HEADER HYDROLASE/NUCLEAR PROTEIN 12-SEP-13 4MOY
TITLE STRUCTURE OF A SECOND NUCLEAR PP1 HOLOENZYME, CRYSTAL FORM 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: PP1 ALPHA CATALYTIC SUBUNIT;
COMPND 6 SYNONYM: PP-1A;
COMPND 7 EC: 3.1.3.16;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT
COMPND 11 10;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: PP1 NUCLEAR TARGETING SUBUNIT;
COMPND 14 SYNONYM: MHC CLASS I REGION PROLINE-RICH PROTEIN CAT53, PHOSPHATASE 1
COMPND 15 NUCLEAR TARGETING SUBUNIT, PROTEIN PNUTS;
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 GENE: PPP1CA, PPP1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 10 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 11 ORGANISM_TAXID: 10116;
SOURCE 12 GENE: PPP1R10, CAT53, PNUTS;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SERINE/THREONINE PHOSPHATASE, NUCLEUS, HYDROLASE-NUCLEAR PROTEIN
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.CHOY,M.HIEKE,W.PETI,R.PAGE
REVDAT 3 28-FEB-24 4MOY 1 REMARK SEQADV LINK
REVDAT 2 23-APR-14 4MOY 1 JRNL
REVDAT 1 26-MAR-14 4MOY 0
JRNL AUTH M.S.CHOY,M.HIEKE,G.S.KUMAR,G.R.LEWIS,K.R.GONZALEZ-DEWHITT,
JRNL AUTH 2 R.P.KESSLER,B.J.STEIN,M.HESSENBERGER,A.C.NAIRN,W.PETI,R.PAGE
JRNL TITL UNDERSTANDING THE ANTAGONISM OF RETINOBLASTOMA PROTEIN
JRNL TITL 2 DEPHOSPHORYLATION BY PNUTS PROVIDES INSIGHTS INTO THE PP1
JRNL TITL 3 REGULATORY CODE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 4097 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 24591642
JRNL DOI 10.1073/PNAS.1317395111
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 24199
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1237
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.9891 - 4.5648 1.00 2675 130 0.1453 0.1403
REMARK 3 2 4.5648 - 3.6238 1.00 2557 138 0.1179 0.1500
REMARK 3 3 3.6238 - 3.1658 1.00 2538 149 0.1551 0.2032
REMARK 3 4 3.1658 - 2.8764 1.00 2564 143 0.1662 0.2205
REMARK 3 5 2.8764 - 2.6703 1.00 2526 129 0.1752 0.2497
REMARK 3 6 2.6703 - 2.5129 1.00 2516 142 0.1722 0.2225
REMARK 3 7 2.5129 - 2.3870 1.00 2527 135 0.1741 0.2327
REMARK 3 8 2.3870 - 2.2831 1.00 2525 134 0.1807 0.2322
REMARK 3 9 2.2831 - 2.1953 0.99 2534 137 0.2119 0.2572
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 2686
REMARK 3 ANGLE : 1.184 3656
REMARK 3 CHIRALITY : 0.077 393
REMARK 3 PLANARITY : 0.005 472
REMARK 3 DIHEDRAL : 13.056 971
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3682 22.6704 19.4766
REMARK 3 T TENSOR
REMARK 3 T11: 0.1795 T22: 0.2179
REMARK 3 T33: 0.2348 T12: 0.0187
REMARK 3 T13: 0.0402 T23: -0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 1.0467 L22: 4.0526
REMARK 3 L33: 1.8467 L12: 0.1946
REMARK 3 L13: 0.2851 L23: 1.3302
REMARK 3 S TENSOR
REMARK 3 S11: 0.0293 S12: -0.0347 S13: -0.0676
REMARK 3 S21: 0.1370 S22: -0.3088 S23: 0.6497
REMARK 3 S31: 0.0728 S32: -0.2275 S33: 0.2401
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 390 THROUGH 424 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.0869 28.9405 20.7716
REMARK 3 T TENSOR
REMARK 3 T11: 0.2648 T22: 0.3914
REMARK 3 T33: 0.2392 T12: -0.0420
REMARK 3 T13: 0.0199 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 0.5233 L22: 1.3716
REMARK 3 L33: 2.1560 L12: -0.3478
REMARK 3 L13: 0.4310 L23: 0.2682
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: 0.2832 S13: -0.1040
REMARK 3 S21: 0.0927 S22: -0.2577 S23: 0.0916
REMARK 3 S31: -0.0042 S32: -0.4973 S33: 0.1067
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4MOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082183.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-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 : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24217
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.195
REMARK 200 RESOLUTION RANGE LOW (A) : 43.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 1 M LICL, 18% PEG 6000, PH
REMARK 280 7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.81667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 15.90833
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 15.90833
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.81667
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 530 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 566 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 624 LIES ON A SPECIAL POSITION.
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 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 GLY A 5
REMARK 465 SER A 6
REMARK 465 LYS B 425
REMARK 465 ILE B 426
REMARK 465 LYS B 427
REMARK 465 ASP B 428
REMARK 465 PHE B 429
REMARK 465 GLY B 430
REMARK 465 GLU B 431
REMARK 465 ALA B 432
REMARK 465 ALA B 433
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 23 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 44 CG CD OE1 OE2
REMARK 470 LYS A 141 CE NZ
REMARK 470 LYS A 147 CD CE NZ
REMARK 470 LYS A 150 CD CE NZ
REMARK 470 ARG A 188 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 194 CG OD1 OD2
REMARK 470 ASP A 197 CG OD1 OD2
REMARK 470 GLN A 198 CG CD OE1 NE2
REMARK 470 LYS A 211 CG CD CE NZ
REMARK 470 GLN A 214 CG CD OE1 NE2
REMARK 470 GLU A 218 CG CD OE1 OE2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 LYS A 234 CG CD CE NZ
REMARK 470 GLU A 287 CD OE1 OE2
REMARK 470 LYS A 297 CE NZ
REMARK 470 ARG B 394 NE CZ NH1 NH2
REMARK 470 LYS B 395 CG CD CE NZ
REMARK 470 GLU B 403 CG CD OE1 OE2
REMARK 470 LYS B 406 CG CD CE NZ
REMARK 470 GLU B 417 CG CD OE1 OE2
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 95 152.30 78.47
REMARK 500 ARG A 96 -46.75 74.09
REMARK 500 TYR A 144 -115.58 -139.46
REMARK 500 GLU A 167 16.76 59.33
REMARK 500 SER A 224 -151.97 60.00
REMARK 500 ALA A 247 -127.22 -133.90
REMARK 500 HIS A 248 -28.63 74.89
REMARK 500 LYS A 260 -122.25 64.83
REMARK 500 CYS A 273 35.68 34.18
REMARK 500 ASP A 277 34.72 -97.41
REMARK 500 LEU A 289 30.55 72.67
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 MN A 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD2
REMARK 620 2 HIS A 66 NE2 99.2
REMARK 620 3 ASP A 92 OD2 87.1 94.7
REMARK 620 4 PO4 A 404 O3 172.6 88.2 93.5
REMARK 620 5 HOH A 633 O 98.5 80.2 173.0 81.5
REMARK 620 6 HOH A 634 O 89.8 170.6 88.7 82.9 95.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 92 OD2
REMARK 620 2 ASN A 124 OD1 96.5
REMARK 620 3 HIS A 173 NE2 88.0 83.0
REMARK 620 4 HIS A 248 ND1 160.5 101.7 87.2
REMARK 620 5 PO4 A 404 O4 99.8 83.5 165.2 89.4
REMARK 620 6 HOH A 634 O 86.9 158.3 118.5 78.9 74.8
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V4Y RELATED DB: PDB
REMARK 900 NIPP1:PP1 HOLOENZYME
DBREF 4MOY A 7 300 UNP P62136 PP1A_HUMAN 7 300
DBREF 4MOY B 393 433 UNP O55000 PP1RA_RAT 393 433
SEQADV 4MOY GLY A 2 UNP P62136 EXPRESSION TAG
SEQADV 4MOY HIS A 3 UNP P62136 EXPRESSION TAG
SEQADV 4MOY MET A 4 UNP P62136 EXPRESSION TAG
SEQADV 4MOY GLY A 5 UNP P62136 EXPRESSION TAG
SEQADV 4MOY SER A 6 UNP P62136 EXPRESSION TAG
SEQADV 4MOY GLY B 390 UNP O55000 EXPRESSION TAG
SEQADV 4MOY ALA B 391 UNP O55000 EXPRESSION TAG
SEQADV 4MOY MET B 392 UNP O55000 EXPRESSION TAG
SEQRES 1 A 299 GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY
SEQRES 2 A 299 ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN
SEQRES 3 A 299 VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU
SEQRES 4 A 299 LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU
SEQRES 5 A 299 GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS
SEQRES 6 A 299 GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY
SEQRES 7 A 299 GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP
SEQRES 8 A 299 TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS
SEQRES 9 A 299 LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE
SEQRES 10 A 299 PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN
SEQRES 11 A 299 ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR
SEQRES 12 A 299 ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN
SEQRES 13 A 299 CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE
SEQRES 14 A 299 CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET
SEQRES 15 A 299 GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO
SEQRES 16 A 299 ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO
SEQRES 17 A 299 ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY
SEQRES 18 A 299 VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE
SEQRES 19 A 299 LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS
SEQRES 20 A 299 GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG
SEQRES 21 A 299 GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY
SEQRES 22 A 299 GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU
SEQRES 23 A 299 THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP
SEQRES 1 B 44 GLY ALA MET GLY ARG LYS ARG LYS THR VAL THR TRP PRO
SEQRES 2 B 44 GLU GLU GLY LYS LEU ARG GLU TYR PHE TYR PHE GLU LEU
SEQRES 3 B 44 ASP GLU THR GLU ARG VAL ASN VAL ASN LYS ILE LYS ASP
SEQRES 4 B 44 PHE GLY GLU ALA ALA
HET MN A 401 1
HET MN A 402 1
HET CL A 403 1
HET PO4 A 404 5
HET GOL A 405 6
HET GOL A 406 6
HETNAM MN MANGANESE (II) ION
HETNAM CL CHLORIDE ION
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MN 2(MN 2+)
FORMUL 5 CL CL 1-
FORMUL 6 PO4 O4 P 3-
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 9 HOH *159(H2 O)
HELIX 1 1 ASN A 8 VAL A 19 1 12
HELIX 2 2 THR A 31 SER A 48 1 18
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 CYS A 127 GLY A 135 1 9
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 ILE A 189 1 8
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
SHEET 1 A 6 LEU A 52 LEU A 55 0
SHEET 2 A 6 ALA A 162 VAL A 165 1 O ILE A 164 N LEU A 55
SHEET 3 A 6 ILE A 169 CYS A 171 -1 O CYS A 171 N ALA A 163
SHEET 4 A 6 LEU A 243 ARG A 246 1 O CYS A 245 N PHE A 170
SHEET 5 A 6 LEU A 263 LEU A 266 1 O LEU A 266 N ARG A 246
SHEET 6 A 6 TYR A 255 PHE A 258 -1 N GLU A 256 O THR A 265
SHEET 1 B 6 PHE A 118 LEU A 120 0
SHEET 2 B 6 TYR A 87 PHE A 89 1 N PHE A 89 O PHE A 119
SHEET 3 B 6 LEU A 59 CYS A 62 1 N LYS A 60 O LEU A 88
SHEET 4 B 6 GLY A 280 VAL A 285 -1 O VAL A 285 N LEU A 59
SHEET 5 B 6 CYS A 291 PRO A 298 -1 O LEU A 296 N GLY A 280
SHEET 6 B 6 ARG B 408 PHE B 413 1 O GLU B 409 N ILE A 295
SHEET 1 C 3 ASP A 208 PRO A 209 0
SHEET 2 C 3 PHE A 225 PHE A 227 1 O PHE A 225 N ASP A 208
SHEET 3 C 3 TRP A 216 GLU A 218 -1 N GLY A 217 O THR A 226
LINK OD2 ASP A 64 MN MN A 401 1555 1555 2.23
LINK NE2 HIS A 66 MN MN A 401 1555 1555 2.30
LINK OD2 ASP A 92 MN MN A 401 1555 1555 2.18
LINK OD2 ASP A 92 MN MN A 402 1555 1555 2.27
LINK OD1 ASN A 124 MN MN A 402 1555 1555 2.18
LINK NE2 HIS A 173 MN MN A 402 1555 1555 2.16
LINK ND1 HIS A 248 MN MN A 402 1555 1555 2.24
LINK MN MN A 401 O3 PO4 A 404 1555 1555 2.38
LINK MN MN A 401 O HOH A 633 1555 1555 2.23
LINK MN MN A 401 O HOH A 634 1555 1555 2.15
LINK MN MN A 402 O4 PO4 A 404 1555 1555 2.08
LINK MN MN A 402 O HOH A 634 1555 1555 2.12
CISPEP 1 ARG A 23 PRO A 24 0 6.16
CISPEP 2 ALA A 57 PRO A 58 0 4.79
CISPEP 3 PRO A 82 PRO A 83 0 7.56
CISPEP 4 ARG A 191 PRO A 192 0 0.64
SITE 1 AC1 7 ASP A 64 HIS A 66 ASP A 92 MN A 402
SITE 2 AC1 7 PO4 A 404 HOH A 633 HOH A 634
SITE 1 AC2 7 ASP A 92 ASN A 124 HIS A 173 HIS A 248
SITE 2 AC2 7 MN A 401 PO4 A 404 HOH A 634
SITE 1 AC3 5 GLY A 215 GLY A 228 ALA A 229 GLU A 230
SITE 2 AC3 5 VAL A 231
SITE 1 AC4 11 HIS A 66 ASP A 92 ARG A 96 ASN A 124
SITE 2 AC4 11 HIS A 125 ARG A 221 HIS A 248 MN A 401
SITE 3 AC4 11 MN A 402 HOH A 633 HOH A 634
SITE 1 AC5 4 PRO A 50 GLU A 54 GLU A 116 PHE A 119
SITE 1 AC6 4 CYS A 127 SER A 129 VAL A 195 HOH A 538
CRYST1 130.788 130.788 47.725 90.00 90.00 120.00 P 32 2 1 6
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 0.007646 0.004414 0.000000 0.00000
SCALE2 0.000000 0.008829 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020953 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
