HEADER HYDROLASE 28-JAN-04 1S70
TITLE COMPLEX BETWEEN PROTEIN SER/THR PHOSPHATASE-1 (DELTA) AND THE MYOSIN
TITLE 2 PHOSPHATASE TARGETING SUBUNIT 1 (MYPT1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE PROTEIN PHOSPHATASE PP1-BETA (OR DELTA)
COMPND 3 CATALYTIC SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: PP-1B;
COMPND 6 EC: 3.1.3.16;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: 130 KDA MYOSIN-BINDING SUBUNIT OF SMOOTH MUSCLE MYOSIN
COMPND 11 PHOPHATASE (M130);
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: N-TERMINAL AA 1 TO 299;
COMPND 14 EC: 3.1.3.53;
COMPND 15 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: PPP1CB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTYB12 IMPACT;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 12 ORGANISM_COMMON: CHICKEN;
SOURCE 13 ORGANISM_TAXID: 9031;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PACYC184-T7
KEYWDS MYOSIN PHOSPHATASE, MYPT1, PP1, MYOSIN REGULATION, DEPOSPHORYLATION,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.KERFF,M.TERRAK,R.DOMINGUEZ
REVDAT 8 23-AUG-23 1S70 1 REMARK
REVDAT 7 27-OCT-21 1S70 1 REMARK SEQADV LINK
REVDAT 6 24-FEB-09 1S70 1 VERSN
REVDAT 5 05-DEC-06 1S70 1 REMARK
REVDAT 4 02-AUG-05 1S70 1 AUTHOR KEYWDS
REVDAT 3 25-JAN-05 1S70 1 AUTHOR KEYWDS REMARK
REVDAT 2 20-JUL-04 1S70 1 AUTHOR
REVDAT 1 22-JUN-04 1S70 0
JRNL AUTH M.TERRAK,F.KERFF,K.LANGSETMO,T.TAO,R.DOMINGUEZ
JRNL TITL STRUCTURAL BASIS OF PROTEIN PHOSPHATASE 1 REGULATION
JRNL REF NATURE V. 429 780 2004
JRNL REFN ISSN 0028-0836
JRNL PMID 15164081
JRNL DOI 10.1038/NATURE02582
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2713055.140
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.1
REMARK 3 NUMBER OF REFLECTIONS : 18135
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 SET) : 0.223
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 927
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2302
REMARK 3 BIN R VALUE (WORKING SET) : 0.3930
REMARK 3 BIN FREE R VALUE : 0.4210
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 151
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4743
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 227
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -23.22000
REMARK 3 B22 (A**2) : -23.22000
REMARK 3 B33 (A**2) : 46.44000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM SIGMAA (A) : 0.79
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.59
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.84
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 5.020 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 7.420 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.260 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.670 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 81.20
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : PEG.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : PEG.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S70 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021446.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-03
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : BENT GE(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18135
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 48.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.1
REMARK 200 DATA REDUNDANCY : 13.60
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
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: AMORE
REMARK 200 STARTING MODEL: 1FJM FOR MOLECULE 1 AND 3 ANKYRIN REPEATS FROM
REMARK 200 1IHB FOR MOLECULE 2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000 MONOMETHYLETHER, GLYCEROL,
REMARK 280 NH4CL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 120.87650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.59400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.59400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 181.31475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.59400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.59400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 60.43825
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.59400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.59400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 181.31475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.59400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.59400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 60.43825
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 120.87650
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: 5740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 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 ALA A -1
REMARK 465 GLY A 0
REMARK 465 LEU A 310
REMARK 465 ASN A 311
REMARK 465 SER A 312
REMARK 465 GLY A 313
REMARK 465 ARG A 314
REMARK 465 PRO A 315
REMARK 465 VAL A 316
REMARK 465 THR A 317
REMARK 465 PRO A 318
REMARK 465 PRO A 319
REMARK 465 ARG A 320
REMARK 465 THR A 321
REMARK 465 ALA A 322
REMARK 465 ASN A 323
REMARK 465 PRO A 324
REMARK 465 PRO A 325
REMARK 465 LYS A 326
REMARK 465 LYS A 327
REMARK 465 ARG A 328
REMARK 465 SER B 292
REMARK 465 GLU B 293
REMARK 465 LYS B 294
REMARK 465 ARG B 295
REMARK 465 GLU B 296
REMARK 465 LYS B 297
REMARK 465 LYS B 298
REMARK 465 SER B 299
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 B 391 O HOH B 391 7466 1.92
REMARK 500 O HOH B 320 O HOH B 320 8665 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 26 C - N - CA ANGL. DEV. = 15.0 DEGREES
REMARK 500 PRO B 26 C - N - CD ANGL. DEV. = -13.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 MET A 2 149.68 -23.21
REMARK 500 ALA A 3 -141.91 85.93
REMARK 500 ASP A 4 -170.97 60.45
REMARK 500 ASP A 92 71.43 52.91
REMARK 500 ASP A 95 148.71 72.74
REMARK 500 ARG A 96 -72.08 74.82
REMARK 500 GLU A 126 41.88 -108.17
REMARK 500 PHE A 144 -111.61 -147.98
REMARK 500 ASP A 166 27.98 41.37
REMARK 500 CYS A 172 147.29 -171.67
REMARK 500 PRO A 178 4.52 -66.93
REMARK 500 ARG A 188 32.45 -87.02
REMARK 500 SER A 207 161.41 -35.63
REMARK 500 SER A 224 -159.61 52.53
REMARK 500 PHE A 225 -150.47 -127.98
REMARK 500 ALA A 247 -124.06 -128.79
REMARK 500 HIS A 248 -34.62 77.26
REMARK 500 LYS A 260 60.27 69.84
REMARK 500 ARG A 261 18.40 57.01
REMARK 500 MET A 282 117.13 -167.59
REMARK 500 LEU A 289 27.95 86.32
REMARK 500 GLU A 300 17.34 54.40
REMARK 500 LYS A 301 62.47 -106.11
REMARK 500 ASP B 5 -90.32 -36.99
REMARK 500 GLU B 12 16.41 -60.00
REMARK 500 SER B 20 -179.24 -53.37
REMARK 500 GLU B 21 50.67 -68.76
REMARK 500 LEU B 24 108.46 -56.12
REMARK 500 GLU B 25 102.94 -26.31
REMARK 500 PRO B 26 25.44 -68.80
REMARK 500 PRO B 27 -104.26 -94.80
REMARK 500 VAL B 28 -46.65 -134.90
REMARK 500 LYS B 30 91.74 -40.02
REMARK 500 LYS B 32 28.19 -79.06
REMARK 500 ASP B 52 65.92 -68.85
REMARK 500 ASN B 67 46.37 -89.14
REMARK 500 ASN B 70 -171.11 -63.73
REMARK 500 ASN B 104 6.57 -64.62
REMARK 500 ASN B 186 -76.08 -56.43
REMARK 500 ARG B 194 133.87 -38.38
REMARK 500 ALA B 196 -38.63 -27.88
REMARK 500 LYS B 197 -79.92 -84.61
REMARK 500 ASP B 224 105.76 -44.31
REMARK 500 PRO B 235 -3.41 -57.22
REMARK 500 GLU B 245 -73.90 -38.41
REMARK 500 ASP B 257 93.83 -57.88
REMARK 500 ASP B 270 -73.81 -60.69
REMARK 500 ALA B 272 27.54 -73.27
REMARK 500 ASP B 273 -27.95 -23.35
REMARK 500 ASP B 275 -89.09 20.09
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
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 OD1
REMARK 620 2 HIS A 66 NE2 77.1
REMARK 620 3 ASP A 92 OD2 72.2 77.5
REMARK 620 N 1 2
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 92 OD2
REMARK 620 2 ASN A 124 OD1 88.9
REMARK 620 3 HIS A 173 NE2 81.8 69.0
REMARK 620 4 HIS A 248 ND1 158.2 88.2 77.0
REMARK 620 N 1 2 3
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 PGE A 331
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FJM RELATED DB: PDB
REMARK 900 PROTEIN SER/THR PHOSPHATASE-1 (ALPHA) COMPLEXED WITH MICROCYSTIN-LR
REMARK 900 TOXIN
REMARK 900 RELATED ID: 1IT6 RELATED DB: PDB
REMARK 900 PROTEIN SER/THR PHOSPHATASE-1 (GAMMA) COMPLEXED WITH CALICULIN A
REMARK 900 RELATED ID: 1JK7 RELATED DB: PDB
REMARK 900 PROTEIN SER/THR PHOSPHATASE-1 (GAMMA) COMPLEXED WITH THE TUMOR-
REMARK 900 PROMOTER OKADAIC ACID
DBREF 1S70 A 2 328 UNP P62140 PP1B_HUMAN 1 327
DBREF 1S70 B 1 299 UNP Q90624 Q90624_CHICK 1 299
SEQADV 1S70 ALA A -1 UNP P62140 ENGINEERED MUTATION
SEQADV 1S70 GLY A 0 UNP P62140 ENGINEERED MUTATION
SEQADV 1S70 HIS A 1 UNP P62140 ENGINEERED MUTATION
SEQRES 1 A 330 ALA GLY HIS MET ALA ASP GLY GLU LEU ASN VAL ASP SER
SEQRES 2 A 330 LEU ILE THR ARG LEU LEU GLU VAL ARG GLY CYS ARG PRO
SEQRES 3 A 330 GLY LYS ILE VAL GLN MET THR GLU ALA GLU VAL ARG GLY
SEQRES 4 A 330 LEU CYS ILE LYS SER ARG GLU ILE PHE LEU SER GLN PRO
SEQRES 5 A 330 ILE LEU LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY
SEQRES 6 A 330 ASP ILE HIS GLY GLN TYR THR ASP LEU LEU ARG LEU PHE
SEQRES 7 A 330 GLU TYR GLY GLY PHE PRO PRO GLU ALA ASN TYR LEU PHE
SEQRES 8 A 330 LEU GLY ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU
SEQRES 9 A 330 THR ILE CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO
SEQRES 10 A 330 GLU ASN PHE PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA
SEQRES 11 A 330 SER ILE ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS
SEQRES 12 A 330 ARG ARG PHE ASN ILE LYS LEU TRP LYS THR PHE THR ASP
SEQRES 13 A 330 CYS PHE ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU
SEQRES 14 A 330 LYS ILE PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU
SEQRES 15 A 330 GLN SER MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR
SEQRES 16 A 330 ASP VAL PRO ASP THR GLY LEU LEU CYS ASP LEU LEU TRP
SEQRES 17 A 330 SER ASP PRO ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN
SEQRES 18 A 330 ASP ARG GLY VAL SER PHE THR PHE GLY ALA ASP VAL VAL
SEQRES 19 A 330 SER LYS PHE LEU ASN ARG HIS ASP LEU ASP LEU ILE CYS
SEQRES 20 A 330 ARG ALA HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE
SEQRES 21 A 330 ALA LYS ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN
SEQRES 22 A 330 TYR CYS GLY GLU PHE ASP ASN ALA GLY GLY MET MET SER
SEQRES 23 A 330 VAL ASP GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS
SEQRES 24 A 330 PRO SER GLU LYS LYS ALA LYS TYR GLN TYR GLY GLY LEU
SEQRES 25 A 330 ASN SER GLY ARG PRO VAL THR PRO PRO ARG THR ALA ASN
SEQRES 26 A 330 PRO PRO LYS LYS ARG
SEQRES 1 B 299 MET LYS MET ALA ASP ALA LYS GLN LYS ARG ASN GLU GLN
SEQRES 2 B 299 LEU LYS ARG TRP ILE GLY SER GLU THR ASP LEU GLU PRO
SEQRES 3 B 299 PRO VAL VAL LYS ARG LYS LYS THR LYS VAL LYS PHE ASP
SEQRES 4 B 299 ASP GLY ALA VAL PHE LEU ALA ALA CYS SER SER GLY ASP
SEQRES 5 B 299 THR GLU GLU VAL LEU ARG LEU LEU GLU ARG GLY ALA ASP
SEQRES 6 B 299 ILE ASN TYR ALA ASN VAL ASP GLY LEU THR ALA LEU HIS
SEQRES 7 B 299 GLN ALA CYS ILE ASP ASP ASN VAL ASP MET VAL LYS PHE
SEQRES 8 B 299 LEU VAL GLU ASN GLY ALA ASN ILE ASN GLN PRO ASP ASN
SEQRES 9 B 299 GLU GLY TRP ILE PRO LEU HIS ALA ALA ALA SER CYS GLY
SEQRES 10 B 299 TYR LEU ASP ILE ALA GLU TYR LEU ILE SER GLN GLY ALA
SEQRES 11 B 299 HIS VAL GLY ALA VAL ASN SER GLU GLY ASP THR PRO LEU
SEQRES 12 B 299 ASP ILE ALA GLU GLU GLU ALA MET GLU GLU LEU LEU GLN
SEQRES 13 B 299 ASN GLU VAL ASN ARG GLN GLY VAL ASP ILE GLU ALA ALA
SEQRES 14 B 299 ARG LYS GLU GLU GLU ARG ILE MET LEU ARG ASP ALA ARG
SEQRES 15 B 299 GLN TRP LEU ASN SER GLY HIS ILE ASN ASP VAL ARG HIS
SEQRES 16 B 299 ALA LYS SER GLY GLY THR ALA LEU HIS VAL ALA ALA ALA
SEQRES 17 B 299 LYS GLY TYR THR GLU VAL LEU LYS LEU LEU ILE GLN ALA
SEQRES 18 B 299 ARG TYR ASP VAL ASN ILE LYS ASP TYR ASP GLY TRP THR
SEQRES 19 B 299 PRO LEU HIS ALA ALA ALA HIS TRP GLY LYS GLU GLU ALA
SEQRES 20 B 299 CYS ARG ILE LEU VAL GLU ASN LEU CYS ASP MET GLU ALA
SEQRES 21 B 299 VAL ASN LYS VAL GLY GLN THR ALA PHE ASP VAL ALA ASP
SEQRES 22 B 299 GLU ASP ILE LEU GLY TYR LEU GLU GLU LEU GLN LYS LYS
SEQRES 23 B 299 GLN ASN LEU LEU HIS SER GLU LYS ARG GLU LYS LYS SER
HET MN A 400 1
HET MN A 401 1
HET PGE A 331 10
HETNAM MN MANGANESE (II) ION
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 3 MN 2(MN 2+)
FORMUL 5 PGE C6 H14 O4
FORMUL 6 HOH *227(H2 O)
HELIX 1 1 ASN A 8 GLU A 18 1 11
HELIX 2 2 THR A 31 LEU A 47 1 17
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 ARG A 132 1 6
HELIX 6 6 GLY A 135 PHE A 144 1 10
HELIX 7 7 ASN A 145 ASN A 157 1 13
HELIX 8 8 MET A 183 ARG A 188 1 6
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 MET B 3 SER B 20 1 18
HELIX 13 13 ASP B 39 GLY B 51 1 13
HELIX 14 14 ASP B 52 GLY B 63 1 12
HELIX 15 15 THR B 75 ASP B 83 1 9
HELIX 16 16 ASN B 85 ASN B 95 1 11
HELIX 17 17 ILE B 108 GLY B 117 1 10
HELIX 18 18 TYR B 118 GLN B 128 1 11
HELIX 19 19 THR B 141 ALA B 146 1 6
HELIX 20 20 GLU B 148 GLY B 163 1 16
HELIX 21 21 ASP B 165 GLY B 188 1 24
HELIX 22 22 THR B 201 GLY B 210 1 10
HELIX 23 23 TYR B 211 GLN B 220 1 10
HELIX 24 24 THR B 234 TRP B 242 1 9
HELIX 25 25 LYS B 244 ASN B 254 1 11
HELIX 26 26 GLU B 274 ILE B 276 5 3
HELIX 27 27 LEU B 277 GLN B 287 1 11
SHEET 1 A 6 LEU A 52 LEU A 55 0
SHEET 2 A 6 ALA A 162 VAL A 165 1 O ALA A 162 N LEU A 53
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 LEU A 243 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 PHE A 258 O LEU A 263
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 CYS A 62 O LEU A 88
SHEET 4 B 6 MET A 283 VAL A 285 -1 O VAL A 285 N LEU A 59
SHEET 5 B 6 MET A 290 PHE A 293 -1 O SER A 292 N SER A 284
SHEET 6 B 6 LYS B 37 PHE B 38 1 O LYS B 37 N CYS A 291
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 227 N ASP A 208
SHEET 3 C 3 TRP A 216 GLU A 218 -1 N GLY A 217 O THR A 226
LINK OD1 ASP A 64 MN MN A 401 1555 1555 2.46
LINK NE2 HIS A 66 MN MN A 401 1555 1555 2.54
LINK OD2 ASP A 92 MN MN A 400 1555 1555 2.37
LINK OD2 ASP A 92 MN MN A 401 1555 1555 2.34
LINK OD1 ASN A 124 MN MN A 400 1555 1555 2.15
LINK NE2 HIS A 173 MN MN A 400 1555 1555 2.28
LINK ND1 HIS A 248 MN MN A 400 1555 1555 2.24
CISPEP 1 ALA A 57 PRO A 58 0 -0.25
CISPEP 2 PRO A 82 PRO A 83 0 0.05
CISPEP 3 ARG A 191 PRO A 192 0 0.17
SITE 1 AC1 6 ASP A 92 ASN A 124 HIS A 173 HIS A 248
SITE 2 AC1 6 MN A 401 HOH A 415
SITE 1 AC2 5 ASP A 64 HIS A 66 ASP A 92 MN A 400
SITE 2 AC2 5 HOH A 415
SITE 1 AC3 10 VAL A 19 GLY A 21 CYS A 22 PRO A 24
SITE 2 AC3 10 GLY A 25 LYS A 26 THR A 70 GLU A 77
SITE 3 AC3 10 GLN A 99 VAL B 264
CRYST1 75.188 75.188 241.753 90.00 90.00 90.00 P 43 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 0.013300 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013300 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004136 0.00000
(ATOM LINES ARE NOT SHOWN.)
END