HEADER HYDROLASE 17-JUL-14 4UT3
TITLE X-RAY STRUCTURE OF THE HUMAN PP1 GAMMA CATALYTIC SUBUNIT TREATED WITH
TITLE 2 HYDROGEN PEROXIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: PP-1G, PROTEIN PHOSPHATASE 1C CATALYTIC SUBUNIT, PROTEIN
COMPND 6 PHOSPHATASE 1 GAMMA ISOFORM;
COMPND 7 EC: 3.1.3.16;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC
COMPND 11 SUBUNIT;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: PP-1G, PROTEIN PHOSPHATASE 1C CATALYTIC SUBUNIT, PROTEIN
COMPND 14 PHOSPHATASE 1 GAMMA ISOFORM;
COMPND 15 EC: 3.1.3.16;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5[ALPHA];
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5[ALPHA];
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 668369
KEYWDS METAL CENTER, METALLOPROTEIN, ENZYME ACTIVATION, PHOSPHOPROTEIN
KEYWDS 2 PHOSPHATASES, PROTEIN PHOSPHATASE 1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZEH SILVA,J.KOPEC,D.FOTINOU,R.A.STEINER
REVDAT 3 10-JAN-24 4UT3 1 REMARK LINK
REVDAT 2 25-JAN-17 4UT3 1 AUTHOR JRNL
REVDAT 1 22-JUL-15 4UT3 0
JRNL AUTH C.X.SANTOS,A.D.HAFSTAD,M.BERETTA,M.ZHANG,C.MOLENAAR,J.KOPEC,
JRNL AUTH 2 D.FOTINOU,T.V.MURRAY,A.M.COBB,D.MARTIN,M.ZEH SILVA,
JRNL AUTH 3 N.ANILKUMAR,K.SCHRODER,C.M.SHANAHAN,A.C.BREWER,R.P.BRANDES,
JRNL AUTH 4 E.BLANC,M.PARSONS,V.BELOUSOV,R.CAMMACK,R.C.HIDER,
JRNL AUTH 5 R.A.STEINER,A.M.SHAH
JRNL TITL TARGETED REDOX INHIBITION OF PROTEIN PHOSPHATASE 1 BY NOX4
JRNL TITL 2 REGULATES EIF2ALPHA-MEDIATED STRESS SIGNALING.
JRNL REF EMBO J. V. 35 319 2016
JRNL REFN ISSN 0261-4189
JRNL PMID 26742780
JRNL DOI 10.15252/EMBJ.201592394
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 33509
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1742
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1959
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4745
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -32.79000
REMARK 3 B22 (A**2) : 46.00000
REMARK 3 B33 (A**2) : -13.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.58000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.050
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.039
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.113
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.460
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4879 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4640 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6583 ; 1.267 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10690 ; 0.810 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 590 ; 5.955 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 242 ;36.751 ;23.967
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 863 ;13.870 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;16.118 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 704 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5480 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1154 ; 0.003 ; 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): 2354 ; 2.918 ; 4.391
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2353 ; 2.917 ; 4.390
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2940 ; 4.351 ; 6.580
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2525 ; 3.882 ; 4.901
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 : 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 4UT3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1290061269.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97620
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35328
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 45.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.62000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 2O8A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7-12% PEG3350, 0.1 M BICINE, PH 9.0
REMARK 280 SOAKING IN RESERVOIR ENRICHED WITH 50MM H2O2 FOR 10 MINS
REMARK 280 CRYOPROTECTION IN RESEVOIR ENRICHED WITH 25% MPD
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 52.61000
REMARK 290 SMTRY3 2 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 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 LEU A 4
REMARK 465 ASP A 5
REMARK 465 GLU A 300
REMARK 465 LYS A 301
REMARK 465 LYS A 302
REMARK 465 LYS A 303
REMARK 465 PRO A 304
REMARK 465 ASN A 305
REMARK 465 ALA A 306
REMARK 465 THR A 307
REMARK 465 ARG A 308
REMARK 465 PRO A 309
REMARK 465 VAL A 310
REMARK 465 THR A 311
REMARK 465 PRO A 312
REMARK 465 PRO A 313
REMARK 465 ARG A 314
REMARK 465 GLY A 315
REMARK 465 MET A 316
REMARK 465 ILE A 317
REMARK 465 THR A 318
REMARK 465 LYS A 319
REMARK 465 GLN A 320
REMARK 465 ALA A 321
REMARK 465 LYS A 322
REMARK 465 LYS A 323
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ASP B 3
REMARK 465 LEU B 4
REMARK 465 ASP B 5
REMARK 465 GLU B 300
REMARK 465 LYS B 301
REMARK 465 LYS B 302
REMARK 465 LYS B 303
REMARK 465 PRO B 304
REMARK 465 ASN B 305
REMARK 465 ALA B 306
REMARK 465 THR B 307
REMARK 465 ARG B 308
REMARK 465 PRO B 309
REMARK 465 VAL B 310
REMARK 465 THR B 311
REMARK 465 PRO B 312
REMARK 465 PRO B 313
REMARK 465 ARG B 314
REMARK 465 GLY B 315
REMARK 465 MET B 316
REMARK 465 ILE B 317
REMARK 465 THR B 318
REMARK 465 LYS B 319
REMARK 465 GLN B 320
REMARK 465 ALA B 321
REMARK 465 LYS B 322
REMARK 465 LYS B 323
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 O1 PO4 B 501 O HOH B 2017 2.13
REMARK 500 O HOH A 2028 O HOH A 2063 2.17
REMARK 500 O4 PO4 A 501 O HOH A 2021 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 95 152.74 83.06
REMARK 500 ARG A 96 -49.60 70.08
REMARK 500 TYR A 144 -109.91 -135.24
REMARK 500 SER A 224 -154.44 61.22
REMARK 500 ALA A 247 -130.85 -126.87
REMARK 500 HIS A 248 -22.68 85.14
REMARK 500 CYS A 273 -1.09 72.05
REMARK 500 ASP B 95 151.77 83.27
REMARK 500 ARG B 96 -49.94 71.45
REMARK 500 TYR B 144 -109.88 -134.55
REMARK 500 SER B 224 -153.49 60.70
REMARK 500 ALA B 247 -130.62 -126.35
REMARK 500 HIS B 248 -23.37 85.67
REMARK 500 CSO B 273 -0.79 72.07
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 B2032 DISTANCE = 6.92 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 MN A 400 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD2
REMARK 620 2 HIS A 66 NE2 100.9
REMARK 620 3 ASP A 92 OD2 96.2 97.5
REMARK 620 4 PO4 A 501 O3 162.2 93.9 91.7
REMARK 620 5 HOH A2021 O 93.6 161.8 69.7 74.2
REMARK 620 6 HOH A2022 O 82.8 87.0 175.5 88.1 106.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 92 OD2
REMARK 620 2 ASN A 124 OD1 104.0
REMARK 620 3 HIS A 173 NE2 89.6 88.7
REMARK 620 4 HIS A 248 ND1 155.7 100.2 88.8
REMARK 620 5 PO4 A 501 O4 94.7 87.8 175.1 88.3
REMARK 620 6 HOH A2021 O 74.7 153.8 117.3 84.5 66.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 400 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 64 OD2
REMARK 620 2 HIS B 66 NE2 98.3
REMARK 620 3 ASP B 92 OD2 96.0 98.0
REMARK 620 4 PO4 B 501 O3 164.5 91.7 94.3
REMARK 620 5 HOH B2017 O 90.9 166.1 70.6 81.7
REMARK 620 6 HOH B2018 O 89.3 96.6 163.6 77.7 93.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 92 OD2
REMARK 620 2 ASN B 124 OD1 102.6
REMARK 620 3 HIS B 173 NE2 91.9 90.1
REMARK 620 4 HIS B 248 ND1 156.2 101.0 91.9
REMARK 620 5 PO4 B 501 O1 91.2 89.0 176.9 85.4
REMARK 620 6 HOH B2017 O 74.0 152.5 117.1 83.3 64.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UT2 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE HUMAN PP1 GAMMA CATALYTIC SUBUNIT TREATED
REMARK 900 WITH ASCORBATE
DBREF 4UT3 A 1 323 UNP P36873 PP1G_HUMAN 1 323
DBREF 4UT3 B 1 323 UNP P36873 PP1G_HUMAN 1 323
SEQRES 1 A 323 MET ALA ASP LEU ASP LYS LEU ASN ILE ASP SER ILE ILE
SEQRES 2 A 323 GLN ARG LEU LEU GLU VAL ARG GLY SER LYS PRO GLY LYS
SEQRES 3 A 323 ASN VAL GLN LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS
SEQRES 4 A 323 LEU LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU
SEQRES 5 A 323 LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE
SEQRES 6 A 323 HIS GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR
SEQRES 7 A 323 GLY GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY
SEQRES 8 A 323 ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE
SEQRES 9 A 323 CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN
SEQRES 10 A 323 PHE PHE LEU LEU ARG GLY ASN HIS GLU CSO ALA SER ILE
SEQRES 11 A 323 ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG
SEQRES 12 A 323 TYR ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE
SEQRES 13 A 323 ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE
SEQRES 14 A 323 PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER
SEQRES 15 A 323 MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL
SEQRES 16 A 323 PRO ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP
SEQRES 17 A 323 PRO ASP LYS ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG
SEQRES 18 A 323 GLY VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS
SEQRES 19 A 323 PHE LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA
SEQRES 20 A 323 HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS
SEQRES 21 A 323 ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS
SEQRES 22 A 323 GLY GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP
SEQRES 23 A 323 GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA
SEQRES 24 A 323 GLU LYS LYS LYS PRO ASN ALA THR ARG PRO VAL THR PRO
SEQRES 25 A 323 PRO ARG GLY MET ILE THR LYS GLN ALA LYS LYS
SEQRES 1 B 323 MET ALA ASP LEU ASP LYS LEU ASN ILE ASP SER ILE ILE
SEQRES 2 B 323 GLN ARG LEU LEU GLU VAL ARG GLY SER LYS PRO GLY LYS
SEQRES 3 B 323 ASN VAL GLN LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS
SEQRES 4 B 323 LEU LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU
SEQRES 5 B 323 LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE
SEQRES 6 B 323 HIS GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR
SEQRES 7 B 323 GLY GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY
SEQRES 8 B 323 ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE
SEQRES 9 B 323 CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN
SEQRES 10 B 323 PHE PHE LEU LEU ARG GLY ASN HIS GLU CSO ALA SER ILE
SEQRES 11 B 323 ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG
SEQRES 12 B 323 TYR ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE
SEQRES 13 B 323 ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE
SEQRES 14 B 323 PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER
SEQRES 15 B 323 MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL
SEQRES 16 B 323 PRO ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP
SEQRES 17 B 323 PRO ASP LYS ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG
SEQRES 18 B 323 GLY VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS
SEQRES 19 B 323 PHE LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA
SEQRES 20 B 323 HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS
SEQRES 21 B 323 ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CSO
SEQRES 22 B 323 GLY GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP
SEQRES 23 B 323 GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA
SEQRES 24 B 323 GLU LYS LYS LYS PRO ASN ALA THR ARG PRO VAL THR PRO
SEQRES 25 B 323 PRO ARG GLY MET ILE THR LYS GLN ALA LYS LYS
MODRES 4UT3 CSO A 127 CYS S-HYDROXYCYSTEINE
MODRES 4UT3 CSO B 127 CYS S-HYDROXYCYSTEINE
MODRES 4UT3 CSO B 273 CYS S-HYDROXYCYSTEINE
HET CSO A 127 7
HET CSO B 127 7
HET CSO B 273 7
HET MN A 400 1
HET MN A 401 1
HET PO4 A 501 5
HET MN B 400 1
HET MN B 401 1
HET PO4 B 501 5
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM MN MANGANESE (II) ION
HETNAM PO4 PHOSPHATE ION
FORMUL 1 CSO 3(C3 H7 N O3 S)
FORMUL 3 MN 4(MN 2+)
FORMUL 5 PO4 2(O4 P 3-)
FORMUL 9 HOH *161(H2 O)
HELIX 1 1 ASN A 8 GLU A 18 1 11
HELIX 2 2 GLN A 31 GLN A 49 1 19
HELIX 3 3 GLN A 68 GLY A 80 1 13
HELIX 4 4 GLN A 99 TYR A 114 1 16
HELIX 5 5 CSO A 127 ARG A 132 1 6
HELIX 6 6 GLY A 135 TYR A 144 1 10
HELIX 7 7 ASN A 145 ASN A 157 1 13
HELIX 8 8 SER A 182 ARG A 188 1 7
HELIX 9 9 GLY A 199 SER A 207 1 9
HELIX 10 10 GLY A 228 ASP A 240 1 13
HELIX 11 11 ASN A 271 GLU A 275 5 5
HELIX 12 12 ASN B 8 GLU B 18 1 11
HELIX 13 13 GLN B 31 GLN B 49 1 19
HELIX 14 14 GLN B 68 GLY B 80 1 13
HELIX 15 15 GLN B 99 TYR B 114 1 16
HELIX 16 16 CSO B 127 ARG B 132 1 6
HELIX 17 17 GLY B 135 TYR B 144 1 10
HELIX 18 18 ASN B 145 ASN B 157 1 13
HELIX 19 19 SER B 182 ARG B 188 1 7
HELIX 20 20 GLY B 199 SER B 207 1 9
HELIX 21 21 GLY B 228 ASP B 240 1 13
HELIX 22 22 ASN B 271 GLU B 275 5 5
SHEET 1 AA 6 LEU A 52 LEU A 55 0
SHEET 2 AA 6 ALA A 162 VAL A 165 1 O ALA A 162 N LEU A 53
SHEET 3 AA 6 ILE A 169 CYS A 172 -1 O ILE A 169 N VAL A 165
SHEET 4 AA 6 LEU A 243 ARG A 246 1 O LEU A 243 N PHE A 170
SHEET 5 AA 6 LEU A 263 LEU A 266 1 O VAL A 264 N ARG A 246
SHEET 6 AA 6 TYR A 255 PHE A 258 -1 O GLU A 256 N THR A 265
SHEET 1 AB 5 PHE A 118 LEU A 120 0
SHEET 2 AB 5 TYR A 87 PHE A 89 1 O TYR A 87 N PHE A 119
SHEET 3 AB 5 LEU A 59 CYS A 62 1 O LYS A 60 N LEU A 88
SHEET 4 AB 5 GLY A 280 VAL A 285 -1 O MET A 283 N ILE A 61
SHEET 5 AB 5 CYS A 291 LEU A 296 -1 O SER A 292 N SER A 284
SHEET 1 AC 3 ASP A 208 PRO A 209 0
SHEET 2 AC 3 PHE A 225 PHE A 227 1 O PHE A 225 N ASP A 208
SHEET 3 AC 3 TRP A 216 GLU A 218 -1 O GLY A 217 N THR A 226
SHEET 1 BA 6 LEU B 52 LEU B 55 0
SHEET 2 BA 6 ALA B 162 VAL B 165 1 O ALA B 162 N LEU B 53
SHEET 3 BA 6 ILE B 169 CYS B 172 -1 O ILE B 169 N VAL B 165
SHEET 4 BA 6 LEU B 243 ARG B 246 1 O LEU B 243 N PHE B 170
SHEET 5 BA 6 LEU B 263 LEU B 266 1 O VAL B 264 N ARG B 246
SHEET 6 BA 6 TYR B 255 PHE B 258 -1 O GLU B 256 N THR B 265
SHEET 1 BB 5 PHE B 118 LEU B 120 0
SHEET 2 BB 5 TYR B 87 PHE B 89 1 O TYR B 87 N PHE B 119
SHEET 3 BB 5 LEU B 59 CYS B 62 1 O LYS B 60 N LEU B 88
SHEET 4 BB 5 GLY B 280 VAL B 285 -1 O MET B 283 N ILE B 61
SHEET 5 BB 5 CYS B 291 LEU B 296 -1 O SER B 292 N SER B 284
SHEET 1 BC 3 ASP B 208 PRO B 209 0
SHEET 2 BC 3 PHE B 225 PHE B 227 1 O PHE B 225 N ASP B 208
SHEET 3 BC 3 TRP B 216 GLU B 218 -1 O GLY B 217 N THR B 226
LINK C GLU A 126 N CSO A 127 1555 1555 1.32
LINK C CSO A 127 N ALA A 128 1555 1555 1.33
LINK C GLU B 126 N CSO B 127 1555 1555 1.32
LINK C CSO B 127 N ALA B 128 1555 1555 1.33
LINK C TYR B 272 N CSO B 273 1555 1555 1.34
LINK C CSO B 273 N GLY B 274 1555 1555 1.33
LINK OD2 ASP A 64 MN MN A 400 1555 1555 1.96
LINK NE2 HIS A 66 MN MN A 400 1555 1555 2.22
LINK OD2 ASP A 92 MN MN A 400 1555 1555 2.06
LINK OD2 ASP A 92 MN MN A 401 1555 1555 2.22
LINK OD1 ASN A 124 MN MN A 401 1555 1555 1.89
LINK NE2 HIS A 173 MN MN A 401 1555 1555 2.24
LINK ND1 HIS A 248 MN MN A 401 1555 1555 2.32
LINK MN MN A 400 O3 PO4 A 501 1555 1555 1.99
LINK MN MN A 400 O HOH A2021 1555 1555 2.23
LINK MN MN A 400 O HOH A2022 1555 1555 1.96
LINK MN MN A 401 O4 PO4 A 501 1555 1555 2.17
LINK MN MN A 401 O HOH A2021 1555 1555 1.79
LINK OD2 ASP B 64 MN MN B 400 1555 1555 1.99
LINK NE2 HIS B 66 MN MN B 400 1555 1555 2.25
LINK OD2 ASP B 92 MN MN B 400 1555 1555 2.04
LINK OD2 ASP B 92 MN MN B 401 1555 1555 2.22
LINK OD1 ASN B 124 MN MN B 401 1555 1555 1.94
LINK NE2 HIS B 173 MN MN B 401 1555 1555 2.15
LINK ND1 HIS B 248 MN MN B 401 1555 1555 2.32
LINK MN MN B 400 O3 PO4 B 501 1555 1555 2.25
LINK MN MN B 400 O HOH B2017 1555 1555 2.20
LINK MN MN B 400 O HOH B2018 1555 1555 2.11
LINK MN MN B 401 O1 PO4 B 501 1555 1555 2.17
LINK MN MN B 401 O HOH B2017 1555 1555 1.81
CISPEP 1 ALA A 57 PRO A 58 0 0.21
CISPEP 2 PRO A 82 PRO A 83 0 9.40
CISPEP 3 ARG A 191 PRO A 192 0 -5.42
CISPEP 4 ALA B 57 PRO B 58 0 4.41
CISPEP 5 PRO B 82 PRO B 83 0 6.12
CISPEP 6 ARG B 191 PRO B 192 0 -8.19
SITE 1 AC1 7 ASP A 64 HIS A 66 ASP A 92 MN A 401
SITE 2 AC1 7 PO4 A 501 HOH A2021 HOH A2022
SITE 1 AC2 7 ASP A 92 ASN A 124 HIS A 173 HIS A 248
SITE 2 AC2 7 MN A 400 PO4 A 501 HOH A2021
SITE 1 AC3 14 HIS A 66 ASP A 92 ARG A 96 ASN A 124
SITE 2 AC3 14 HIS A 125 ARG A 221 HIS A 248 MN A 400
SITE 3 AC3 14 MN A 401 HOH A2021 HOH A2022 HOH A2034
SITE 4 AC3 14 HOH A2035 HOH A2074
SITE 1 AC4 7 ASP B 64 HIS B 66 ASP B 92 MN B 401
SITE 2 AC4 7 PO4 B 501 HOH B2017 HOH B2018
SITE 1 AC5 7 ASP B 92 ASN B 124 HIS B 173 HIS B 248
SITE 2 AC5 7 MN B 400 PO4 B 501 HOH B2017
SITE 1 AC6 13 HIS B 66 ASP B 92 ARG B 96 ASN B 124
SITE 2 AC6 13 HIS B 125 ARG B 221 HIS B 248 MN B 400
SITE 3 AC6 13 MN B 401 HOH B2017 HOH B2018 HOH B2030
SITE 4 AC6 13 HOH B2064
CRYST1 38.450 105.220 89.820 90.00 90.34 90.00 P 1 21 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 0.026008 0.000000 0.000154 0.00000
SCALE2 0.000000 0.009504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011134 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
