HEADER HYDROLASE 18-FEB-13 4JA9
TITLE RAT PP5 APO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 5;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PP5, PROTEIN PHOSPHATASE T, PPT;
COMPND 5 EC: 3.1.3.16;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: PPP5C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PP5, ACTIVATION, TAU-DEPHOSPHORYLATION, NEURODEGENERATIVE DISEASE,
KEYWDS 2 SER/THR-PROTEIN PHOSPHATASE DOMAIN, TETRATRICOPEPTIDE REPEAT DOMAIN,
KEYWDS 3 HSP90, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.HASLBECK,M.HELMUTH,F.ALTE,G.POPOWICZ,W.SCHMIDT,M.WEIWAD,G.FISCHER,
AUTHOR 2 G.GEMMECKER,M.SATTLER,F.STRIGGOW,M.GROLL,K.RICHTER
REVDAT 5 20-SEP-23 4JA9 1 REMARK SEQADV LINK
REVDAT 4 10-AUG-16 4JA9 1 JRNL
REVDAT 3 10-FEB-16 4JA9 1 JRNL
REVDAT 2 11-NOV-15 4JA9 1 JRNL REMARK
REVDAT 1 19-FEB-14 4JA9 0
JRNL AUTH V.HASLBECK,A.DRAZIC,J.M.ECKL,F.ALTE,M.HELMUTH,G.POPOWICZ,
JRNL AUTH 2 W.SCHMIDT,F.BRAUN,M.WEIWAD,G.FISCHER,G.GEMMECKER,M.SATTLER,
JRNL AUTH 3 F.STRIGGOW,M.GROLL,K.RICHTER
JRNL TITL SELECTIVE ACTIVATORS OF PROTEIN PHOSPHATASE 5 TARGET THE
JRNL TITL 2 AUTO-INHIBITORY MECHANISM.
JRNL REF BIOSCI.REP. V. 35 2015
JRNL REFN ISSN 0144-8463
JRNL PMID 26182372
JRNL DOI 10.1042/BSR20150042
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 21718
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) : 0.239
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1144
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1526
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3755
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 63
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.16000
REMARK 3 B22 (A**2) : 2.16000
REMARK 3 B33 (A**2) : -4.31000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.267
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.223
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.802
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3837 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3623 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5176 ; 0.991 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8357 ; 0.730 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 465 ; 6.427 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;38.271 ;24.550
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 687 ;18.862 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;14.276 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 552 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4351 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 895 ; 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): 7460 ; 1.329 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 27 ;36.141 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 7416 ; 6.820 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 23 A 498
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2042 -1.5230 -22.7721
REMARK 3 T TENSOR
REMARK 3 T11: 0.1119 T22: 0.0308
REMARK 3 T33: 0.0393 T12: 0.0427
REMARK 3 T13: -0.0200 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.1905 L22: 0.3355
REMARK 3 L33: 0.7151 L12: -0.0022
REMARK 3 L13: 0.0679 L23: 0.2020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0250 S12: -0.0439 S13: -0.0514
REMARK 3 S21: -0.0104 S22: 0.0032 S23: -0.0640
REMARK 3 S31: -0.1253 S32: -0.1125 S33: 0.0217
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
REMARK 4
REMARK 4 4JA9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT. SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22932
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.53700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4JA7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MG(NO3)2, 20% PEG 3350, PH 7.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 189.59500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 25.04500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 25.04500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 94.79750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 25.04500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 25.04500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 284.39250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 25.04500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 25.04500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 94.79750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 25.04500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 25.04500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 284.39250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 189.59500
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 12
REMARK 465 SER A 13
REMARK 465 HIS A 14
REMARK 465 MET A 15
REMARK 465 ARG A 16
REMARK 465 ASP A 17
REMARK 465 GLU A 18
REMARK 465 PRO A 19
REMARK 465 PRO A 20
REMARK 465 ALA A 21
REMARK 465 GLU A 22
REMARK 465 ARG A 150
REMARK 465 ALA A 151
REMARK 465 ILE A 152
REMARK 465 ALA A 153
REMARK 465 GLY A 154
REMARK 465 ASP A 155
REMARK 465 GLU A 156
REMARK 465 HIS A 157
REMARK 465 ARG A 158
REMARK 465 MET A 499
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 LYS A 42 18.57 55.73
REMARK 500 LYS A 126 27.32 80.74
REMARK 500 ASN A 128 59.73 -112.30
REMARK 500 ALA A 132 -79.41 -53.12
REMARK 500 SER A 164 35.53 -69.95
REMARK 500 ILE A 167 -73.36 -72.06
REMARK 500 SER A 177 44.85 -100.68
REMARK 500 GLU A 233 -66.20 1.42
REMARK 500 ASN A 269 56.22 -102.04
REMARK 500 ASP A 274 162.53 74.15
REMARK 500 ARG A 275 -67.95 67.62
REMARK 500 GLU A 305 61.07 -102.78
REMARK 500 TYR A 323 -126.96 -125.33
REMARK 500 ASN A 345 15.24 58.60
REMARK 500 ASN A 372 72.74 -62.21
REMARK 500 ARG A 373 -177.19 179.71
REMARK 500 SER A 403 -147.00 72.38
REMARK 500 SER A 426 -122.21 -130.49
REMARK 500 HIS A 427 -42.75 82.29
REMARK 500 GLN A 454 -34.09 -143.02
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 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 242 OD2
REMARK 620 2 ASP A 271 OD2 75.1
REMARK 620 3 HOH A 602 O 160.2 86.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 271 OD2
REMARK 620 2 ASN A 303 OD1 97.0
REMARK 620 3 HOH A 602 O 84.4 108.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WAO RELATED DB: PDB
REMARK 900 HUMAN PP5 WILD TYPE
REMARK 900 RELATED ID: 4JA7 RELATED DB: PDB
REMARK 900 RAT PP5 CO-CRYSTALLIZED WITH P5SA-2
DBREF 4JA9 A 16 499 UNP P53042 PPP5_RAT 16 499
SEQADV 4JA9 GLY A 12 UNP P53042 EXPRESSION TAG
SEQADV 4JA9 SER A 13 UNP P53042 EXPRESSION TAG
SEQADV 4JA9 HIS A 14 UNP P53042 EXPRESSION TAG
SEQADV 4JA9 MET A 15 UNP P53042 EXPRESSION TAG
SEQRES 1 A 488 GLY SER HIS MET ARG ASP GLU PRO PRO ALA GLU GLY THR
SEQRES 2 A 488 LEU LYS ARG ALA GLU GLU LEU LYS THR GLN ALA ASN ASP
SEQRES 3 A 488 TYR PHE LYS ALA LYS ASP TYR GLU ASN ALA ILE LYS PHE
SEQRES 4 A 488 TYR SER GLN ALA ILE GLU LEU ASN PRO SER ASN ALA ILE
SEQRES 5 A 488 TYR TYR GLY ASN ARG SER LEU ALA TYR LEU ARG THR GLU
SEQRES 6 A 488 CYS TYR GLY TYR ALA LEU GLY ASP ALA THR ARG ALA ILE
SEQRES 7 A 488 GLU LEU ASP LYS LYS TYR ILE LYS GLY TYR TYR ARG ARG
SEQRES 8 A 488 ALA ALA SER ASN MET ALA LEU GLY LYS PHE ARG ALA ALA
SEQRES 9 A 488 LEU ARG ASP TYR GLU THR VAL VAL LYS VAL LYS PRO ASN
SEQRES 10 A 488 ASP LYS ASP ALA LYS MET LYS TYR GLN GLU CYS SER LYS
SEQRES 11 A 488 ILE VAL LYS GLN LYS ALA PHE GLU ARG ALA ILE ALA GLY
SEQRES 12 A 488 ASP GLU HIS ARG ARG SER VAL VAL ASP SER LEU ASP ILE
SEQRES 13 A 488 GLU SER MET THR ILE GLU ASP GLU TYR SER GLY PRO LYS
SEQRES 14 A 488 LEU GLU ASP GLY LYS VAL THR ILE THR PHE MET LYS ASP
SEQRES 15 A 488 LEU MET GLN TRP TYR LYS ASP GLN LYS LYS LEU HIS ARG
SEQRES 16 A 488 LYS CYS ALA TYR GLN ILE LEU VAL GLN VAL LYS GLU VAL
SEQRES 17 A 488 LEU CYS LYS LEU SER THR LEU VAL GLU THR THR LEU LYS
SEQRES 18 A 488 GLU THR GLU LYS ILE THR VAL CYS GLY ASP THR HIS GLY
SEQRES 19 A 488 GLN PHE TYR ASP LEU LEU ASN ILE PHE GLU LEU ASN GLY
SEQRES 20 A 488 LEU PRO SER GLU THR ASN PRO TYR ILE PHE ASN GLY ASP
SEQRES 21 A 488 PHE VAL ASP ARG GLY SER PHE SER VAL GLU VAL ILE LEU
SEQRES 22 A 488 THR LEU PHE GLY PHE LYS LEU LEU TYR PRO ASP HIS PHE
SEQRES 23 A 488 HIS LEU LEU ARG GLY ASN HIS GLU THR ASP ASN MET ASN
SEQRES 24 A 488 GLN ILE TYR GLY PHE GLU GLY GLU VAL LYS ALA LYS TYR
SEQRES 25 A 488 THR ALA GLN MET TYR GLU LEU PHE SER GLU VAL PHE GLU
SEQRES 26 A 488 TRP LEU PRO LEU ALA GLN CYS ILE ASN GLY LYS VAL LEU
SEQRES 27 A 488 ILE MET HIS GLY GLY LEU PHE SER GLU ASP GLY VAL THR
SEQRES 28 A 488 LEU ASP ASP ILE ARG LYS ILE GLU ARG ASN ARG GLN PRO
SEQRES 29 A 488 PRO ASP SER GLY PRO MET CYS ASP LEU LEU TRP SER ASP
SEQRES 30 A 488 PRO GLN PRO GLN ASN GLY ARG SER VAL SER LYS ARG GLY
SEQRES 31 A 488 VAL SER CYS GLN PHE GLY PRO ASP VAL THR LYS ALA PHE
SEQRES 32 A 488 LEU GLU GLU ASN GLN LEU ASP TYR ILE ILE ARG SER HIS
SEQRES 33 A 488 GLU VAL LYS ALA GLU GLY TYR GLU VAL ALA HIS GLY GLY
SEQRES 34 A 488 ARG CYS VAL THR VAL PHE SER ALA PRO ASN TYR CYS ASP
SEQRES 35 A 488 GLN MET GLY ASN LYS ALA SER TYR ILE HIS LEU GLN GLY
SEQRES 36 A 488 SER ASP LEU ARG PRO GLN PHE HIS GLN PHE THR ALA VAL
SEQRES 37 A 488 PRO HIS PRO ASN VAL LYS PRO MET ALA TYR ALA ASN THR
SEQRES 38 A 488 LEU LEU GLN LEU GLY MET MET
HET MG A 501 1
HET MG A 502 1
HETNAM MG MAGNESIUM ION
FORMUL 2 MG 2(MG 2+)
FORMUL 4 HOH *63(H2 O)
HELIX 1 1 GLY A 23 ALA A 41 1 19
HELIX 2 2 ASP A 43 ASN A 58 1 16
HELIX 3 3 ASN A 61 THR A 75 1 15
HELIX 4 4 CYS A 77 ASP A 92 1 16
HELIX 5 5 TYR A 95 LEU A 109 1 15
HELIX 6 6 LYS A 111 LYS A 124 1 14
HELIX 7 7 MET A 134 GLU A 149 1 16
HELIX 8 8 THR A 187 ASP A 200 1 14
HELIX 9 9 HIS A 205 LEU A 223 1 19
HELIX 10 10 GLN A 246 GLY A 258 1 13
HELIX 11 11 PHE A 278 TYR A 293 1 16
HELIX 12 12 THR A 306 GLN A 311 1 6
HELIX 13 13 GLY A 314 TYR A 323 1 10
HELIX 14 14 THR A 324 TRP A 337 1 14
HELIX 15 15 THR A 362 LYS A 368 1 7
HELIX 16 16 GLY A 379 SER A 387 1 9
HELIX 17 17 GLY A 407 ASN A 418 1 12
HELIX 18 18 ASN A 450 GLN A 454 5 5
HELIX 19 19 ASN A 491 GLN A 495 5 5
SHEET 1 A 3 LEU A 226 THR A 229 0
SHEET 2 A 3 ALA A 341 ILE A 344 1 O CYS A 343 N VAL A 227
SHEET 3 A 3 VAL A 348 MET A 351 -1 O ILE A 350 N GLN A 342
SHEET 1 B 5 PHE A 297 LEU A 300 0
SHEET 2 B 5 TYR A 266 ASN A 269 1 N PHE A 268 O HIS A 298
SHEET 3 B 5 LYS A 236 CYS A 240 1 N CYS A 240 O ILE A 267
SHEET 4 B 5 ALA A 459 GLN A 465 -1 O LEU A 464 N ILE A 237
SHEET 5 B 5 GLN A 472 PHE A 476 -1 O HIS A 474 N TYR A 461
SHEET 1 C 3 ASP A 388 PRO A 389 0
SHEET 2 C 3 CYS A 404 PHE A 406 1 O PHE A 406 N ASP A 388
SHEET 3 C 3 ARG A 395 VAL A 397 -1 N SER A 396 O GLN A 405
SHEET 1 D 3 ILE A 423 ARG A 425 0
SHEET 2 D 3 CYS A 442 VAL A 445 1 O VAL A 443 N ARG A 425
SHEET 3 D 3 TYR A 434 ALA A 437 -1 N GLU A 435 O THR A 444
LINK OD2 ASP A 242 MG MG A 501 1555 1555 2.31
LINK OD2 ASP A 271 MG MG A 501 1555 1555 2.25
LINK OD2 ASP A 271 MG MG A 502 1555 1555 2.30
LINK OD1 ASN A 303 MG MG A 502 1555 1555 2.45
LINK MG MG A 501 O HOH A 602 1555 1555 2.51
LINK MG MG A 502 O HOH A 602 1555 1555 2.54
SITE 1 AC1 6 ASP A 242 HIS A 244 ASP A 271 HIS A 427
SITE 2 AC1 6 MG A 502 HOH A 602
SITE 1 AC2 7 ASP A 242 ASP A 271 ASN A 303 HIS A 352
SITE 2 AC2 7 HIS A 427 MG A 501 HOH A 602
CRYST1 50.090 50.090 379.190 90.00 90.00 90.00 P 41 21 2 8
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 0.019964 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002637 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
