HEADER HYDROLASE 11-JUN-15 5BZX
TITLE CRYSTAL STRUCTURE OF HUMAN PHOSPHATASE PTEN TREATED WITH A
TITLE 2 BISPEROXOVANADIUM COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE AND
COMPND 3 DUAL-SPECIFICITY PROTEIN PHOSPHATASE PTEN;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: PTEN WT 7-353 DELTA 286-309;
COMPND 6 SYNONYM: MUTATED IN MULTIPLE ADVANCED CANCERS 1,PHOSPHATASE AND
COMPND 7 TENSIN HOMOLOG;
COMPND 8 EC: 3.1.3.16,3.1.3.48,3.1.3.67;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PTEN, MMAC1, TEP1;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFH1
KEYWDS PHOSPHATASE, C2 DOMAIN, DISULFIDE, OXIDIZED, VANADATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-U.LEE,D.BIER,S.HENNIG,T.N.GROSSMANN
REVDAT 2 11-NOV-15 5BZX 1 JRNL
REVDAT 1 07-OCT-15 5BZX 0
JRNL AUTH C.U.LEE,G.HAHNE,J.HANSKE,T.BANGE,D.BIER,C.RADEMACHER,
JRNL AUTH 2 S.HENNIG,T.N.GROSSMANN
JRNL TITL REDOX MODULATION OF PTEN PHOSPHATASE ACTIVITY BY HYDROGEN
JRNL TITL 2 PEROXIDE AND BISPEROXIDOVANADIUM COMPLEXES.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 54 13796 2015
JRNL REFN ESSN 1521-3773
JRNL PMID 26418532
JRNL DOI 10.1002/ANIE.201506338
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 62095
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3297
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4369
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.3420
REMARK 3 BIN FREE R VALUE SET COUNT : 231
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10310
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -33.11000
REMARK 3 B22 (A**2) : -30.39000
REMARK 3 B33 (A**2) : 63.50000
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): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.673
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10650 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9820 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14409 ; 1.538 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22568 ; 1.451 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1252 ;12.460 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 543 ;31.762 ;23.499
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1772 ;18.237 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 62 ;22.534 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1488 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12052 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2672 ; 0.005 ; 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): 5020 ; 3.550 ; 6.109
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5019 ; 3.549 ; 6.108
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6268 ; 5.666 ; 9.163
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.501
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.499
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 : 1.20
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5BZX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210556.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.77119
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65393
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 46.293
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.91
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.55200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 1D5R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.25 M L-TARTRAT,
REMARK 280 7.5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.83500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.83500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 103.53000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 103.45000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 103.53000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 103.45000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 43.83500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 103.53000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 103.45000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.83500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 103.53000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 103.45000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
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: C
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: 4
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: D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 510 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 522 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 624 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 620 LIES ON A SPECIAL POSITION.
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 40 CG CD OE1 OE2
REMARK 470 VAL A 45 CG1 CG2
REMARK 470 TYR A 46 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 62 CG CD CE NZ
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 80 CG CD CE NZ
REMARK 470 ASN A 82 CG OD1 ND2
REMARK 470 HIS A 185 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 311 CG OD1 ND2
REMARK 470 ASP A 312 CG OD1 OD2
REMARK 470 LYS A 349 CG CD CE NZ
REMARK 470 ARG B 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 40 CG CD OE1 OE2
REMARK 470 LYS B 62 CG CD CE NZ
REMARK 470 ASP B 116 CG OD1 OD2
REMARK 470 LYS B 183 CG CD CE NZ
REMARK 470 LYS B 221 CG CD CE NZ
REMARK 470 LYS B 260 CG CD CE NZ
REMARK 470 ASN B 262 CG OD1 ND2
REMARK 470 LEU B 265 CG CD1 CD2
REMARK 470 LYS B 266 CG CD CE NZ
REMARK 470 ASN B 311 CG OD1 ND2
REMARK 470 ASP B 312 CG OD1 OD2
REMARK 470 GLU B 314 CG CD OE1 OE2
REMARK 470 ARG C 14 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 47 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 80 CG CD CE NZ
REMARK 470 LYS C 221 CG CD CE NZ
REMARK 470 LYS C 260 CG CD CE NZ
REMARK 470 GLN C 261 CG CD OE1 NE2
REMARK 470 MET C 264 CG SD CE
REMARK 470 LEU C 265 CG CD1 CD2
REMARK 470 LYS C 266 CG CD CE NZ
REMARK 470 GLU C 284 CG CD OE1 OE2
REMARK 470 GLU C 285 CG CD OE1 OE2
REMARK 470 ASP C 310 CG OD1 OD2
REMARK 470 ARG D 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 40 CG CD OE1 OE2
REMARK 470 TYR D 46 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 62 CG CD CE NZ
REMARK 470 GLU D 91 CG CD OE1 OE2
REMARK 470 LYS D 221 CG CD CE NZ
REMARK 470 GLN D 261 CG CD OE1 NE2
REMARK 470 LYS D 263 CG CD CE NZ
REMARK 470 MET D 264 CG SD CE
REMARK 470 LEU D 265 CG CD1 CD2
REMARK 470 LYS D 266 CG CD CE NZ
REMARK 470 GLU D 285 CG CD OE1 OE2
REMARK 470 ASP D 310 CG OD1 OD2
REMARK 470 ASP D 312 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 683 O HOH B 688 0.35
REMARK 500 O HOH D 596 O HOH D 646 0.86
REMARK 500 O HOH D 506 O HOH D 539 1.81
REMARK 500 O HOH B 597 O HOH B 636 1.87
REMARK 500 SG CYS C 218 O HOH C 675 1.88
REMARK 500 OD1 ASP B 24 O HOH B 501 1.94
REMARK 500 OD1 ASP B 92 O HOH B 502 1.94
REMARK 500 O ASP A 312 N LYS C 266 1.97
REMARK 500 O41 TLA B 401 O HOH B 503 1.98
REMARK 500 NH2 ARG B 15 O TYR B 27 1.99
REMARK 500 SG CYS A 218 O HOH A 599 1.99
REMARK 500 O HOH A 582 O HOH A 602 2.00
REMARK 500 O LEU C 220 O HOH C 501 2.00
REMARK 500 O ASP A 312 CB LEU C 265 2.01
REMARK 500 N LYS D 327 O HOH D 501 2.01
REMARK 500 O HOH A 601 O HOH A 628 2.02
REMARK 500 O HOH C 507 O HOH C 639 2.02
REMARK 500 O HOH D 665 O HOH D 697 2.05
REMARK 500 O HOH A 647 O HOH A 666 2.07
REMARK 500 O HOH C 508 O HOH C 627 2.08
REMARK 500 O GLY D 127 NH1 ARG D 159 2.08
REMARK 500 NH2 ARG C 55 O HOH C 502 2.09
REMARK 500 O HOH C 562 O HOH C 636 2.09
REMARK 500 O HOH C 543 O HOH C 560 2.10
REMARK 500 O4 TLA D 401 O HOH D 502 2.10
REMARK 500 O HOH A 572 O HOH A 603 2.11
REMARK 500 O HOH D 677 O HOH D 705 2.12
REMARK 500 NZ LYS C 237 O HOH C 503 2.13
REMARK 500 ND2 ASN A 49 OD2 ASP A 52 2.13
REMARK 500 SG CYS A 250 O HOH A 519 2.13
REMARK 500 O HOH A 566 O HOH A 614 2.14
REMARK 500 O HOH C 632 O HOH C 653 2.14
REMARK 500 O CYS A 250 O HOH A 501 2.14
REMARK 500 O HOH B 636 O HOH B 670 2.14
REMARK 500 O HOH C 525 O HOH C 600 2.15
REMARK 500 O HOH D 684 O HOH D 687 2.15
REMARK 500 O HOH C 657 O HOH C 672 2.15
REMARK 500 N LYS B 327 O HOH B 504 2.15
REMARK 500 OE2 GLU C 43 O HOH C 504 2.16
REMARK 500 O HOH A 575 O HOH A 655 2.16
REMARK 500 O ASP A 326 O HOH A 502 2.16
REMARK 500 NE2 GLN A 87 O HOH A 503 2.16
REMARK 500 O PRO A 95 O HOH A 504 2.16
REMARK 500 O HOH B 609 O HOH B 634 2.16
REMARK 500 NH2 ARG D 84 O HOH D 503 2.16
REMARK 500 SG CYS B 250 O HOH B 526 2.16
REMARK 500 O HOH A 504 O HOH A 537 2.17
REMARK 500 O ASN D 117 O HOH D 504 2.18
REMARK 500 O HOH A 546 O HOH A 614 2.18
REMARK 500 OE1 GLU C 73 O HOH C 505 2.19
REMARK 500
REMARK 500 THIS ENTRY HAS 54 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CB GLU D 43 O HOH B 512 1554 1.92
REMARK 500 OE2 GLU C 150 NH1 ARG C 161 3556 2.15
REMARK 500 O HOH D 692 O HOH D 692 4555 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 B 74 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG C 74 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 PRO C 281 C - N - CA ANGL. DEV. = 11.2 DEGREES
REMARK 500 PRO C 281 C - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG D 41 NE - CZ - NH1 ANGL. DEV. = 3.2 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 TYR A 16 -55.25 -140.69
REMARK 500 ARG A 47 -82.20 -155.68
REMARK 500 HIS A 61 53.43 -148.07
REMARK 500 CYS A 124 -105.38 -129.29
REMARK 500 LYS A 125 -79.89 -93.77
REMARK 500 LYS A 128 -92.27 -116.09
REMARK 500 LEU A 220 -135.17 59.01
REMARK 500 ASP A 236 -108.80 60.41
REMARK 500 ASN A 262 -0.73 71.50
REMARK 500 MET A 270 -63.73 -94.49
REMARK 500 ASN A 340 -2.96 76.68
REMARK 500 TYR B 16 -52.63 -142.50
REMARK 500 PHE B 21 12.37 -144.77
REMARK 500 ASP B 22 93.62 -10.32
REMARK 500 HIS B 61 53.53 -147.83
REMARK 500 PHE B 81 31.11 -96.40
REMARK 500 ASN B 82 29.85 49.46
REMARK 500 CYS B 124 -105.68 -129.03
REMARK 500 LYS B 125 -80.22 -94.77
REMARK 500 LYS B 128 -92.79 -115.30
REMARK 500 LEU B 220 -136.07 58.89
REMARK 500 SER B 229 133.61 -38.38
REMARK 500 ASP B 236 -110.48 60.33
REMARK 500 MET B 270 -63.78 -93.25
REMARK 500 ASN B 340 -8.34 79.97
REMARK 500 GLU C 43 -106.58 -85.34
REMARK 500 VAL C 45 7.82 -30.22
REMARK 500 HIS C 61 53.48 -148.41
REMARK 500 PHE C 81 31.43 -96.66
REMARK 500 CYS C 124 -105.13 -128.25
REMARK 500 LYS C 125 -79.12 -95.27
REMARK 500 LYS C 128 -92.47 -115.76
REMARK 500 LEU C 220 -136.26 58.78
REMARK 500 ASP C 236 -106.96 62.73
REMARK 500 ASN C 262 -7.65 73.13
REMARK 500 LEU C 265 -122.36 58.72
REMARK 500 MET C 270 -63.35 -94.48
REMARK 500 GLU C 284 116.58 32.11
REMARK 500 ASN C 340 -2.71 76.93
REMARK 500 LEU D 42 -115.98 58.77
REMARK 500 TYR D 46 114.61 78.30
REMARK 500 HIS D 61 53.65 -148.03
REMARK 500 PHE D 81 31.06 -96.14
REMARK 500 ASN D 82 29.93 49.25
REMARK 500 CYS D 124 -105.10 -129.31
REMARK 500 LYS D 125 -79.66 -95.29
REMARK 500 LYS D 128 -92.83 -115.78
REMARK 500 LEU D 220 -136.11 59.74
REMARK 500 ASP D 236 -111.55 61.77
REMARK 500 MET D 270 -63.33 -93.14
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 19 GLY A 20 129.48
REMARK 500 GLU A 40 ARG A 41 133.74
REMARK 500 ARG A 41 LEU A 42 -143.07
REMARK 500 LEU A 42 GLU A 43 133.79
REMARK 500 HIS A 123 CYS A 124 142.17
REMARK 500 MET A 264 LEU A 265 -122.87
REMARK 500 LEU A 265 LYS A 266 -146.68
REMARK 500 ILE A 280 PRO A 281 49.73
REMARK 500 GLY A 282 PRO A 283 -118.76
REMARK 500 GLU A 285 ASP A 310 -138.05
REMARK 500 ASP A 312 LYS A 313 -79.36
REMARK 500 LYS A 313 GLU A 314 146.66
REMARK 500 ASP B 19 GLY B 20 129.19
REMARK 500 GLY B 20 PHE B 21 -134.06
REMARK 500 PHE B 21 ASP B 22 -132.13
REMARK 500 HIS B 123 CYS B 124 142.59
REMARK 500 ILE B 280 PRO B 281 -76.07
REMARK 500 GLU B 284 GLU B 285 -122.52
REMARK 500 ASN B 311 ASP B 312 -147.38
REMARK 500 ASP C 19 GLY C 20 129.10
REMARK 500 ARG C 41 LEU C 42 -149.49
REMARK 500 LEU C 42 GLU C 43 -142.16
REMARK 500 GLY C 44 VAL C 45 -115.17
REMARK 500 TYR C 46 ARG C 47 -147.14
REMARK 500 HIS C 123 CYS C 124 141.88
REMARK 500 ILE C 280 PRO C 281 -109.18
REMARK 500 GLY C 282 PRO C 283 -147.09
REMARK 500 PRO C 283 GLU C 284 144.92
REMARK 500 ASP C 310 ASN C 311 -113.59
REMARK 500 ASP C 312 LYS C 313 -128.43
REMARK 500 ASP D 19 GLY D 20 129.08
REMARK 500 HIS D 123 CYS D 124 141.85
REMARK 500 LYS D 263 MET D 264 141.46
REMARK 500 PRO D 281 GLY D 282 113.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ILE A 280 11.52
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 A 678 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 679 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 680 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 681 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 682 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 683 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A 684 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 685 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A 686 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH A 687 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH A 688 DISTANCE = 7.38 ANGSTROMS
REMARK 525 HOH A 689 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH A 690 DISTANCE = 7.67 ANGSTROMS
REMARK 525 HOH A 691 DISTANCE = 7.74 ANGSTROMS
REMARK 525 HOH A 692 DISTANCE = 8.47 ANGSTROMS
REMARK 525 HOH A 693 DISTANCE = 8.65 ANGSTROMS
REMARK 525 HOH A 694 DISTANCE = 8.73 ANGSTROMS
REMARK 525 HOH A 695 DISTANCE = 8.99 ANGSTROMS
REMARK 525 HOH A 696 DISTANCE = 10.00 ANGSTROMS
REMARK 525 HOH A 697 DISTANCE = 10.21 ANGSTROMS
REMARK 525 HOH A 698 DISTANCE = 10.21 ANGSTROMS
REMARK 525 HOH A 699 DISTANCE = 10.45 ANGSTROMS
REMARK 525 HOH A 700 DISTANCE = 10.56 ANGSTROMS
REMARK 525 HOH A 701 DISTANCE = 10.99 ANGSTROMS
REMARK 525 HOH A 702 DISTANCE = 12.50 ANGSTROMS
REMARK 525 HOH A 703 DISTANCE = 12.51 ANGSTROMS
REMARK 525 HOH B 684 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 685 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 686 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B 687 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 688 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B 689 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B 690 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH B 691 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH B 692 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH B 693 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH B 694 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH B 695 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH B 696 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH B 697 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH B 698 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH B 699 DISTANCE = 7.66 ANGSTROMS
REMARK 525 HOH B 700 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH B 701 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH B 702 DISTANCE = 7.91 ANGSTROMS
REMARK 525 HOH B 703 DISTANCE = 8.53 ANGSTROMS
REMARK 525 HOH B 704 DISTANCE = 8.59 ANGSTROMS
REMARK 525 HOH B 705 DISTANCE = 8.83 ANGSTROMS
REMARK 525 HOH B 706 DISTANCE = 8.84 ANGSTROMS
REMARK 525 HOH B 707 DISTANCE = 8.90 ANGSTROMS
REMARK 525 HOH B 708 DISTANCE = 9.10 ANGSTROMS
REMARK 525 HOH B 709 DISTANCE = 9.90 ANGSTROMS
REMARK 525 HOH B 710 DISTANCE = 10.24 ANGSTROMS
REMARK 525 HOH B 711 DISTANCE = 10.79 ANGSTROMS
REMARK 525 HOH B 712 DISTANCE = 11.12 ANGSTROMS
REMARK 525 HOH B 713 DISTANCE = 11.15 ANGSTROMS
REMARK 525 HOH B 714 DISTANCE = 11.34 ANGSTROMS
REMARK 525 HOH B 715 DISTANCE = 11.69 ANGSTROMS
REMARK 525 HOH B 716 DISTANCE = 11.85 ANGSTROMS
REMARK 525 HOH B 717 DISTANCE = 12.94 ANGSTROMS
REMARK 525 HOH B 718 DISTANCE = 13.28 ANGSTROMS
REMARK 525 HOH B 719 DISTANCE = 13.36 ANGSTROMS
REMARK 525 HOH B 720 DISTANCE = 13.96 ANGSTROMS
REMARK 525 HOH B 721 DISTANCE = 16.18 ANGSTROMS
REMARK 525 HOH B 722 DISTANCE = 16.50 ANGSTROMS
REMARK 525 HOH B 723 DISTANCE = 18.02 ANGSTROMS
REMARK 525 HOH B 724 DISTANCE = 20.37 ANGSTROMS
REMARK 525 HOH C 689 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH C 690 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH C 691 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH C 692 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH C 693 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH C 694 DISTANCE = 7.21 ANGSTROMS
REMARK 525 HOH C 695 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH C 696 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH C 697 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH C 698 DISTANCE = 8.24 ANGSTROMS
REMARK 525 HOH C 699 DISTANCE = 8.24 ANGSTROMS
REMARK 525 HOH C 700 DISTANCE = 8.51 ANGSTROMS
REMARK 525 HOH C 701 DISTANCE = 9.06 ANGSTROMS
REMARK 525 HOH C 702 DISTANCE = 9.33 ANGSTROMS
REMARK 525 HOH C 703 DISTANCE = 11.30 ANGSTROMS
REMARK 525 HOH C 704 DISTANCE = 11.57 ANGSTROMS
REMARK 525 HOH C 705 DISTANCE = 12.43 ANGSTROMS
REMARK 525 HOH C 706 DISTANCE = 13.11 ANGSTROMS
REMARK 525 HOH C 707 DISTANCE = 15.47 ANGSTROMS
REMARK 525 HOH C 708 DISTANCE = 16.40 ANGSTROMS
REMARK 525 HOH C 709 DISTANCE = 19.63 ANGSTROMS
REMARK 525 HOH D 717 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH D 718 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH D 719 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH D 720 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH D 721 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH D 722 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH D 723 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH D 724 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH D 725 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH D 726 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH D 727 DISTANCE = 7.70 ANGSTROMS
REMARK 525 HOH D 728 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH D 729 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH D 730 DISTANCE = 8.31 ANGSTROMS
REMARK 525 HOH D 731 DISTANCE = 8.40 ANGSTROMS
REMARK 525 HOH D 732 DISTANCE = 8.55 ANGSTROMS
REMARK 525 HOH D 733 DISTANCE = 8.74 ANGSTROMS
REMARK 525 HOH D 734 DISTANCE = 8.88 ANGSTROMS
REMARK 525 HOH D 735 DISTANCE = 9.05 ANGSTROMS
REMARK 525 HOH D 736 DISTANCE = 9.18 ANGSTROMS
REMARK 525 HOH D 737 DISTANCE = 9.28 ANGSTROMS
REMARK 525 HOH D 738 DISTANCE = 9.69 ANGSTROMS
REMARK 525 HOH D 739 DISTANCE = 10.18 ANGSTROMS
REMARK 525 HOH D 740 DISTANCE = 10.54 ANGSTROMS
REMARK 525 HOH D 741 DISTANCE = 10.84 ANGSTROMS
REMARK 525 HOH D 742 DISTANCE = 11.31 ANGSTROMS
REMARK 525 HOH D 743 DISTANCE = 12.90 ANGSTROMS
REMARK 525 HOH D 744 DISTANCE = 13.43 ANGSTROMS
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 VO4 C 402 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TLA C 401 O2
REMARK 620 2 VO4 C 402 O1 68.0
REMARK 620 3 VO4 C 402 O2 98.7 111.2
REMARK 620 4 VO4 C 402 O3 48.2 107.9 108.3
REMARK 620 5 VO4 C 402 O4 149.8 110.1 109.3 110.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TLA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TLA D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues TLA C 401 and VO4 C
REMARK 800 402
DBREF 5BZX A 14 351 UNP P60484 PTEN_HUMAN 14 351
DBREF 5BZX B 14 351 UNP P60484 PTEN_HUMAN 14 351
DBREF 5BZX C 14 351 UNP P60484 PTEN_HUMAN 14 351
DBREF 5BZX D 14 351 UNP P60484 PTEN_HUMAN 14 351
SEQADV 5BZX A UNP P60484 THR 286 DELETION
SEQADV 5BZX A UNP P60484 SER 287 DELETION
SEQADV 5BZX A UNP P60484 GLU 288 DELETION
SEQADV 5BZX A UNP P60484 LYS 289 DELETION
SEQADV 5BZX A UNP P60484 VAL 290 DELETION
SEQADV 5BZX A UNP P60484 GLU 291 DELETION
SEQADV 5BZX A UNP P60484 ASN 292 DELETION
SEQADV 5BZX A UNP P60484 GLY 293 DELETION
SEQADV 5BZX A UNP P60484 SER 294 DELETION
SEQADV 5BZX A UNP P60484 LEU 295 DELETION
SEQADV 5BZX A UNP P60484 CYS 296 DELETION
SEQADV 5BZX A UNP P60484 ASP 297 DELETION
SEQADV 5BZX A UNP P60484 GLN 298 DELETION
SEQADV 5BZX A UNP P60484 GLU 299 DELETION
SEQADV 5BZX A UNP P60484 ILE 300 DELETION
SEQADV 5BZX A UNP P60484 ASP 301 DELETION
SEQADV 5BZX A UNP P60484 SER 302 DELETION
SEQADV 5BZX A UNP P60484 ILE 303 DELETION
SEQADV 5BZX A UNP P60484 CYS 304 DELETION
SEQADV 5BZX A UNP P60484 SER 305 DELETION
SEQADV 5BZX A UNP P60484 ILE 306 DELETION
SEQADV 5BZX A UNP P60484 GLU 307 DELETION
SEQADV 5BZX A UNP P60484 ARG 308 DELETION
SEQADV 5BZX A UNP P60484 ALA 309 DELETION
SEQADV 5BZX B UNP P60484 THR 286 DELETION
SEQADV 5BZX B UNP P60484 SER 287 DELETION
SEQADV 5BZX B UNP P60484 GLU 288 DELETION
SEQADV 5BZX B UNP P60484 LYS 289 DELETION
SEQADV 5BZX B UNP P60484 VAL 290 DELETION
SEQADV 5BZX B UNP P60484 GLU 291 DELETION
SEQADV 5BZX B UNP P60484 ASN 292 DELETION
SEQADV 5BZX B UNP P60484 GLY 293 DELETION
SEQADV 5BZX B UNP P60484 SER 294 DELETION
SEQADV 5BZX B UNP P60484 LEU 295 DELETION
SEQADV 5BZX B UNP P60484 CYS 296 DELETION
SEQADV 5BZX B UNP P60484 ASP 297 DELETION
SEQADV 5BZX B UNP P60484 GLN 298 DELETION
SEQADV 5BZX B UNP P60484 GLU 299 DELETION
SEQADV 5BZX B UNP P60484 ILE 300 DELETION
SEQADV 5BZX B UNP P60484 ASP 301 DELETION
SEQADV 5BZX B UNP P60484 SER 302 DELETION
SEQADV 5BZX B UNP P60484 ILE 303 DELETION
SEQADV 5BZX B UNP P60484 CYS 304 DELETION
SEQADV 5BZX B UNP P60484 SER 305 DELETION
SEQADV 5BZX B UNP P60484 ILE 306 DELETION
SEQADV 5BZX B UNP P60484 GLU 307 DELETION
SEQADV 5BZX B UNP P60484 ARG 308 DELETION
SEQADV 5BZX B UNP P60484 ALA 309 DELETION
SEQADV 5BZX C UNP P60484 THR 286 DELETION
SEQADV 5BZX C UNP P60484 SER 287 DELETION
SEQADV 5BZX C UNP P60484 GLU 288 DELETION
SEQADV 5BZX C UNP P60484 LYS 289 DELETION
SEQADV 5BZX C UNP P60484 VAL 290 DELETION
SEQADV 5BZX C UNP P60484 GLU 291 DELETION
SEQADV 5BZX C UNP P60484 ASN 292 DELETION
SEQADV 5BZX C UNP P60484 GLY 293 DELETION
SEQADV 5BZX C UNP P60484 SER 294 DELETION
SEQADV 5BZX C UNP P60484 LEU 295 DELETION
SEQADV 5BZX C UNP P60484 CYS 296 DELETION
SEQADV 5BZX C UNP P60484 ASP 297 DELETION
SEQADV 5BZX C UNP P60484 GLN 298 DELETION
SEQADV 5BZX C UNP P60484 GLU 299 DELETION
SEQADV 5BZX C UNP P60484 ILE 300 DELETION
SEQADV 5BZX C UNP P60484 ASP 301 DELETION
SEQADV 5BZX C UNP P60484 SER 302 DELETION
SEQADV 5BZX C UNP P60484 ILE 303 DELETION
SEQADV 5BZX C UNP P60484 CYS 304 DELETION
SEQADV 5BZX C UNP P60484 SER 305 DELETION
SEQADV 5BZX C UNP P60484 ILE 306 DELETION
SEQADV 5BZX C UNP P60484 GLU 307 DELETION
SEQADV 5BZX C UNP P60484 ARG 308 DELETION
SEQADV 5BZX C UNP P60484 ALA 309 DELETION
SEQADV 5BZX D UNP P60484 THR 286 DELETION
SEQADV 5BZX D UNP P60484 SER 287 DELETION
SEQADV 5BZX D UNP P60484 GLU 288 DELETION
SEQADV 5BZX D UNP P60484 LYS 289 DELETION
SEQADV 5BZX D UNP P60484 VAL 290 DELETION
SEQADV 5BZX D UNP P60484 GLU 291 DELETION
SEQADV 5BZX D UNP P60484 ASN 292 DELETION
SEQADV 5BZX D UNP P60484 GLY 293 DELETION
SEQADV 5BZX D UNP P60484 SER 294 DELETION
SEQADV 5BZX D UNP P60484 LEU 295 DELETION
SEQADV 5BZX D UNP P60484 CYS 296 DELETION
SEQADV 5BZX D UNP P60484 ASP 297 DELETION
SEQADV 5BZX D UNP P60484 GLN 298 DELETION
SEQADV 5BZX D UNP P60484 GLU 299 DELETION
SEQADV 5BZX D UNP P60484 ILE 300 DELETION
SEQADV 5BZX D UNP P60484 ASP 301 DELETION
SEQADV 5BZX D UNP P60484 SER 302 DELETION
SEQADV 5BZX D UNP P60484 ILE 303 DELETION
SEQADV 5BZX D UNP P60484 CYS 304 DELETION
SEQADV 5BZX D UNP P60484 SER 305 DELETION
SEQADV 5BZX D UNP P60484 ILE 306 DELETION
SEQADV 5BZX D UNP P60484 GLU 307 DELETION
SEQADV 5BZX D UNP P60484 ARG 308 DELETION
SEQADV 5BZX D UNP P60484 ALA 309 DELETION
SEQRES 1 A 314 ARG ARG TYR GLN GLU ASP GLY PHE ASP LEU ASP LEU THR
SEQRES 2 A 314 TYR ILE TYR PRO ASN ILE ILE ALA MET GLY PHE PRO ALA
SEQRES 3 A 314 GLU ARG LEU GLU GLY VAL TYR ARG ASN ASN ILE ASP ASP
SEQRES 4 A 314 VAL VAL ARG PHE LEU ASP SER LYS HIS LYS ASN HIS TYR
SEQRES 5 A 314 LYS ILE TYR ASN LEU CYS ALA GLU ARG HIS TYR ASP THR
SEQRES 6 A 314 ALA LYS PHE ASN CYS ARG VAL ALA GLN TYR PRO PHE GLU
SEQRES 7 A 314 ASP HIS ASN PRO PRO GLN LEU GLU LEU ILE LYS PRO PHE
SEQRES 8 A 314 CYS GLU ASP LEU ASP GLN TRP LEU SER GLU ASP ASP ASN
SEQRES 9 A 314 HIS VAL ALA ALA ILE HIS CYS LYS ALA GLY LYS GLY ARG
SEQRES 10 A 314 THR GLY VAL MET ILE CYS ALA TYR LEU LEU HIS ARG GLY
SEQRES 11 A 314 LYS PHE LEU LYS ALA GLN GLU ALA LEU ASP PHE TYR GLY
SEQRES 12 A 314 GLU VAL ARG THR ARG ASP LYS LYS GLY VAL THR ILE PRO
SEQRES 13 A 314 SER GLN ARG ARG TYR VAL TYR TYR TYR SER TYR LEU LEU
SEQRES 14 A 314 LYS ASN HIS LEU ASP TYR ARG PRO VAL ALA LEU LEU PHE
SEQRES 15 A 314 HIS LYS MET MET PHE GLU THR ILE PRO MET PHE SER GLY
SEQRES 16 A 314 GLY THR CYS ASN PRO GLN PHE VAL VAL CYS GLN LEU LYS
SEQRES 17 A 314 VAL LYS ILE TYR SER SER ASN SER GLY PRO THR ARG ARG
SEQRES 18 A 314 GLU ASP LYS PHE MET TYR PHE GLU PHE PRO GLN PRO LEU
SEQRES 19 A 314 PRO VAL CYS GLY ASP ILE LYS VAL GLU PHE PHE HIS LYS
SEQRES 20 A 314 GLN ASN LYS MET LEU LYS LYS ASP LYS MET PHE HIS PHE
SEQRES 21 A 314 TRP VAL ASN THR PHE PHE ILE PRO GLY PRO GLU GLU ASP
SEQRES 22 A 314 ASN ASP LYS GLU TYR LEU VAL LEU THR LEU THR LYS ASN
SEQRES 23 A 314 ASP LEU ASP LYS ALA ASN LYS ASP LYS ALA ASN ARG TYR
SEQRES 24 A 314 PHE SER PRO ASN PHE LYS VAL LYS LEU TYR PHE THR LYS
SEQRES 25 A 314 THR VAL
SEQRES 1 B 314 ARG ARG TYR GLN GLU ASP GLY PHE ASP LEU ASP LEU THR
SEQRES 2 B 314 TYR ILE TYR PRO ASN ILE ILE ALA MET GLY PHE PRO ALA
SEQRES 3 B 314 GLU ARG LEU GLU GLY VAL TYR ARG ASN ASN ILE ASP ASP
SEQRES 4 B 314 VAL VAL ARG PHE LEU ASP SER LYS HIS LYS ASN HIS TYR
SEQRES 5 B 314 LYS ILE TYR ASN LEU CYS ALA GLU ARG HIS TYR ASP THR
SEQRES 6 B 314 ALA LYS PHE ASN CYS ARG VAL ALA GLN TYR PRO PHE GLU
SEQRES 7 B 314 ASP HIS ASN PRO PRO GLN LEU GLU LEU ILE LYS PRO PHE
SEQRES 8 B 314 CYS GLU ASP LEU ASP GLN TRP LEU SER GLU ASP ASP ASN
SEQRES 9 B 314 HIS VAL ALA ALA ILE HIS CYS LYS ALA GLY LYS GLY ARG
SEQRES 10 B 314 THR GLY VAL MET ILE CYS ALA TYR LEU LEU HIS ARG GLY
SEQRES 11 B 314 LYS PHE LEU LYS ALA GLN GLU ALA LEU ASP PHE TYR GLY
SEQRES 12 B 314 GLU VAL ARG THR ARG ASP LYS LYS GLY VAL THR ILE PRO
SEQRES 13 B 314 SER GLN ARG ARG TYR VAL TYR TYR TYR SER TYR LEU LEU
SEQRES 14 B 314 LYS ASN HIS LEU ASP TYR ARG PRO VAL ALA LEU LEU PHE
SEQRES 15 B 314 HIS LYS MET MET PHE GLU THR ILE PRO MET PHE SER GLY
SEQRES 16 B 314 GLY THR CYS ASN PRO GLN PHE VAL VAL CYS GLN LEU LYS
SEQRES 17 B 314 VAL LYS ILE TYR SER SER ASN SER GLY PRO THR ARG ARG
SEQRES 18 B 314 GLU ASP LYS PHE MET TYR PHE GLU PHE PRO GLN PRO LEU
SEQRES 19 B 314 PRO VAL CYS GLY ASP ILE LYS VAL GLU PHE PHE HIS LYS
SEQRES 20 B 314 GLN ASN LYS MET LEU LYS LYS ASP LYS MET PHE HIS PHE
SEQRES 21 B 314 TRP VAL ASN THR PHE PHE ILE PRO GLY PRO GLU GLU ASP
SEQRES 22 B 314 ASN ASP LYS GLU TYR LEU VAL LEU THR LEU THR LYS ASN
SEQRES 23 B 314 ASP LEU ASP LYS ALA ASN LYS ASP LYS ALA ASN ARG TYR
SEQRES 24 B 314 PHE SER PRO ASN PHE LYS VAL LYS LEU TYR PHE THR LYS
SEQRES 25 B 314 THR VAL
SEQRES 1 C 314 ARG ARG TYR GLN GLU ASP GLY PHE ASP LEU ASP LEU THR
SEQRES 2 C 314 TYR ILE TYR PRO ASN ILE ILE ALA MET GLY PHE PRO ALA
SEQRES 3 C 314 GLU ARG LEU GLU GLY VAL TYR ARG ASN ASN ILE ASP ASP
SEQRES 4 C 314 VAL VAL ARG PHE LEU ASP SER LYS HIS LYS ASN HIS TYR
SEQRES 5 C 314 LYS ILE TYR ASN LEU CYS ALA GLU ARG HIS TYR ASP THR
SEQRES 6 C 314 ALA LYS PHE ASN CYS ARG VAL ALA GLN TYR PRO PHE GLU
SEQRES 7 C 314 ASP HIS ASN PRO PRO GLN LEU GLU LEU ILE LYS PRO PHE
SEQRES 8 C 314 CYS GLU ASP LEU ASP GLN TRP LEU SER GLU ASP ASP ASN
SEQRES 9 C 314 HIS VAL ALA ALA ILE HIS CYS LYS ALA GLY LYS GLY ARG
SEQRES 10 C 314 THR GLY VAL MET ILE CYS ALA TYR LEU LEU HIS ARG GLY
SEQRES 11 C 314 LYS PHE LEU LYS ALA GLN GLU ALA LEU ASP PHE TYR GLY
SEQRES 12 C 314 GLU VAL ARG THR ARG ASP LYS LYS GLY VAL THR ILE PRO
SEQRES 13 C 314 SER GLN ARG ARG TYR VAL TYR TYR TYR SER TYR LEU LEU
SEQRES 14 C 314 LYS ASN HIS LEU ASP TYR ARG PRO VAL ALA LEU LEU PHE
SEQRES 15 C 314 HIS LYS MET MET PHE GLU THR ILE PRO MET PHE SER GLY
SEQRES 16 C 314 GLY THR CYS ASN PRO GLN PHE VAL VAL CYS GLN LEU LYS
SEQRES 17 C 314 VAL LYS ILE TYR SER SER ASN SER GLY PRO THR ARG ARG
SEQRES 18 C 314 GLU ASP LYS PHE MET TYR PHE GLU PHE PRO GLN PRO LEU
SEQRES 19 C 314 PRO VAL CYS GLY ASP ILE LYS VAL GLU PHE PHE HIS LYS
SEQRES 20 C 314 GLN ASN LYS MET LEU LYS LYS ASP LYS MET PHE HIS PHE
SEQRES 21 C 314 TRP VAL ASN THR PHE PHE ILE PRO GLY PRO GLU GLU ASP
SEQRES 22 C 314 ASN ASP LYS GLU TYR LEU VAL LEU THR LEU THR LYS ASN
SEQRES 23 C 314 ASP LEU ASP LYS ALA ASN LYS ASP LYS ALA ASN ARG TYR
SEQRES 24 C 314 PHE SER PRO ASN PHE LYS VAL LYS LEU TYR PHE THR LYS
SEQRES 25 C 314 THR VAL
SEQRES 1 D 314 ARG ARG TYR GLN GLU ASP GLY PHE ASP LEU ASP LEU THR
SEQRES 2 D 314 TYR ILE TYR PRO ASN ILE ILE ALA MET GLY PHE PRO ALA
SEQRES 3 D 314 GLU ARG LEU GLU GLY VAL TYR ARG ASN ASN ILE ASP ASP
SEQRES 4 D 314 VAL VAL ARG PHE LEU ASP SER LYS HIS LYS ASN HIS TYR
SEQRES 5 D 314 LYS ILE TYR ASN LEU CYS ALA GLU ARG HIS TYR ASP THR
SEQRES 6 D 314 ALA LYS PHE ASN CYS ARG VAL ALA GLN TYR PRO PHE GLU
SEQRES 7 D 314 ASP HIS ASN PRO PRO GLN LEU GLU LEU ILE LYS PRO PHE
SEQRES 8 D 314 CYS GLU ASP LEU ASP GLN TRP LEU SER GLU ASP ASP ASN
SEQRES 9 D 314 HIS VAL ALA ALA ILE HIS CYS LYS ALA GLY LYS GLY ARG
SEQRES 10 D 314 THR GLY VAL MET ILE CYS ALA TYR LEU LEU HIS ARG GLY
SEQRES 11 D 314 LYS PHE LEU LYS ALA GLN GLU ALA LEU ASP PHE TYR GLY
SEQRES 12 D 314 GLU VAL ARG THR ARG ASP LYS LYS GLY VAL THR ILE PRO
SEQRES 13 D 314 SER GLN ARG ARG TYR VAL TYR TYR TYR SER TYR LEU LEU
SEQRES 14 D 314 LYS ASN HIS LEU ASP TYR ARG PRO VAL ALA LEU LEU PHE
SEQRES 15 D 314 HIS LYS MET MET PHE GLU THR ILE PRO MET PHE SER GLY
SEQRES 16 D 314 GLY THR CYS ASN PRO GLN PHE VAL VAL CYS GLN LEU LYS
SEQRES 17 D 314 VAL LYS ILE TYR SER SER ASN SER GLY PRO THR ARG ARG
SEQRES 18 D 314 GLU ASP LYS PHE MET TYR PHE GLU PHE PRO GLN PRO LEU
SEQRES 19 D 314 PRO VAL CYS GLY ASP ILE LYS VAL GLU PHE PHE HIS LYS
SEQRES 20 D 314 GLN ASN LYS MET LEU LYS LYS ASP LYS MET PHE HIS PHE
SEQRES 21 D 314 TRP VAL ASN THR PHE PHE ILE PRO GLY PRO GLU GLU ASP
SEQRES 22 D 314 ASN ASP LYS GLU TYR LEU VAL LEU THR LEU THR LYS ASN
SEQRES 23 D 314 ASP LEU ASP LYS ALA ASN LYS ASP LYS ALA ASN ARG TYR
SEQRES 24 D 314 PHE SER PRO ASN PHE LYS VAL LYS LEU TYR PHE THR LYS
SEQRES 25 D 314 THR VAL
HET VO4 A 401 5
HET TLA B 401 10
HET TLA C 401 10
HET VO4 C 402 5
HET TLA D 401 10
HETNAM VO4 VANADATE ION
HETNAM TLA L(+)-TARTARIC ACID
FORMUL 5 VO4 2(O4 V 3-)
FORMUL 6 TLA 3(C4 H6 O6)
FORMUL 10 HOH *880(H2 O)
HELIX 1 AA1 ASN A 49 LYS A 62 1 14
HELIX 2 AA2 ASP A 77 ASN A 82 5 6
HELIX 3 AA3 GLN A 97 GLU A 99 5 3
HELIX 4 AA4 LEU A 100 ASP A 115 1 16
HELIX 5 AA5 LYS A 128 ARG A 142 1 15
HELIX 6 AA6 LYS A 147 THR A 160 1 14
HELIX 7 AA7 ILE A 168 ASN A 184 1 17
HELIX 8 AA8 PHE A 278 ILE A 280 5 3
HELIX 9 AA9 ASN A 323 LEU A 325 5 3
HELIX 10 AB1 LYS A 327 ASP A 331 5 5
HELIX 11 AB2 ILE B 50 LYS B 62 1 13
HELIX 12 AB3 ASP B 77 ASN B 82 5 6
HELIX 13 AB4 GLN B 97 GLU B 99 5 3
HELIX 14 AB5 LEU B 100 ASP B 115 1 16
HELIX 15 AB6 LYS B 128 ARG B 142 1 15
HELIX 16 AB7 LYS B 147 THR B 160 1 14
HELIX 17 AB8 ILE B 168 ASN B 184 1 17
HELIX 18 AB9 PHE B 278 ILE B 280 5 3
HELIX 19 AC1 ASN B 323 LEU B 325 5 3
HELIX 20 AC2 LYS B 327 ASP B 331 5 5
HELIX 21 AC3 ASN C 49 LYS C 62 1 14
HELIX 22 AC4 ASP C 77 ASN C 82 5 6
HELIX 23 AC5 GLN C 97 GLU C 99 5 3
HELIX 24 AC6 LEU C 100 ASP C 115 1 16
HELIX 25 AC7 LYS C 128 ARG C 142 1 15
HELIX 26 AC8 LYS C 147 THR C 160 1 14
HELIX 27 AC9 ILE C 168 ASN C 184 1 17
HELIX 28 AD1 PHE C 278 ILE C 280 5 3
HELIX 29 AD2 ASN C 323 LEU C 325 5 3
HELIX 30 AD3 LYS C 327 ASP C 331 5 5
HELIX 31 AD4 ASN D 49 LYS D 62 1 14
HELIX 32 AD5 ASP D 77 ASN D 82 5 6
HELIX 33 AD6 GLN D 97 GLU D 99 5 3
HELIX 34 AD7 LEU D 100 ASP D 115 1 16
HELIX 35 AD8 LYS D 128 ARG D 142 1 15
HELIX 36 AD9 LYS D 147 THR D 160 1 14
HELIX 37 AE1 ILE D 168 ASN D 184 1 17
HELIX 38 AE2 PHE D 278 ILE D 280 5 3
HELIX 39 AE3 ASN D 323 LEU D 325 5 3
HELIX 40 AE4 LYS D 327 ASP D 331 5 5
SHEET 1 AA1 5 LEU A 25 TYR A 29 0
SHEET 2 AA1 5 ILE A 32 MET A 35 -1 O ALA A 34 N THR A 26
SHEET 3 AA1 5 VAL A 119 HIS A 123 1 O ALA A 120 N ILE A 33
SHEET 4 AA1 5 TYR A 65 ASN A 69 1 N LYS A 66 O ALA A 121
SHEET 5 AA1 5 VAL A 85 GLN A 87 1 O ALA A 86 N ASN A 69
SHEET 1 AA2 5 ARG A 233 GLU A 235 0
SHEET 2 AA2 5 PHE A 238 CYS A 250 -1 O TYR A 240 N ARG A 233
SHEET 3 AA2 5 ALA A 192 PHE A 200 -1 N PHE A 195 O LEU A 247
SHEET 4 AA2 5 LYS A 342 LYS A 349 -1 O THR A 348 N LEU A 194
SHEET 5 AA2 5 LEU A 316 THR A 321 -1 N LEU A 316 O PHE A 347
SHEET 1 AA3 4 VAL A 222 SER A 226 0
SHEET 2 AA3 4 PRO A 213 GLN A 219 -1 N GLN A 219 O VAL A 222
SHEET 3 AA3 4 ASP A 252 HIS A 259 -1 O PHE A 258 N GLN A 214
SHEET 4 AA3 4 ASP A 268 ASN A 276 -1 O PHE A 271 N PHE A 257
SHEET 1 AA4 5 LEU B 25 TYR B 29 0
SHEET 2 AA4 5 ILE B 32 MET B 35 -1 O ALA B 34 N THR B 26
SHEET 3 AA4 5 VAL B 119 HIS B 123 1 O ALA B 120 N ILE B 33
SHEET 4 AA4 5 TYR B 65 ASN B 69 1 N LYS B 66 O ALA B 121
SHEET 5 AA4 5 VAL B 85 GLN B 87 1 O ALA B 86 N ASN B 69
SHEET 1 AA5 2 PRO B 38 ALA B 39 0
SHEET 2 AA5 2 ASN B 48 ASN B 49 1 O ASN B 48 N ALA B 39
SHEET 1 AA6 5 ARG B 233 GLU B 235 0
SHEET 2 AA6 5 PHE B 238 CYS B 250 -1 O TYR B 240 N ARG B 233
SHEET 3 AA6 5 ALA B 192 PHE B 200 -1 N PHE B 195 O LEU B 247
SHEET 4 AA6 5 LYS B 342 LYS B 349 -1 O THR B 348 N LEU B 194
SHEET 5 AA6 5 LEU B 316 THR B 321 -1 N LEU B 316 O PHE B 347
SHEET 1 AA7 4 VAL B 222 SER B 226 0
SHEET 2 AA7 4 PRO B 213 GLN B 219 -1 N GLN B 219 O VAL B 222
SHEET 3 AA7 4 ASP B 252 GLN B 261 -1 O PHE B 258 N GLN B 214
SHEET 4 AA7 4 MET B 264 ASN B 276 -1 O MET B 264 N GLN B 261
SHEET 1 AA8 5 LEU C 25 TYR C 29 0
SHEET 2 AA8 5 ILE C 32 MET C 35 -1 O ALA C 34 N THR C 26
SHEET 3 AA8 5 VAL C 119 HIS C 123 1 O ALA C 120 N ILE C 33
SHEET 4 AA8 5 TYR C 65 ASN C 69 1 N LYS C 66 O ALA C 121
SHEET 5 AA8 5 VAL C 85 GLN C 87 1 O ALA C 86 N ASN C 69
SHEET 1 AA9 5 ARG C 233 GLU C 235 0
SHEET 2 AA9 5 PHE C 238 CYS C 250 -1 O TYR C 240 N ARG C 233
SHEET 3 AA9 5 ALA C 192 PHE C 200 -1 N PHE C 195 O LEU C 247
SHEET 4 AA9 5 LYS C 342 LYS C 349 -1 O THR C 348 N LEU C 194
SHEET 5 AA9 5 LEU C 316 THR C 321 -1 N LEU C 316 O PHE C 347
SHEET 1 AB1 4 VAL C 222 SER C 226 0
SHEET 2 AB1 4 PRO C 213 GLN C 219 -1 N GLN C 219 O VAL C 222
SHEET 3 AB1 4 ASP C 252 HIS C 259 -1 O PHE C 258 N GLN C 214
SHEET 4 AB1 4 ASP C 268 ASN C 276 -1 O PHE C 271 N PHE C 257
SHEET 1 AB2 5 LEU D 25 TYR D 29 0
SHEET 2 AB2 5 ILE D 32 MET D 35 -1 O ALA D 34 N THR D 26
SHEET 3 AB2 5 VAL D 119 HIS D 123 1 O ALA D 120 N ILE D 33
SHEET 4 AB2 5 TYR D 65 ASN D 69 1 N LYS D 66 O ALA D 121
SHEET 5 AB2 5 VAL D 85 GLN D 87 1 O ALA D 86 N ASN D 69
SHEET 1 AB3 5 ARG D 233 GLU D 235 0
SHEET 2 AB3 5 PHE D 238 CYS D 250 -1 O TYR D 240 N ARG D 233
SHEET 3 AB3 5 ALA D 192 PHE D 200 -1 N PHE D 195 O LEU D 247
SHEET 4 AB3 5 LYS D 342 LYS D 349 -1 O THR D 348 N LEU D 194
SHEET 5 AB3 5 LEU D 316 THR D 321 -1 N LEU D 316 O PHE D 347
SHEET 1 AB4 4 VAL D 222 SER D 226 0
SHEET 2 AB4 4 PRO D 213 GLN D 219 -1 N GLN D 219 O VAL D 222
SHEET 3 AB4 4 ASP D 252 HIS D 259 -1 O PHE D 258 N GLN D 214
SHEET 4 AB4 4 ASP D 268 ASN D 276 -1 O PHE D 271 N PHE D 257
SSBOND 1 CYS A 71 CYS A 124 1555 1555 2.04
SSBOND 2 CYS B 71 CYS B 124 1555 1555 2.05
SSBOND 3 CYS C 71 CYS C 124 1555 1555 2.05
SSBOND 4 CYS D 71 CYS D 124 1555 1555 2.04
LINK C2 TLA C 401 O1 VO4 C 402 1555 1555 1.20
LINK O2 TLA C 401 V VO4 C 402 1555 1555 2.37
SITE 1 AC1 10 CYS A 124 LYS A 125 ALA A 126 GLY A 127
SITE 2 AC1 10 LYS A 128 GLY A 129 ARG A 130 THR A 131
SITE 3 AC1 10 HOH A 507 HOH A 563
SITE 1 AC2 13 ASP B 92 HIS B 93 CYS B 124 LYS B 125
SITE 2 AC2 13 ALA B 126 GLY B 127 LYS B 128 GLY B 129
SITE 3 AC2 13 ARG B 130 THR B 131 HOH B 502 HOH B 503
SITE 4 AC2 13 HOH B 521
SITE 1 AC3 13 ASP D 92 HIS D 93 CYS D 124 LYS D 125
SITE 2 AC3 13 ALA D 126 GLY D 127 LYS D 128 GLY D 129
SITE 3 AC3 13 ARG D 130 THR D 131 HOH D 502 HOH D 510
SITE 4 AC3 13 HOH D 521
SITE 1 AC4 12 ASP C 92 HIS C 93 CYS C 124 LYS C 125
SITE 2 AC4 12 ALA C 126 GLY C 127 LYS C 128 GLY C 129
SITE 3 AC4 12 ARG C 130 THR C 131 GLN C 171 HOH C 542
CRYST1 207.060 206.900 87.670 90.00 90.00 90.00 C 2 2 21 32
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 0.004830 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004833 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011406 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
