA CA B 303 O HOH B 556 1555 1555 2.30
LINK CA CA A 303 O HOH A 563 1555 1555 2.42
LINK CA CA B 303 O HOH B 554 1555 1555 2.44
SITE 1 AC1 4 HIS A 40 ASP A 43 HIS A 151 TAM A 309
SITE 1 AC2 5 MSE A 1 GLU A 225 CL A 305 CL A 306
SITE 2 AC2 5 CL A 307
SITE 1 AC3 5 HIS A 193 ASP A 265 HOH A 563 HOH A 564
SITE 2 AC3 5 HOH A 565
SITE 1 AC4 5 ARG A 152 ARG A 153 TAM A 308 HEZ A 310
SITE 2 AC4 5 HOH A 524
SITE 1 AC5 3 GLU A 225 CD A 302 PHE B 2
SITE 1 AC6 7 GLU A 225 CD A 302 CL A 307 PHE B 2
SITE 2 AC6 7 ASN B 4 VAL B 5 LYS B 14
SITE 1 AC7 6 MSE A 1 CD A 302 CL A 306 PHE B 2
SITE 2 AC7 6 GLU B 3 ASN B 4
SITE 1 AC8 5 TYR A 116 ARG A 153 CL A 304 HEZ A 310
SITE 2 AC8 5 HOH A 463
SITE 1 AC9 13 HIS A 40 ASP A 42 ASP A 43 ILE A 46
SITE 2 AC9 13 HIS A 151 TYR A 191 GLN A 218 HIS A 259
SITE 3 AC9 13 ILE A 260 CD A 301 HEZ A 315 HOH A 456
SITE 4 AC9 13 HOH A 465
SITE 1 BC1 6 PRO A 141 PHE A 156 CL A 304 TAM A 308
SITE 2 BC1 6 HOH A 413 HOH A 463
SITE 1 BC2 5 PRO A 195 ASN A 196 TYR A 197 ILE A 198
SITE 2 BC2 5 ILE A 242
SITE 1 BC3 4 PHE A 237 GLU A 240 LYS A 241 HOH A 533
SITE 1 BC4 5 GLU A 93 VAL A 101 LYS A 103 ILE A 104
SITE 2 BC4 5 HOH A 496
SITE 1 BC5 7 GLU A 113 PRO A 115 TYR A 116 ARG A 153
SITE 2 BC5 7 HOH A 428 HOH A 435 HOH A 523
SITE 1 BC6 3 GLN A 218 TRP A 227 TAM A 309
SITE 1 BC7 6 LEU A 20 PHE A 22 ASN A 23 PRO A 254
SITE 2 BC7 6 HOH A 530 HOH A 532
SITE 1 BC8 9 GLN A 166 SER A 183 VAL A 184 SER A 185
SITE 2 BC8 9 PHE A 186 ILE A 187 MSE A 253 HEZ A 319
SITE 3 BC8 9 HOH A 426
SITE 1 BC9 6 SER A 6 MSE A 236 GLU A 240 GLY A 243
SITE 2 BC9 6 VAL A 244 ARG A 245
SITE 1 CC1 6 HIS A 148 ILE A 159 ALA A 163 ILE A 187
SITE 2 CC1 6 GLY A 255 HEZ A 317
SITE 1 CC2 4 HIS B 40 ASP B 43 HIS B 151 TAM B 309
SITE 1 CC3 5 MSE B 1 GLU B 225 CL B 305 CL B 306
SITE 2 CC3 5 CL B 307
SITE 1 CC4 5 HIS B 193 ASP B 265 HOH B 554 HOH B 555
SITE 2 CC4 5 HOH B 556
SITE 1 CC5 4 ARG B 152 ARG B 153 TAM B 308 HEZ B 312
SITE 1 CC6 7 PHE A 2 ASN A 4 VAL A 5 LYS A 14
SITE 2 CC6 7 GLU B 225 CD B 302 CL B 306
SITE 1 CC7 6 PHE A 2 GLU A 3 ASN A 4 MSE B 1
SITE 2 CC7 6 CD B 302 CL B 305
SITE 1 CC8 3 PHE A 2 GLU B 225 CD B 302
SITE 1 CC9 6 TYR B 116 ARG B 153 CL B 304 HEZ B 312
SITE 2 CC9 6 HEZ B 313 HOH B 531
SITE 1 DC1 13 HIS B 40 ASP B 42 ASP B 43 ILE B 46
SITE 2 DC1 13 ARG B 88 HIS B 151 TYR B 191 GLN B 218
SITE 3 DC1 13 HIS B 259 ILE B 260 CD B 301 HOH B 452
SITE 4 DC1 13 HOH B 463
SITE 1 DC2 9 GLN B 166 SER B 183 VAL B 184 PHE B 186
SITE 2 DC2 9 ILE B 187 MSE B 253 HEZ B 314 HOH B 428
SITE 3 DC2 9 HOH B 530
SITE 1 DC3 6 PRO B 195 ASN B 196 TYR B 197 ILE B 198
SITE 2 DC3 6 LYS B 241 ILE B 242
SITE 1 DC4 6 PRO B 141 PHE B 156 CL B 304 TAM B 308
SITE 2 DC4 6 HOH B 412 HOH B 531
SITE 1 DC5 7 GLU B 113 PRO B 115 TYR B 116 ARG B 153
SITE 2 DC5 7 TAM B 308 HEZ B 320 HOH B 536
SITE 1 DC6 5 SER B 147 ILE B 159 ALA B 163 HEZ B 310
SITE 2 DC6 5 HEZ B 318
SITE 1 DC7 5 GLU B 93 VAL B 101 LYS B 103 ILE B 104
SITE 2 DC7 5 HOH B 486
SITE 1 DC8 12 ILE B 46 GLY B 47 TYR B 191 LYS B 208
SITE 2 DC8 12 LEU B 231 VAL B 234 THR B 235 TYR B 238
SITE 3 DC8 12 GLY B 247 GLU B 248 ILE B 260 HOH B 432
SITE 1 DC9 10 ARG A 89 ASP B 76 GLU B 77 LYS B 78
SITE 2 DC9 10 LEU B 79 SER B 80 PRO B 168 ASN B 169
SITE 3 DC9 10 HOH B 434 HOH B 535
SITE 1 EC1 9 MSE B 72 ASP B 111 THR B 112 HIS B 148
SITE 2 EC1 9 ALA B 163 GLN B 166 LEU B 167 HEZ B 314
SITE 3 EC1 9 HOH B 452
SITE 1 EC2 5 LEU B 20 PHE B 22 PRO B 254 GLY B 255
SITE 2 EC2 5 HOH B 426
SITE 1 EC3 10 HOH A 445 TYR B 109 ARG B 110 GLU B 113
SITE 2 EC3 10 PRO B 115 ARG B 118 HEZ B 313 HOH B 431
SITE 3 EC3 10 HOH B 439 HOH B 506
SITE 1 EC4 2 TYR B 145 HOH B 442
SITE 1 EC5 5 PHE B 8 PHE B 237 GLU B 240 LYS B 241
SITE 2 EC5 5 HOH B 511
CRYST1 113.894 113.894 201.029 90.00 90.00 120.00 H 3 18
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 0.008780 0.005069 0.000000 0.00000
SCALE2 0.000000 0.010138 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004974 0.00000
HETATM 1 N MSE A 1 -23.634 29.602 -14.149 1.00 22.68 N
HETATM 2 CA MSE A 1 -24.559 28.578 -14.680 1.00 19.18 C
HETATM 3 C MSE A 1 -25.748 29.204 -15.348 1.00 19.38 C
HETATM 4 O MSE A 1 -26.143 30.321 -14.990 1.00 21.12 O
HETATM 5 CB MSE A 1 -25.137 27.730 -13.534 1.00 19.08 C
HETATM 6 CG MSE A 1 -24.016 26.826 -12.909 1.00 19.56 C
HETATM 7 SE MSE A 1 -24.584 25.878 -11.313 1.00 23.40 SE
HETATM 8 CE MSE A 1 -24.189 27.334 -10.018 1.00 26.25 C
(ATOM LINES ARE NOT SHOWN.)
END