HEADER HYDROLASE/PROTEIN BINDING 29-MAR-16 5J28
TITLE KI67-PP1G (PROTEIN PHOSPHATASE 1, GAMMA ISOFORM) HOLOENZYME COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: UNP RESIDUES 7-308;
COMPND 6 SYNONYM: PP-1G,PROTEIN PHOSPHATASE 1C CATALYTIC SUBUNIT;
COMPND 7 EC: 3.1.3.16;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ANTIGEN KI-67;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: UNP RESIDUES 496-536;
COMPND 13 ENGINEERED: YES;
COMPND 14 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: PPP1CC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: RP1B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: MKI67;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET-M30 MBP
KEYWDS PP1 GAMMA; REPOMAN, KI-67; PHOSPHATASE, HYDROLASE-PROTEIN BINDING
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.S.KUMAR,W.PETI,R.PAGE
REVDAT 5 27-SEP-23 5J28 1 REMARK
REVDAT 4 18-DEC-19 5J28 1 REMARK
REVDAT 3 27-SEP-17 5J28 1 REMARK
REVDAT 2 12-OCT-16 5J28 1 JRNL
REVDAT 1 05-OCT-16 5J28 0
JRNL AUTH G.S.KUMAR,E.GOKHAN,S.DE MUNTER,M.BOLLEN,P.VAGNARELLI,W.PETI,
JRNL AUTH 2 R.PAGE
JRNL TITL THE KI-67 AND REPOMAN MITOTIC PHOSPHATASES ASSEMBLE VIA AN
JRNL TITL 2 IDENTICAL, YET NOVEL MECHANISM.
JRNL REF ELIFE V. 5 2016
JRNL REFN ESSN 2050-084X
JRNL PMID 27572260
JRNL DOI 10.7554/ELIFE.16539
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 64920
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 38.6454 - 4.8179 0.97 4534 145 0.1386 0.2018
REMARK 3 2 4.8179 - 3.8252 0.97 4504 143 0.1209 0.1199
REMARK 3 3 3.8252 - 3.3420 0.97 4505 138 0.1449 0.1839
REMARK 3 4 3.3420 - 3.0366 0.97 4490 142 0.1631 0.2185
REMARK 3 5 3.0366 - 2.8190 0.97 4490 142 0.1568 0.1957
REMARK 3 6 2.8190 - 2.6528 0.97 4495 145 0.1706 0.2157
REMARK 3 7 2.6528 - 2.5200 0.97 4481 146 0.1733 0.2256
REMARK 3 8 2.5200 - 2.4103 0.97 4510 144 0.1725 0.1832
REMARK 3 9 2.4103 - 2.3175 0.97 4464 143 0.1819 0.2461
REMARK 3 10 2.3175 - 2.2376 0.97 4479 141 0.1990 0.2412
REMARK 3 11 2.2376 - 2.1676 0.97 4465 144 0.1987 0.2332
REMARK 3 12 2.1676 - 2.1057 0.97 4501 142 0.2013 0.2312
REMARK 3 13 2.1057 - 2.0502 0.97 4500 141 0.2077 0.2533
REMARK 3 14 2.0502 - 2.0002 0.97 4470 142 0.2159 0.2797
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.230
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 : 0.007 5283
REMARK 3 ANGLE : 0.861 7156
REMARK 3 CHIRALITY : 0.047 770
REMARK 3 PLANARITY : 0.005 946
REMARK 3 DIHEDRAL : 11.732 3160
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5J28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219710.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL, NON FIXED EXIT SLIT
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS NOV 3, 2014
REMARK 200 DATA SCALING SOFTWARE : AIMLESS NOV 3, 2014
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64993
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.331
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 10.30
REMARK 200 R MERGE FOR SHELL (I) : 0.08610
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 5INB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M SODIUM MALONATE PH 4.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 68.90567
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 137.81133
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 103.35850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 172.26417
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 34.45283
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
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: 2690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 4
REMARK 465 HIS A 5
REMARK 465 MET A 6
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 GLY B 4
REMARK 465 HIS B 5
REMARK 465 MET B 6
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 GLY C 491
REMARK 465 ALA C 492
REMARK 465 MET C 493
REMARK 465 GLY C 494
REMARK 465 TYR C 495
REMARK 465 SER C 496
REMARK 465 GLU C 497
REMARK 465 GLY C 498
REMARK 465 ILE C 499
REMARK 465 PRO C 500
REMARK 465 LEU C 501
REMARK 465 LYS C 502
REMARK 465 ARG C 536
REMARK 465 GLY D 491
REMARK 465 ALA D 492
REMARK 465 MET D 493
REMARK 465 GLY D 494
REMARK 465 TYR D 495
REMARK 465 SER D 496
REMARK 465 GLU D 497
REMARK 465 GLY D 498
REMARK 465 ILE D 499
REMARK 465 PRO D 500
REMARK 465 LEU D 501
REMARK 465 LYS D 502
REMARK 465 ARG D 536
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 GLN A 31 CD OE1 NE2
REMARK 470 LEU A 40 CD1 CD2
REMARK 470 GLU A 56 CD OE1 OE2
REMARK 470 LYS A 98 CD CE NZ
REMARK 470 LYS A 147 CD CE NZ
REMARK 470 LYS A 211 CD CE NZ
REMARK 470 LYS A 260 CE NZ
REMARK 470 LYS B 23 CD CE NZ
REMARK 470 GLN B 29 CG CD OE1 NE2
REMARK 470 GLN B 31 CG CD OE1 NE2
REMARK 470 LYS B 41 CD CE NZ
REMARK 470 GLU B 56 CD OE1 OE2
REMARK 470 LYS B 98 CD CE NZ
REMARK 470 ILE B 133 CD1
REMARK 470 LYS B 147 CD CE NZ
REMARK 470 GLU B 184 CG CD OE1 OE2
REMARK 470 LYS B 211 CD CE NZ
REMARK 470 LYS B 260 CE NZ
REMARK 470 ARG C 503 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 504 CG CD NE CZ NH1 NH2
REMARK 470 MET C 525 CG SD CE
REMARK 470 LYS C 528 CG CD CE NZ
REMARK 470 THR C 534 OG1 CG2
REMARK 470 LYS C 535 CG CD CE NZ
REMARK 470 ARG D 503 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 504 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 505 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 511 CG ND1 CD2 CE1 NE2
REMARK 470 LEU D 516 CG CD1 CD2
REMARK 470 ASP D 518 CG OD1 OD2
REMARK 470 ASN D 520 CG OD1 ND2
REMARK 470 LEU D 521 CG CD1 CD2
REMARK 470 LYS D 528 CG CD CE NZ
REMARK 470 ARG D 529 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 535 CG CD CE NZ
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 A 506 O HOH A 510 1.99
REMARK 500 O HOH A 556 O HOH A 590 2.01
REMARK 500 O HOH A 508 O HOH C 612 2.11
REMARK 500 O HOH A 581 O HOH A 584 2.14
REMARK 500 O HOH A 532 O HOH A 595 2.15
REMARK 500 O HOH B 585 O HOH B 591 2.18
REMARK 500 O HOH A 536 O HOH A 578 2.19
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 O HOH A 576 O HOH B 579 5554 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 273 CB CYS A 273 SG -0.107
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 92 70.09 60.65
REMARK 500 ASP A 95 147.91 78.56
REMARK 500 ARG A 96 -48.17 82.36
REMARK 500 TYR A 144 -104.87 -134.22
REMARK 500 SER A 224 -149.95 68.62
REMARK 500 ALA A 247 -124.65 -128.33
REMARK 500 HIS A 248 -12.19 78.39
REMARK 500 CYS A 273 16.06 56.22
REMARK 500 ASP A 277 70.00 -111.50
REMARK 500 ASP B 95 150.23 71.84
REMARK 500 ARG B 96 -47.59 76.52
REMARK 500 TYR B 144 -104.45 -132.19
REMARK 500 ARG B 221 -9.99 -59.42
REMARK 500 SER B 224 -146.98 62.18
REMARK 500 ALA B 247 -125.72 -126.24
REMARK 500 HIS B 248 -14.16 80.02
REMARK 500 ASN B 271 59.53 39.82
REMARK 500 ASP B 277 52.30 -99.97
REMARK 500 ARG C 504 80.40 50.88
REMARK 500 MET C 525 78.14 -118.09
REMARK 500 ASN D 524 32.59 -83.35
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 NA A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 54 OE2
REMARK 620 2 GLU A 167 OE1 94.7
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5INB RELATED DB: PDB
REMARK 900 PP1 GAMMA IN COMPLEX WITH REPOMAN
REMARK 900 RELATED ID: 5IOH RELATED DB: PDB
REMARK 900 PP1 ALPHA IN COMPLEX WITH REPOMAN
REMARK 900 RELATED ID: 25981 RELATED DB: BMRB
REMARK 900 ASSIGNMENTS OF REPOMAN PP1 BINDING DOMAIN
DBREF 5J28 A 7 308 UNP P36873 PP1G_HUMAN 7 308
DBREF 5J28 B 7 308 UNP P36873 PP1G_HUMAN 7 308
DBREF 5J28 C 496 536 UNP P46013 KI67_HUMAN 496 536
DBREF 5J28 D 496 536 UNP P46013 KI67_HUMAN 496 536
SEQADV 5J28 GLY A 4 UNP P36873 EXPRESSION TAG
SEQADV 5J28 HIS A 5 UNP P36873 EXPRESSION TAG
SEQADV 5J28 MET A 6 UNP P36873 EXPRESSION TAG
SEQADV 5J28 GLY B 4 UNP P36873 EXPRESSION TAG
SEQADV 5J28 HIS B 5 UNP P36873 EXPRESSION TAG
SEQADV 5J28 MET B 6 UNP P36873 EXPRESSION TAG
SEQADV 5J28 GLY C 491 UNP P46013 EXPRESSION TAG
SEQADV 5J28 ALA C 492 UNP P46013 EXPRESSION TAG
SEQADV 5J28 MET C 493 UNP P46013 EXPRESSION TAG
SEQADV 5J28 GLY C 494 UNP P46013 EXPRESSION TAG
SEQADV 5J28 TYR C 495 UNP P46013 EXPRESSION TAG
SEQADV 5J28 MET C 525 UNP P46013 THR 525 ENGINEERED MUTATION
SEQADV 5J28 GLY D 491 UNP P46013 EXPRESSION TAG
SEQADV 5J28 ALA D 492 UNP P46013 EXPRESSION TAG
SEQADV 5J28 MET D 493 UNP P46013 EXPRESSION TAG
SEQADV 5J28 GLY D 494 UNP P46013 EXPRESSION TAG
SEQADV 5J28 TYR D 495 UNP P46013 EXPRESSION TAG
SEQADV 5J28 MET D 525 UNP P46013 THR 525 ENGINEERED MUTATION
SEQRES 1 A 305 GLY HIS MET LEU ASN ILE ASP SER ILE ILE GLN ARG LEU
SEQRES 2 A 305 LEU GLU VAL ARG GLY SER LYS PRO GLY LYS ASN VAL GLN
SEQRES 3 A 305 LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS LEU LYS SER
SEQRES 4 A 305 ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU GLU LEU
SEQRES 5 A 305 GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS GLY GLN
SEQRES 6 A 305 TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY GLY PHE
SEQRES 7 A 305 PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP TYR VAL
SEQRES 8 A 305 ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS LEU LEU
SEQRES 9 A 305 LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE PHE LEU
SEQRES 10 A 305 LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN ARG ILE
SEQRES 11 A 305 TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR ASN ILE
SEQRES 12 A 305 LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN CYS LEU
SEQRES 13 A 305 PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE CYS CYS
SEQRES 14 A 305 HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET GLU GLN
SEQRES 15 A 305 ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO ASP GLN
SEQRES 16 A 305 GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO ASP LYS
SEQRES 17 A 305 ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG GLY VAL SER
SEQRES 18 A 305 PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE LEU HIS
SEQRES 19 A 305 LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS GLN VAL
SEQRES 20 A 305 VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG GLN LEU
SEQRES 21 A 305 VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY GLU PHE
SEQRES 22 A 305 ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU THR LEU
SEQRES 23 A 305 MET CYS SER PHE GLN ILE LEU LYS PRO ALA GLU LYS LYS
SEQRES 24 A 305 LYS PRO ASN ALA THR ARG
SEQRES 1 B 305 GLY HIS MET LEU ASN ILE ASP SER ILE ILE GLN ARG LEU
SEQRES 2 B 305 LEU GLU VAL ARG GLY SER LYS PRO GLY LYS ASN VAL GLN
SEQRES 3 B 305 LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS LEU LYS SER
SEQRES 4 B 305 ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU GLU LEU
SEQRES 5 B 305 GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS GLY GLN
SEQRES 6 B 305 TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY GLY PHE
SEQRES 7 B 305 PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP TYR VAL
SEQRES 8 B 305 ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS LEU LEU
SEQRES 9 B 305 LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE PHE LEU
SEQRES 10 B 305 LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN ARG ILE
SEQRES 11 B 305 TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR ASN ILE
SEQRES 12 B 305 LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN CYS LEU
SEQRES 13 B 305 PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE CYS CYS
SEQRES 14 B 305 HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET GLU GLN
SEQRES 15 B 305 ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO ASP GLN
SEQRES 16 B 305 GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO ASP LYS
SEQRES 17 B 305 ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG GLY VAL SER
SEQRES 18 B 305 PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE LEU HIS
SEQRES 19 B 305 LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS GLN VAL
SEQRES 20 B 305 VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG GLN LEU
SEQRES 21 B 305 VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY GLU PHE
SEQRES 22 B 305 ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU THR LEU
SEQRES 23 B 305 MET CYS SER PHE GLN ILE LEU LYS PRO ALA GLU LYS LYS
SEQRES 24 B 305 LYS PRO ASN ALA THR ARG
SEQRES 1 C 46 GLY ALA MET GLY TYR SER GLU GLY ILE PRO LEU LYS ARG
SEQRES 2 C 46 ARG ARG VAL SER PHE GLY GLY HIS LEU ARG PRO GLU LEU
SEQRES 3 C 46 PHE ASP GLU ASN LEU PRO PRO ASN MET PRO LEU LYS ARG
SEQRES 4 C 46 GLY GLU ALA PRO THR LYS ARG
SEQRES 1 D 46 GLY ALA MET GLY TYR SER GLU GLY ILE PRO LEU LYS ARG
SEQRES 2 D 46 ARG ARG VAL SER PHE GLY GLY HIS LEU ARG PRO GLU LEU
SEQRES 3 D 46 PHE ASP GLU ASN LEU PRO PRO ASN MET PRO LEU LYS ARG
SEQRES 4 D 46 GLY GLU ALA PRO THR LYS ARG
HET MLI A 401 7
HET NA A 402 1
HET MLI B 401 7
HETNAM MLI MALONATE ION
HETNAM NA SODIUM ION
FORMUL 5 MLI 2(C3 H2 O4 2-)
FORMUL 6 NA NA 1+
FORMUL 8 HOH *232(H2 O)
HELIX 1 AA1 ASN A 8 LEU A 17 1 10
HELIX 2 AA2 GLU A 18 SER A 22 5 5
HELIX 3 AA3 GLN A 31 GLN A 49 1 19
HELIX 4 AA4 GLN A 68 GLY A 80 1 13
HELIX 5 AA5 GLN A 99 TYR A 114 1 16
HELIX 6 AA6 CYS A 127 ARG A 132 1 6
HELIX 7 AA7 GLY A 135 TYR A 144 1 10
HELIX 8 AA8 ASN A 145 ASN A 157 1 13
HELIX 9 AA9 MET A 183 ARG A 188 1 6
HELIX 10 AB1 GLY A 199 SER A 207 1 9
HELIX 11 AB2 GLY A 228 ASP A 240 1 13
HELIX 12 AB3 ASN A 271 GLU A 275 5 5
HELIX 13 AB4 ASN B 8 LEU B 17 1 10
HELIX 14 AB5 GLU B 18 SER B 22 5 5
HELIX 15 AB6 GLN B 31 GLN B 49 1 19
HELIX 16 AB7 GLN B 68 GLY B 80 1 13
HELIX 17 AB8 GLN B 99 TYR B 114 1 16
HELIX 18 AB9 CYS B 127 ARG B 132 1 6
HELIX 19 AC1 GLY B 135 TYR B 144 1 10
HELIX 20 AC2 ASN B 145 ASN B 157 1 13
HELIX 21 AC3 MET B 183 ARG B 188 1 6
HELIX 22 AC4 GLY B 199 SER B 207 1 9
HELIX 23 AC5 GLY B 228 ASP B 240 1 13
HELIX 24 AC6 ASN B 271 GLU B 275 5 5
SHEET 1 AA1 6 LEU A 52 LEU A 55 0
SHEET 2 AA1 6 ALA A 162 VAL A 165 1 O ILE A 164 N LEU A 53
SHEET 3 AA1 6 ILE A 169 CYS A 172 -1 O CYS A 171 N ALA A 163
SHEET 4 AA1 6 LEU A 243 ARG A 246 1 O CYS A 245 N PHE A 170
SHEET 5 AA1 6 LEU A 263 LEU A 266 1 O LEU A 266 N ARG A 246
SHEET 6 AA1 6 TYR A 255 PHE A 258 -1 N GLU A 256 O THR A 265
SHEET 1 AA2 6 PHE A 118 LEU A 120 0
SHEET 2 AA2 6 TYR A 87 PHE A 89 1 N PHE A 89 O PHE A 119
SHEET 3 AA2 6 LEU A 59 CYS A 62 1 N CYS A 62 O LEU A 88
SHEET 4 AA2 6 GLY A 280 VAL A 285 -1 O VAL A 285 N LEU A 59
SHEET 5 AA2 6 MET A 290 PRO A 298 -1 O LEU A 296 N GLY A 280
SHEET 6 AA2 6 SER C 507 PHE C 508 1 O SER C 507 N CYS A 291
SHEET 1 AA3 6 PHE A 118 LEU A 120 0
SHEET 2 AA3 6 TYR A 87 PHE A 89 1 N PHE A 89 O PHE A 119
SHEET 3 AA3 6 LEU A 59 CYS A 62 1 N CYS A 62 O LEU A 88
SHEET 4 AA3 6 GLY A 280 VAL A 285 -1 O VAL A 285 N LEU A 59
SHEET 5 AA3 6 MET A 290 PRO A 298 -1 O LEU A 296 N GLY A 280
SHEET 6 AA3 6 GLU C 515 PHE C 517 1 O GLU C 515 N ILE A 295
SHEET 1 AA4 3 ASP A 208 PRO A 209 0
SHEET 2 AA4 3 PHE A 225 PHE A 227 1 O PHE A 227 N ASP A 208
SHEET 3 AA4 3 TRP A 216 GLU A 218 -1 N GLY A 217 O THR A 226
SHEET 1 AA5 6 LEU B 52 LEU B 55 0
SHEET 2 AA5 6 ALA B 162 VAL B 165 1 O ILE B 164 N LEU B 55
SHEET 3 AA5 6 ILE B 169 CYS B 172 -1 O CYS B 171 N ALA B 163
SHEET 4 AA5 6 LEU B 243 ARG B 246 1 O CYS B 245 N PHE B 170
SHEET 5 AA5 6 LEU B 263 LEU B 266 1 O LEU B 266 N ARG B 246
SHEET 6 AA5 6 TYR B 255 PHE B 258 -1 N PHE B 258 O LEU B 263
SHEET 1 AA6 6 PHE B 118 LEU B 120 0
SHEET 2 AA6 6 TYR B 87 PHE B 89 1 N PHE B 89 O PHE B 119
SHEET 3 AA6 6 LEU B 59 CYS B 62 1 N LYS B 60 O LEU B 88
SHEET 4 AA6 6 GLY B 280 VAL B 285 -1 O VAL B 285 N LEU B 59
SHEET 5 AA6 6 MET B 290 PRO B 298 -1 O LEU B 296 N GLY B 280
SHEET 6 AA6 6 SER D 507 PHE D 508 1 O SER D 507 N CYS B 291
SHEET 1 AA7 6 PHE B 118 LEU B 120 0
SHEET 2 AA7 6 TYR B 87 PHE B 89 1 N PHE B 89 O PHE B 119
SHEET 3 AA7 6 LEU B 59 CYS B 62 1 N LYS B 60 O LEU B 88
SHEET 4 AA7 6 GLY B 280 VAL B 285 -1 O VAL B 285 N LEU B 59
SHEET 5 AA7 6 MET B 290 PRO B 298 -1 O LEU B 296 N GLY B 280
SHEET 6 AA7 6 GLU D 515 PHE D 517 1 O GLU D 515 N ILE B 295
SHEET 1 AA8 3 ASP B 208 PRO B 209 0
SHEET 2 AA8 3 PHE B 225 PHE B 227 1 O PHE B 225 N ASP B 208
SHEET 3 AA8 3 TRP B 216 GLU B 218 -1 N GLY B 217 O THR B 226
LINK OE2 GLU A 54 NA NA A 402 1555 1555 2.98
LINK OE1 GLU A 167 NA NA A 402 1555 1555 2.74
CISPEP 1 ALA A 57 PRO A 58 0 1.58
CISPEP 2 PRO A 82 PRO A 83 0 -1.06
CISPEP 3 ARG A 191 PRO A 192 0 -2.04
CISPEP 4 ALA B 57 PRO B 58 0 0.84
CISPEP 5 PRO B 82 PRO B 83 0 5.51
CISPEP 6 ARG B 191 PRO B 192 0 -1.03
SITE 1 AC1 11 ASP A 64 HIS A 66 ASP A 92 ARG A 221
SITE 2 AC1 11 HIS A 248 TYR A 272 HOH A 514 HOH A 526
SITE 3 AC1 11 HOH A 528 GLU B 218 ASP B 220
SITE 1 AC2 3 GLU A 54 ILE A 164 GLU A 167
SITE 1 AC3 10 GLU A 218 ASP A 220 ASP B 64 HIS B 66
SITE 2 AC3 10 ASP B 92 ARG B 221 HIS B 248 TYR B 272
SITE 3 AC3 10 HOH B 527 HOH B 528
CRYST1 90.832 90.832 206.717 90.00 90.00 120.00 P 61 12
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 0.011009 0.006356 0.000000 0.00000
SCALE2 0.000000 0.012712 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004838 0.00000
(ATOM LINES ARE NOT SHOWN.)
END