HEADER HYDROLASE 26-APR-12 4ARV
TITLE YERSINIA KRISTENSENII PHYTASE APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHYTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.3.26;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA KRISTENSENII;
SOURCE 3 ORGANISM_TAXID: 28152;
SOURCE 4 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS HYDROLASE, 6-PHYTASE, MYO-INOSITOL HEXAKIS PHOSPHATE
KEYWDS 2 PHOSPHOHYDROLASE, HISTIDINE ACID PHOSPHATASE, HAPP
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ARIZA,O.V.MOROZ,E.B.BLAGOVA,J.P.TURKENBURG,J.VEVODOVA,S.ROBERTS,
AUTHOR 2 J.VIND,C.SJOHOLM,S.F.LASSEN,L.DE MARIA,V.GLITSOE,L.K.SKOV,K.S.WILSON
REVDAT 4 20-DEC-23 4ARV 1 REMARK
REVDAT 3 05-FEB-14 4ARV 1 JRNL
REVDAT 2 19-JUN-13 4ARV 1 JRNL FORMUL
REVDAT 1 08-MAY-13 4ARV 0
JRNL AUTH A.ARIZA,O.V.MOROZ,E.V.BLAGOVA,J.P.TURKENBURG,J.WATERMAN,
JRNL AUTH 2 S.M.ROBERTS,J.VIND,C.SJOHOLM,S.F.LASSEN,L.DE MARIA,
JRNL AUTH 3 V.GLITSOE,L.K.SKOV,K.S.WILSON
JRNL TITL DEGRADATION OF PHYTATE BY THE 6-PHYTASE FROM HAFNIA ALVEI: A
JRNL TITL 2 COMBINED STRUCTURAL AND SOLUTION STUDY.
JRNL REF PLOS ONE V. 8 65062 2013
JRNL REFN ESSN 1932-6203
JRNL PMID 23741456
JRNL DOI 10.1371/JOURNAL.PONE.0065062
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 103327
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5512
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) : 1.67
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.71
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6884
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 369
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6360
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 1160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.25000
REMARK 3 B13 (A**2) : -0.21000
REMARK 3 B23 (A**2) : 0.44000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.093
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.095
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.814
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6723 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6480 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9150 ; 1.805 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14955 ; 0.875 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 862 ; 5.815 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 306 ;37.783 ;25.294
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1146 ;12.793 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;16.824 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1001 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7684 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1495 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 23
REMARK 3 RESIDUE RANGE : A 45 A 134
REMARK 3 RESIDUE RANGE : A 264 A 414
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1851 3.5781 42.9771
REMARK 3 T TENSOR
REMARK 3 T11: 0.0597 T22: 0.0968
REMARK 3 T33: 0.0839 T12: -0.0209
REMARK 3 T13: -0.0028 T23: 0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 1.1407 L22: 1.2294
REMARK 3 L33: 1.4777 L12: -0.0605
REMARK 3 L13: 0.2760 L23: -0.2736
REMARK 3 S TENSOR
REMARK 3 S11: 0.0423 S12: -0.2854 S13: -0.2428
REMARK 3 S21: 0.1365 S22: 0.0716 S23: 0.0882
REMARK 3 S31: 0.1884 S32: -0.1866 S33: -0.1139
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 24 A 44
REMARK 3 RESIDUE RANGE : A 135 A 263
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2670 20.1151 21.6598
REMARK 3 T TENSOR
REMARK 3 T11: 0.0402 T22: 0.0204
REMARK 3 T33: 0.0672 T12: -0.0051
REMARK 3 T13: 0.0098 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 2.3625 L22: 0.8663
REMARK 3 L33: 2.1617 L12: -0.2159
REMARK 3 L13: 0.7356 L23: -0.6605
REMARK 3 S TENSOR
REMARK 3 S11: -0.0150 S12: 0.1441 S13: 0.3387
REMARK 3 S21: -0.0189 S22: -0.0195 S23: -0.0409
REMARK 3 S31: -0.2334 S32: 0.0808 S33: 0.0345
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 23
REMARK 3 RESIDUE RANGE : B 45 B 134
REMARK 3 RESIDUE RANGE : B 264 B 414
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3666 -5.6628 6.6744
REMARK 3 T TENSOR
REMARK 3 T11: 0.0363 T22: 0.0339
REMARK 3 T33: 0.0666 T12: -0.0149
REMARK 3 T13: -0.0020 T23: 0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 1.0361 L22: 0.9914
REMARK 3 L33: 1.2363 L12: -0.0280
REMARK 3 L13: 0.0592 L23: -0.1380
REMARK 3 S TENSOR
REMARK 3 S11: 0.0382 S12: -0.1444 S13: -0.2014
REMARK 3 S21: 0.0818 S22: -0.0036 S23: 0.0546
REMARK 3 S31: 0.1556 S32: -0.0688 S33: -0.0347
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 24 B 44
REMARK 3 RESIDUE RANGE : B 135 B 263
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4597 12.3197 -13.4637
REMARK 3 T TENSOR
REMARK 3 T11: 0.0571 T22: 0.0388
REMARK 3 T33: 0.0662 T12: -0.0097
REMARK 3 T13: -0.0031 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 2.3866 L22: 0.9507
REMARK 3 L33: 1.9996 L12: -0.0839
REMARK 3 L13: 0.8374 L23: -0.5219
REMARK 3 S TENSOR
REMARK 3 S11: -0.0634 S12: 0.2242 S13: 0.3203
REMARK 3 S21: -0.0574 S22: -0.0187 S23: -0.0366
REMARK 3 S31: -0.2625 S32: 0.1284 S33: 0.0822
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES WITH TLS ADDED HYDROGENS HAVE
REMARK 3 BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 4ARV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1290052243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118484
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 1.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.18000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4ARS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN CONCENTRATION 10MG/ML;
REMARK 280 CONDITION A12 FROM PACT SCREEN: SUCCINATE PHOSPHATE BORATE PH
REMARK 280 5.0, 25% PEG1500
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A -26
REMARK 465 THR A -25
REMARK 465 VAL A -24
REMARK 465 ALA A -23
REMARK 465 LYS A -22
REMARK 465 LYS A -21
REMARK 465 TYR A -20
REMARK 465 LEU A -19
REMARK 465 ARG A -18
REMARK 465 LEU A -17
REMARK 465 SER A -16
REMARK 465 VAL A -15
REMARK 465 LEU A -14
REMARK 465 THR A -13
REMARK 465 LEU A -12
REMARK 465 VAL A -11
REMARK 465 LEU A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 PHE A -7
REMARK 465 THR A -6
REMARK 465 LEU A -5
REMARK 465 SER A -4
REMARK 465 ALA A -3
REMARK 465 ALA A -2
REMARK 465 PRO A -1
REMARK 465 LEU A 0
REMARK 465 ALA A 1
REMARK 465 ALA A 2
REMARK 465 GLN A 3
REMARK 465 SER A 4
REMARK 465 THR A 5
REMARK 465 MET B -26
REMARK 465 THR B -25
REMARK 465 VAL B -24
REMARK 465 ALA B -23
REMARK 465 LYS B -22
REMARK 465 LYS B -21
REMARK 465 TYR B -20
REMARK 465 LEU B -19
REMARK 465 ARG B -18
REMARK 465 LEU B -17
REMARK 465 SER B -16
REMARK 465 VAL B -15
REMARK 465 LEU B -14
REMARK 465 THR B -13
REMARK 465 LEU B -12
REMARK 465 VAL B -11
REMARK 465 LEU B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 PHE B -7
REMARK 465 THR B -6
REMARK 465 LEU B -5
REMARK 465 SER B -4
REMARK 465 ALA B -3
REMARK 465 ALA B -2
REMARK 465 PRO B -1
REMARK 465 LEU B 0
REMARK 465 ALA B 1
REMARK 465 ALA B 2
REMARK 465 GLN B 3
REMARK 465 SER B 4
REMARK 465 THR B 5
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 C1 EDO B 1419 O HOH B 2591 2.12
REMARK 500 OE1 GLU B 168 O HOH B 2347 2.14
REMARK 500 O HOH B 2234 O HOH B 2236 2.19
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 ARG A 147 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 158 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 158 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 GLU A 199 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 233 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 MET A 360 CG - SD - CE ANGL. DEV. = 10.3 DEGREES
REMARK 500 GLU B 199 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP B 233 CB - CG - OD1 ANGL. DEV. = 7.0 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 ALA A 105 59.09 -148.39
REMARK 500 CYS A 188 65.45 -102.04
REMARK 500 LYS A 372 -61.78 -99.62
REMARK 500 CYS B 188 55.16 -91.86
REMARK 500 LYS B 372 -61.71 -90.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2028 DISTANCE = 6.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1419
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TOE A 1420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1418
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1419
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P15 B 1420
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ARO RELATED DB: PDB
REMARK 900 HAFNIA ALVEI PHYTASE IN COMPLEX WITH MYO-INOSITOL HEXAKIS SULPHATE
REMARK 900 RELATED ID: 4ARS RELATED DB: PDB
REMARK 900 HAFNIA ALVEI PHYTASE APO FORM
REMARK 900 RELATED ID: 4ARU RELATED DB: PDB
REMARK 900 HAFNIA ALVEI PHYTASE IN COMPLEX WITH TARTRATE
DBREF 4ARV A -26 414 UNP H9TUK6 H9TUK6_YERKR 1 441
DBREF 4ARV B -26 414 UNP H9TUK6 H9TUK6_YERKR 1 441
SEQRES 1 A 441 MET THR VAL ALA LYS LYS TYR LEU ARG LEU SER VAL LEU
SEQRES 2 A 441 THR LEU VAL LEU SER SER PHE THR LEU SER ALA ALA PRO
SEQRES 3 A 441 LEU ALA ALA GLN SER THR GLY TYR THR LEU GLU ARG VAL
SEQRES 4 A 441 VAL ILE LEU SER ARG HIS GLY VAL ARG SER PRO THR LYS
SEQRES 5 A 441 GLN THR GLN LEU MET ASN ASP VAL THR PRO ASP LYS TRP
SEQRES 6 A 441 PRO GLN TRP PRO VAL LYS ALA GLY TYR LEU THR PRO ARG
SEQRES 7 A 441 GLY ALA GLY LEU VAL THR LEU MET GLY GLY PHE TYR GLY
SEQRES 8 A 441 ASP TYR PHE ARG SER TYR GLY LEU LEU PRO ALA GLY CYS
SEQRES 9 A 441 PRO ALA ASP GLU SER ILE TYR VAL GLN ALA ASP VAL ASP
SEQRES 10 A 441 GLN ARG THR ARG LEU THR GLY GLN ALA PHE LEU ASP GLY
SEQRES 11 A 441 ILE ALA PRO ASP CYS GLY LEU LYS VAL HIS TYR GLN ALA
SEQRES 12 A 441 ASP LEU LYS LYS ILE ASP PRO LEU PHE HIS THR VAL GLU
SEQRES 13 A 441 ALA GLY VAL CYS LYS LEU ASP PRO GLU LYS THR HIS GLN
SEQRES 14 A 441 ALA VAL GLU LYS ARG LEU GLY GLY PRO LEU ASN GLU LEU
SEQRES 15 A 441 SER GLN ARG TYR ALA LYS PRO PHE ALA LEU MET GLY GLU
SEQRES 16 A 441 VAL LEU ASN PHE SER ALA SER PRO TYR CYS ASN SER LEU
SEQRES 17 A 441 GLN GLN LYS GLY LYS ALA CYS ASP PHE ALA THR PHE ALA
SEQRES 18 A 441 ALA ASN GLU ILE GLU VAL ASN LYS GLU GLY THR LYS VAL
SEQRES 19 A 441 SER LEU SER GLY PRO LEU ALA LEU SER SER THR LEU GLY
SEQRES 20 A 441 GLU ILE PHE LEU LEU GLN ASN SER GLN ALA MET PRO ASP
SEQRES 21 A 441 VAL ALA TRP ASN ARG LEU SER GLY GLU GLU ASN TRP ILE
SEQRES 22 A 441 SER LEU LEU SER LEU HIS ASN ALA GLN PHE ASP LEU MET
SEQRES 23 A 441 ALA LYS THR PRO TYR ILE ALA ARG HIS LYS GLY THR PRO
SEQRES 24 A 441 LEU LEU GLN GLN ILE ASP THR ALA LEU VAL LEU GLN ARG
SEQRES 25 A 441 ASP ALA GLN GLY GLN THR LEU PRO LEU SER PRO GLN THR
SEQRES 26 A 441 LYS LEU LEU PHE LEU GLY GLY HIS ASP THR ASN ILE ALA
SEQRES 27 A 441 ASN ILE ALA GLY MET LEU GLY ALA ASN TRP GLN LEU PRO
SEQRES 28 A 441 GLN GLN PRO ASP ASN THR PRO PRO GLY GLY GLY LEU VAL
SEQRES 29 A 441 PHE GLU LEU TRP GLN ASN PRO ASP ASN HIS GLN ARG TYR
SEQRES 30 A 441 VAL ALA VAL LYS MET PHE TYR GLN THR MET GLU GLN LEU
SEQRES 31 A 441 ARG ASN ALA ASP LYS LEU ASP LEU LYS ASN ASN PRO ALA
SEQRES 32 A 441 ARG ILE VAL PRO ILE ALA ILE GLU GLY CYS GLU ASN GLU
SEQRES 33 A 441 GLY ASP ASN LYS LEU CYS GLN LEU GLU THR PHE GLN LYS
SEQRES 34 A 441 LYS VAL ALA GLN VAL ILE GLU PRO SER CYS HIS ILE
SEQRES 1 B 441 MET THR VAL ALA LYS LYS TYR LEU ARG LEU SER VAL LEU
SEQRES 2 B 441 THR LEU VAL LEU SER SER PHE THR LEU SER ALA ALA PRO
SEQRES 3 B 441 LEU ALA ALA GLN SER THR GLY TYR THR LEU GLU ARG VAL
SEQRES 4 B 441 VAL ILE LEU SER ARG HIS GLY VAL ARG SER PRO THR LYS
SEQRES 5 B 441 GLN THR GLN LEU MET ASN ASP VAL THR PRO ASP LYS TRP
SEQRES 6 B 441 PRO GLN TRP PRO VAL LYS ALA GLY TYR LEU THR PRO ARG
SEQRES 7 B 441 GLY ALA GLY LEU VAL THR LEU MET GLY GLY PHE TYR GLY
SEQRES 8 B 441 ASP TYR PHE ARG SER TYR GLY LEU LEU PRO ALA GLY CYS
SEQRES 9 B 441 PRO ALA ASP GLU SER ILE TYR VAL GLN ALA ASP VAL ASP
SEQRES 10 B 441 GLN ARG THR ARG LEU THR GLY GLN ALA PHE LEU ASP GLY
SEQRES 11 B 441 ILE ALA PRO ASP CYS GLY LEU LYS VAL HIS TYR GLN ALA
SEQRES 12 B 441 ASP LEU LYS LYS ILE ASP PRO LEU PHE HIS THR VAL GLU
SEQRES 13 B 441 ALA GLY VAL CYS LYS LEU ASP PRO GLU LYS THR HIS GLN
SEQRES 14 B 441 ALA VAL GLU LYS ARG LEU GLY GLY PRO LEU ASN GLU LEU
SEQRES 15 B 441 SER GLN ARG TYR ALA LYS PRO PHE ALA LEU MET GLY GLU
SEQRES 16 B 441 VAL LEU ASN PHE SER ALA SER PRO TYR CYS ASN SER LEU
SEQRES 17 B 441 GLN GLN LYS GLY LYS ALA CYS ASP PHE ALA THR PHE ALA
SEQRES 18 B 441 ALA ASN GLU ILE GLU VAL ASN LYS GLU GLY THR LYS VAL
SEQRES 19 B 441 SER LEU SER GLY PRO LEU ALA LEU SER SER THR LEU GLY
SEQRES 20 B 441 GLU ILE PHE LEU LEU GLN ASN SER GLN ALA MET PRO ASP
SEQRES 21 B 441 VAL ALA TRP ASN ARG LEU SER GLY GLU GLU ASN TRP ILE
SEQRES 22 B 441 SER LEU LEU SER LEU HIS ASN ALA GLN PHE ASP LEU MET
SEQRES 23 B 441 ALA LYS THR PRO TYR ILE ALA ARG HIS LYS GLY THR PRO
SEQRES 24 B 441 LEU LEU GLN GLN ILE ASP THR ALA LEU VAL LEU GLN ARG
SEQRES 25 B 441 ASP ALA GLN GLY GLN THR LEU PRO LEU SER PRO GLN THR
SEQRES 26 B 441 LYS LEU LEU PHE LEU GLY GLY HIS ASP THR ASN ILE ALA
SEQRES 27 B 441 ASN ILE ALA GLY MET LEU GLY ALA ASN TRP GLN LEU PRO
SEQRES 28 B 441 GLN GLN PRO ASP ASN THR PRO PRO GLY GLY GLY LEU VAL
SEQRES 29 B 441 PHE GLU LEU TRP GLN ASN PRO ASP ASN HIS GLN ARG TYR
SEQRES 30 B 441 VAL ALA VAL LYS MET PHE TYR GLN THR MET GLU GLN LEU
SEQRES 31 B 441 ARG ASN ALA ASP LYS LEU ASP LEU LYS ASN ASN PRO ALA
SEQRES 32 B 441 ARG ILE VAL PRO ILE ALA ILE GLU GLY CYS GLU ASN GLU
SEQRES 33 B 441 GLY ASP ASN LYS LEU CYS GLN LEU GLU THR PHE GLN LYS
SEQRES 34 B 441 LYS VAL ALA GLN VAL ILE GLU PRO SER CYS HIS ILE
HET PO4 A1415 5
HET PO4 A1416 5
HET EDO A1417 4
HET EDO A1418 4
HET EDO A1419 4
HET TOE A1420 11
HET PO4 B1415 5
HET PO4 B1416 5
HET EDO B1417 4
HET EDO B1418 4
HET EDO B1419 4
HET P15 B1420 20
HETNAM PO4 PHOSPHATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL
HETNAM P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PO4 4(O4 P 3-)
FORMUL 5 EDO 6(C2 H6 O2)
FORMUL 8 TOE C7 H16 O4
FORMUL 14 P15 C13 H28 O7
FORMUL 15 HOH *1160(H2 O)
HELIX 1 1 THR A 27 VAL A 33 1 7
HELIX 2 2 THR A 49 TYR A 70 1 22
HELIX 3 3 ASP A 90 ALA A 105 1 16
HELIX 4 4 ASP A 136 GLY A 149 1 14
HELIX 5 5 PRO A 151 ASN A 153 5 3
HELIX 6 6 GLU A 154 TYR A 159 1 6
HELIX 7 7 TYR A 159 ASN A 171 1 13
HELIX 8 8 PHE A 172 ALA A 174 5 3
HELIX 9 9 SER A 175 LYS A 184 1 10
HELIX 10 10 ASP A 189 PHE A 193 5 5
HELIX 11 11 GLY A 211 GLN A 229 1 19
HELIX 12 12 VAL A 234 ARG A 238 5 5
HELIX 13 13 GLY A 241 LYS A 261 1 21
HELIX 14 14 THR A 262 LEU A 283 1 22
HELIX 15 15 HIS A 306 GLY A 318 1 13
HELIX 16 16 THR A 359 ASN A 365 1 7
HELIX 17 17 LEU A 397 ILE A 408 1 12
HELIX 18 18 GLU A 409 HIS A 413 5 5
HELIX 19 19 THR B 27 VAL B 33 1 7
HELIX 20 20 THR B 49 TYR B 70 1 22
HELIX 21 21 ASP B 90 ALA B 105 1 16
HELIX 22 22 ASP B 136 GLY B 149 1 14
HELIX 23 23 PRO B 151 ASN B 153 5 3
HELIX 24 24 GLU B 154 TYR B 159 1 6
HELIX 25 25 TYR B 159 ASN B 171 1 13
HELIX 26 26 PHE B 172 ALA B 174 5 3
HELIX 27 27 SER B 175 LYS B 184 1 10
HELIX 28 28 ASP B 189 PHE B 193 5 5
HELIX 29 29 GLY B 211 GLN B 229 1 19
HELIX 30 30 VAL B 234 ARG B 238 5 5
HELIX 31 31 GLY B 241 LYS B 261 1 21
HELIX 32 32 THR B 262 VAL B 282 1 21
HELIX 33 33 HIS B 306 GLY B 318 1 13
HELIX 34 34 THR B 359 ALA B 366 1 8
HELIX 35 35 LEU B 397 ILE B 408 1 12
HELIX 36 36 GLU B 409 HIS B 413 5 5
SHEET 1 AA 7 HIS A 113 TYR A 114 0
SHEET 2 AA 7 ILE A 83 ALA A 87 1 O VAL A 85 N HIS A 113
SHEET 3 AA 7 LEU A 300 GLY A 305 1 O LEU A 300 N TYR A 84
SHEET 4 AA 7 THR A 8 ARG A 17 1 O VAL A 12 N LEU A 301
SHEET 5 AA 7 GLY A 335 GLN A 342 -1 O LEU A 336 N LEU A 15
SHEET 6 AA 7 ARG A 349 TYR A 357 -1 O TYR A 350 N TRP A 341
SHEET 7 AA 7 ARG A 377 PRO A 380 -1 O ARG A 377 N TYR A 357
SHEET 1 AB 7 HIS A 113 TYR A 114 0
SHEET 2 AB 7 ILE A 83 ALA A 87 1 O VAL A 85 N HIS A 113
SHEET 3 AB 7 LEU A 300 GLY A 305 1 O LEU A 300 N TYR A 84
SHEET 4 AB 7 THR A 8 ARG A 17 1 O VAL A 12 N LEU A 301
SHEET 5 AB 7 GLY A 335 GLN A 342 -1 O LEU A 336 N LEU A 15
SHEET 6 AB 7 ARG A 349 TYR A 357 -1 O TYR A 350 N TRP A 341
SHEET 7 AB 7 CYS A 395 GLN A 396 -1 O CYS A 395 N VAL A 351
SHEET 1 AC 2 ARG A 377 PRO A 380 0
SHEET 2 AC 2 ARG A 349 TYR A 357 -1 O MET A 355 N VAL A 379
SHEET 1 AD 2 GLU A 197 VAL A 200 0
SHEET 2 AD 2 VAL A 207 SER A 210 -1 O SER A 208 N GLU A 199
SHEET 1 BA 6 ILE B 83 ALA B 87 0
SHEET 2 BA 6 LEU B 300 GLY B 305 1 O LEU B 300 N TYR B 84
SHEET 3 BA 6 THR B 8 ARG B 17 1 O VAL B 12 N LEU B 301
SHEET 4 BA 6 GLY B 335 GLN B 342 -1 O LEU B 336 N LEU B 15
SHEET 5 BA 6 ARG B 349 TYR B 357 -1 O TYR B 350 N TRP B 341
SHEET 6 BA 6 ARG B 377 PRO B 380 -1 O ARG B 377 N TYR B 357
SHEET 1 BB 6 ILE B 83 ALA B 87 0
SHEET 2 BB 6 LEU B 300 GLY B 305 1 O LEU B 300 N TYR B 84
SHEET 3 BB 6 THR B 8 ARG B 17 1 O VAL B 12 N LEU B 301
SHEET 4 BB 6 GLY B 335 GLN B 342 -1 O LEU B 336 N LEU B 15
SHEET 5 BB 6 ARG B 349 TYR B 357 -1 O TYR B 350 N TRP B 341
SHEET 6 BB 6 CYS B 395 GLN B 396 -1 O CYS B 395 N VAL B 351
SHEET 1 BC 2 ARG B 377 PRO B 380 0
SHEET 2 BC 2 ARG B 349 TYR B 357 -1 O MET B 355 N VAL B 379
SHEET 1 BD 2 GLU B 197 VAL B 200 0
SHEET 2 BD 2 VAL B 207 SER B 210 -1 O SER B 208 N GLU B 199
SSBOND 1 CYS A 77 CYS A 108 1555 1555 2.03
SSBOND 2 CYS A 133 CYS A 412 1555 1555 2.12
SSBOND 3 CYS A 178 CYS A 188 1555 1555 2.00
SSBOND 4 CYS A 386 CYS A 395 1555 1555 2.10
SSBOND 5 CYS B 77 CYS B 108 1555 1555 2.01
SSBOND 6 CYS B 133 CYS B 412 1555 1555 2.12
SSBOND 7 CYS B 178 CYS B 188 1555 1555 2.02
SSBOND 8 CYS B 386 CYS B 395 1555 1555 2.09
SITE 1 AC1 7 ARG A 17 HIS A 18 ARG A 21 ARG A 92
SITE 2 AC1 7 HIS A 306 ASP A 307 HOH A2561
SITE 1 AC2 10 ASP A 90 ARG A 92 HIS A 126 HIS A 306
SITE 2 AC2 10 HOH A2164 HOH A2170 HOH A2226 HOH A2227
SITE 3 AC2 10 HOH A2561 HOH A2562
SITE 1 AC3 8 ARG A 21 PRO A 23 THR A 24 THR A 218
SITE 2 AC3 8 GLU A 221 ILE A 222 HOH A2037 HOH A2414
SITE 1 AC4 2 GLN A 183 HOH A2563
SITE 1 AC5 5 LYS A 134 HIS A 268 SER A 411 HOH A2428
SITE 2 AC5 5 HOH A2564
SITE 1 AC6 5 TYR A 7 TYR A 70 ASN A 392 HOH A2002
SITE 2 AC6 5 HOH A2566
SITE 1 AC7 7 ARG B 17 HIS B 18 ARG B 21 ARG B 92
SITE 2 AC7 7 HIS B 306 ASP B 307 HOH B2187
SITE 1 AC8 9 ASP B 90 ARG B 92 HIS B 126 HIS B 306
SITE 2 AC8 9 HOH B2182 HOH B2187 HOH B2188 HOH B2262
SITE 3 AC8 9 HOH B2263
SITE 1 AC9 8 ARG B 21 PRO B 23 THR B 24 THR B 218
SITE 2 AC9 8 GLU B 221 ILE B 222 HOH B2039 HOH B2438
SITE 1 BC1 5 GLY B 167 ASN B 171 PHE B 172 SER B 173
SITE 2 BC1 5 HOH B2345
SITE 1 BC2 8 VAL B 207 MET B 259 ALA B 260 LYS B 269
SITE 2 BC2 8 THR B 308 ASN B 312 HOH B2388 HOH B2591
SITE 1 BC3 9 TYR B 7 TYR B 70 TRP B 341 ILE B 378
SITE 2 BC3 9 ASN B 392 HOH B2002 HOH B2592 HOH B2593
SITE 3 BC3 9 HOH B2594
CRYST1 55.410 67.723 73.164 76.67 87.35 78.32 P 1 2
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 0.018047 -0.003731 0.000009 0.00000
SCALE2 0.000000 0.015078 -0.003500 0.00000
SCALE3 0.000000 0.000000 0.014046 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
