HEADER HYDROLASE/TOXIN 17-SEP-06 2IE3
TITLE STRUCTURE OF THE PROTEIN PHOSPHATASE 2A CORE ENZYME BOUND TO TUMOR-
TITLE 2 INDUCING TOXINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN PHOSPHATASE 2, REGULATORY SUBUNIT A (PR 65), ALPHA
COMPND 3 ISOFORM;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: SCAFFOLDING SUBUNIT;
COMPND 6 SYNONYM: PROTEIN PHOSPHATASE 2A;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 2A CATALYTIC SUBUNIT
COMPND 10 ALPHA ISOFORM;
COMPND 11 CHAIN: C;
COMPND 12 FRAGMENT: CATALYTIC SUBUNIT;
COMPND 13 SYNONYM: SERINE/THREONINE PROTEIN PHOSPHATASE; PP2A-ALPHA;
COMPND 14 REPLICATION PROTEIN C; RP-C;
COMPND 15 EC: 3.1.3.16;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 3;
COMPND 18 MOLECULE: MICROCYSTIN LR;
COMPND 19 CHAIN: I;
COMPND 20 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: PPP2R1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: PPP2CA;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: HI-5;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: CYANOBACTERIA;
SOURCE 24 ORGANISM_TAXID: 1117
KEYWDS HEAT REPEAT, SIGNALING PROTEIN, HYDROLASE-TOXIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XING,Y.XU,Y.CHEN,P.D.JEFFREY,Y.CHAO,Y.SHI
REVDAT 7 15-NOV-23 2IE3 1 REMARK SEQADV LINK ATOM
REVDAT 6 27-JUL-11 2IE3 1 HETNAM HETSYN REMARK
REVDAT 5 13-JUL-11 2IE3 1 VERSN
REVDAT 4 25-AUG-10 2IE3 1 FORMUL HET HETATM HETNAM
REVDAT 4 2 1 MODRES REMARK SEQRES
REVDAT 3 24-FEB-09 2IE3 1 VERSN
REVDAT 2 14-NOV-06 2IE3 1 LINK ATOM REMARK
REVDAT 1 07-NOV-06 2IE3 0
JRNL AUTH Y.XING,Y.XU,Y.CHEN,P.D.JEFFREY,Y.CHAO,Z.LIN,Z.LI,S.STRACK,
JRNL AUTH 2 J.B.STOCK,Y.SHI
JRNL TITL STRUCTURE OF PROTEIN PHOSPHATASE 2A CORE ENZYME BOUND TO
JRNL TITL 2 TUMOR-INDUCING TOXINS
JRNL REF CELL(CAMBRIDGE,MASS.) V. 127 341 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 17055435
JRNL DOI 10.1016/J.CELL.2006.09.025
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 42363
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) : 0.221
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 40267
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 0
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) : 7.55300
REMARK 3 B22 (A**2) : 5.81500
REMARK 3 B33 (A**2) : -13.36800
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.530
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.280 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.668 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.714 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.569 ; 3.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2IE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-06.
REMARK 100 THE DEPOSITION ID IS D_1000039468.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 0.9796
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44149
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 MM LITHIUM SULFATE, 1.5 M AMMONIUM
REMARK 280 SULFATE, 0.1 M TRIS-CL PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 46.53500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 97.54500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 100.95500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.53500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 97.54500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 100.95500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.53500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 97.54500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 100.95500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.53500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 97.54500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 100.95500
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, I
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE MICROCYSTIN LR IS OLIGOPEPTIDE, A MEMBER OF TOXIN CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: MICROCYSTIN LR
REMARK 400 CHAIN: I
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ASP A 5
REMARK 465 GLY A 6
REMARK 465 ASP A 7
REMARK 465 ASP A 8
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 GLU C 3
REMARK 465 LYS C 4
REMARK 465 LEU C 5
REMARK 465 ARG C 294
REMARK 465 ARG C 295
REMARK 465 GLY C 296
REMARK 465 GLU C 297
REMARK 465 PRO C 298
REMARK 465 HIS C 299
REMARK 465 VAL C 300
REMARK 465 THR C 301
REMARK 465 ARG C 302
REMARK 465 ARG C 303
REMARK 465 THR C 304
REMARK 465 PRO C 305
REMARK 465 ASP C 306
REMARK 465 TYR C 307
REMARK 465 PHE C 308
REMARK 465 LEU C 309
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 TYR A 11 N - CA - C ANGL. DEV. = 18.0 DEGREES
REMARK 500 PRO A 12 C - N - CA ANGL. DEV. = -20.1 DEGREES
REMARK 500 PRO A 12 C - N - CD ANGL. DEV. = 13.3 DEGREES
REMARK 500 ARG C 206 N - CA - C ANGL. DEV. = -16.9 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 ALA A 14 -6.95 -53.08
REMARK 500 ARG A 21 -118.44 -79.14
REMARK 500 ASN A 22 7.59 -164.14
REMARK 500 GLU A 23 -155.07 -63.29
REMARK 500 LYS A 34 44.19 -98.26
REMARK 500 SER A 36 38.50 -71.92
REMARK 500 THR A 37 -39.83 -132.25
REMARK 500 ASP A 57 -130.01 -76.78
REMARK 500 THR A 58 62.61 22.47
REMARK 500 ASP A 61 83.26 -31.38
REMARK 500 ASP A 63 -66.25 42.71
REMARK 500 THR A 75 59.35 -115.50
REMARK 500 LEU A 79 0.51 -52.63
REMARK 500 VAL A 99 -157.66 -77.95
REMARK 500 GLU A 100 -79.15 -104.31
REMARK 500 GLU A 101 112.22 -39.97
REMARK 500 ASP A 139 -79.64 -79.73
REMARK 500 TRP A 140 163.00 -43.25
REMARK 500 LEU A 198 -68.26 -19.73
REMARK 500 SER A 214 41.33 -107.59
REMARK 500 LEU A 222 -39.45 -37.43
REMARK 500 VAL A 244 -54.95 -129.37
REMARK 500 ASP A 254 139.70 -37.54
REMARK 500 ASP A 316 -82.64 -33.13
REMARK 500 ARG A 318 -79.46 -61.43
REMARK 500 GLU A 319 -17.26 -36.66
REMARK 500 ASP A 336 159.39 -49.52
REMARK 500 VAL A 348 -20.16 -153.05
REMARK 500 CYS A 377 106.30 -56.81
REMARK 500 VAL A 394 -72.81 -82.80
REMARK 500 ALA A 415 -85.46 -65.50
REMARK 500 LEU A 429 -70.49 -77.13
REMARK 500 ALA A 431 -80.44 -51.67
REMARK 500 ILE A 482 -50.52 -122.90
REMARK 500 GLN A 514 -36.68 -38.40
REMARK 500 PRO A 549 -5.46 -55.24
REMARK 500 ASP A 570 153.80 -46.84
REMARK 500 SER A 587 6.25 81.10
REMARK 500 MET C 83 38.35 -92.25
REMARK 500 ASP C 85 55.46 73.01
REMARK 500 ASP C 88 160.95 71.73
REMARK 500 ARG C 89 -64.49 65.95
REMARK 500 PHE C 129 -35.05 -31.99
REMARK 500 TYR C 137 -161.26 -116.66
REMARK 500 LEU C 186 76.94 -68.46
REMARK 500 ALA C 240 -123.25 -142.50
REMARK 500 HIS C 241 -16.93 64.14
REMARK 500 ASN C 264 65.62 33.87
REMARK 500 ARG C 268 -47.43 -130.49
REMARK 500 ASP C 279 -163.95 -75.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 1ZN I 5 FGA I 6 142.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1ZN I 5 -19.45
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 C 502 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 57 OD2
REMARK 620 2 HIS C 59 NE2 97.5
REMARK 620 3 ASP C 85 OD2 79.7 81.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 85 OD2
REMARK 620 2 ASN C 117 OD1 91.3
REMARK 620 3 HIS C 167 NE2 91.5 78.9
REMARK 620 4 HIS C 241 ND1 165.4 101.4 84.0
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 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IE4 RELATED DB: PDB
DBREF 2IE3 A 1 589 UNP Q96DH3 Q96DH3_HUMAN 1 589
DBREF 2IE3 C 1 309 UNP P67775 PP2AA_HUMAN 1 309
DBREF 2IE3 I 1 7 NOR NOR00109 NOR00109 1 7
SEQADV 2IE3 LEU C 5 UNP P67775 VAL 5 CONFLICT
SEQRES 1 A 589 MET ALA ALA ALA ASP GLY ASP ASP SER LEU TYR PRO ILE
SEQRES 2 A 589 ALA VAL LEU ILE ASP GLU LEU ARG ASN GLU ASP VAL GLN
SEQRES 3 A 589 LEU ARG LEU ASN SER ILE LYS LYS LEU SER THR ILE ALA
SEQRES 4 A 589 LEU ALA LEU GLY VAL GLU ARG THR ARG SER GLU LEU LEU
SEQRES 5 A 589 PRO PHE LEU THR ASP THR ILE TYR ASP GLU ASP GLU VAL
SEQRES 6 A 589 LEU LEU ALA LEU ALA GLU GLN LEU GLY THR PHE THR THR
SEQRES 7 A 589 LEU VAL GLY GLY PRO GLU TYR VAL HIS CYS LEU LEU PRO
SEQRES 8 A 589 PRO LEU GLU SER LEU ALA THR VAL GLU GLU THR VAL VAL
SEQRES 9 A 589 ARG ASP LYS ALA VAL GLU SER LEU ARG ALA ILE SER HIS
SEQRES 10 A 589 GLU HIS SER PRO SER ASP LEU GLU ALA HIS PHE VAL PRO
SEQRES 11 A 589 LEU VAL LYS ARG LEU ALA GLY GLY ASP TRP PHE THR SER
SEQRES 12 A 589 ARG THR SER ALA CYS GLY LEU PHE SER VAL CYS TYR PRO
SEQRES 13 A 589 ARG VAL SER SER ALA VAL LYS ALA GLU LEU ARG GLN TYR
SEQRES 14 A 589 PHE ARG ASN LEU CYS SER ASP ASP THR PRO MET VAL ARG
SEQRES 15 A 589 ARG ALA ALA ALA SER LYS LEU GLY GLU PHE ALA LYS VAL
SEQRES 16 A 589 LEU GLU LEU ASP ASN VAL LYS SER GLU ILE ILE PRO MET
SEQRES 17 A 589 PHE SER ASN LEU ALA SER ASP GLU GLN ASP SER VAL ARG
SEQRES 18 A 589 LEU LEU ALA VAL GLU ALA CYS VAL ASN ILE ALA GLN LEU
SEQRES 19 A 589 LEU PRO GLN GLU ASP LEU GLU ALA LEU VAL MET PRO THR
SEQRES 20 A 589 LEU ARG GLN ALA ALA GLU ASP LYS SER TRP ARG VAL ARG
SEQRES 21 A 589 TYR MET VAL ALA ASP LYS PHE THR GLU LEU GLN LYS ALA
SEQRES 22 A 589 VAL GLY PRO GLU ILE THR LYS THR ASP LEU VAL PRO ALA
SEQRES 23 A 589 PHE GLN ASN LEU MET LYS ASP CYS GLU ALA GLU VAL ARG
SEQRES 24 A 589 ALA ALA ALA SER HIS LYS VAL LYS GLU PHE CYS GLU ASN
SEQRES 25 A 589 LEU SER ALA ASP CYS ARG GLU ASN VAL ILE MET SER GLN
SEQRES 26 A 589 ILE LEU PRO CYS ILE LYS GLU LEU VAL SER ASP ALA ASN
SEQRES 27 A 589 GLN HIS VAL LYS SER ALA LEU ALA SER VAL ILE MET GLY
SEQRES 28 A 589 LEU SER PRO ILE LEU GLY LYS ASP ASN THR ILE GLU HIS
SEQRES 29 A 589 LEU LEU PRO LEU PHE LEU ALA GLN LEU LYS ASP GLU CYS
SEQRES 30 A 589 PRO GLU VAL ARG LEU ASN ILE ILE SER ASN LEU ASP CYS
SEQRES 31 A 589 VAL ASN GLU VAL ILE GLY ILE ARG GLN LEU SER GLN SER
SEQRES 32 A 589 LEU LEU PRO ALA ILE VAL GLU LEU ALA GLU ASP ALA LYS
SEQRES 33 A 589 TRP ARG VAL ARG LEU ALA ILE ILE GLU TYR MET PRO LEU
SEQRES 34 A 589 LEU ALA GLY GLN LEU GLY VAL GLU PHE PHE ASP GLU LYS
SEQRES 35 A 589 LEU ASN SER LEU CYS MET ALA TRP LEU VAL ASP HIS VAL
SEQRES 36 A 589 TYR ALA ILE ARG GLU ALA ALA THR SER ASN LEU LYS LYS
SEQRES 37 A 589 LEU VAL GLU LYS PHE GLY LYS GLU TRP ALA HIS ALA THR
SEQRES 38 A 589 ILE ILE PRO LYS VAL LEU ALA MET SER GLY ASP PRO ASN
SEQRES 39 A 589 TYR LEU HIS ARG MET THR THR LEU PHE CYS ILE ASN VAL
SEQRES 40 A 589 LEU SER GLU VAL CYS GLY GLN ASP ILE THR THR LYS HIS
SEQRES 41 A 589 MET LEU PRO THR VAL LEU ARG MET ALA GLY ASP PRO VAL
SEQRES 42 A 589 ALA ASN VAL ARG PHE ASN VAL ALA LYS SER LEU GLN LYS
SEQRES 43 A 589 ILE GLY PRO ILE LEU ASP ASN SER THR LEU GLN SER GLU
SEQRES 44 A 589 VAL LYS PRO ILE LEU GLU LYS LEU THR GLN ASP GLN ASP
SEQRES 45 A 589 VAL ASP VAL LYS TYR PHE ALA GLN GLU ALA LEU THR VAL
SEQRES 46 A 589 LEU SER LEU ALA
SEQRES 1 C 309 MET ASP GLU LYS LEU PHE THR LYS GLU LEU ASP GLN TRP
SEQRES 2 C 309 ILE GLU GLN LEU ASN GLU CYS LYS GLN LEU SER GLU SER
SEQRES 3 C 309 GLN VAL LYS SER LEU CYS GLU LYS ALA LYS GLU ILE LEU
SEQRES 4 C 309 THR LYS GLU SER ASN VAL GLN GLU VAL ARG CYS PRO VAL
SEQRES 5 C 309 THR VAL CYS GLY ASP VAL HIS GLY GLN PHE HIS ASP LEU
SEQRES 6 C 309 MET GLU LEU PHE ARG ILE GLY GLY LYS SER PRO ASP THR
SEQRES 7 C 309 ASN TYR LEU PHE MET GLY ASP TYR VAL ASP ARG GLY TYR
SEQRES 8 C 309 TYR SER VAL GLU THR VAL THR LEU LEU VAL ALA LEU LYS
SEQRES 9 C 309 VAL ARG TYR ARG GLU ARG ILE THR ILE LEU ARG GLY ASN
SEQRES 10 C 309 HIS GLU SER ARG GLN ILE THR GLN VAL TYR GLY PHE TYR
SEQRES 11 C 309 ASP GLU CYS LEU ARG LYS TYR GLY ASN ALA ASN VAL TRP
SEQRES 12 C 309 LYS TYR PHE THR ASP LEU PHE ASP TYR LEU PRO LEU THR
SEQRES 13 C 309 ALA LEU VAL ASP GLY GLN ILE PHE CYS LEU HIS GLY GLY
SEQRES 14 C 309 LEU SER PRO SER ILE ASP THR LEU ASP HIS ILE ARG ALA
SEQRES 15 C 309 LEU ASP ARG LEU GLN GLU VAL PRO HIS GLU GLY PRO MET
SEQRES 16 C 309 CYS ASP LEU LEU TRP SER ASP PRO ASP ASP ARG GLY GLY
SEQRES 17 C 309 TRP GLY ILE SER PRO ARG GLY ALA GLY TYR THR PHE GLY
SEQRES 18 C 309 GLN ASP ILE SER GLU THR PHE ASN HIS ALA ASN GLY LEU
SEQRES 19 C 309 THR LEU VAL SER ARG ALA HIS GLN LEU VAL MET GLU GLY
SEQRES 20 C 309 TYR ASN TRP CYS HIS ASP ARG ASN VAL VAL THR ILE PHE
SEQRES 21 C 309 SER ALA PRO ASN TYR CYS TYR ARG CYS GLY ASN GLN ALA
SEQRES 22 C 309 ALA ILE MET GLU LEU ASP ASP THR LEU LYS TYR SER PHE
SEQRES 23 C 309 LEU GLN PHE ASP PRO ALA PRO ARG ARG GLY GLU PRO HIS
SEQRES 24 C 309 VAL THR ARG ARG THR PRO ASP TYR PHE LEU
SEQRES 1 I 7 DAL LEU ACB ARG 1ZN FGA DAM
HET DAL I 1 5
HET ACB I 3 9
HET 1ZN I 5 23
HET FGA I 6 9
HET DAM I 7 6
HET MN C 501 1
HET MN C 502 1
HETNAM DAL D-ALANINE
HETNAM ACB 3-METHYL-BETA-D-ASPARTIC ACID
HETNAM 1ZN (2S,3S,4E,6E,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-
HETNAM 2 1ZN 10-PHENYLDECA-4,6-DIENOIC ACID
HETNAM FGA GAMMA-D-GLUTAMIC ACID
HETNAM DAM N-METHYL-ALPHA-BETA-DEHYDROALANINE
HETNAM MN MANGANESE (II) ION
HETSYN ACB (3S)-3-METHYL-D-ASPARTIC ACID; D-METHYL ASPARTIC ACID
HETSYN FGA D-GLUTAMIC ACID
FORMUL 3 DAL C3 H7 N O2
FORMUL 3 ACB C5 H9 N O4
FORMUL 3 1ZN C20 H29 N O3
FORMUL 3 FGA C5 H9 N O4
FORMUL 3 DAM C4 H7 N O2
FORMUL 4 MN 2(MN 2+)
HELIX 1 1 PRO A 12 LEU A 16 5 5
HELIX 2 2 ARG A 28 LYS A 33 1 6
HELIX 3 3 THR A 37 LEU A 42 1 6
HELIX 4 4 GLY A 43 GLU A 50 1 8
HELIX 5 5 GLU A 50 ASP A 57 1 8
HELIX 6 6 ASP A 63 LEU A 73 1 11
HELIX 7 7 GLY A 74 PHE A 76 5 3
HELIX 8 8 GLY A 82 CYS A 88 5 7
HELIX 9 9 LEU A 89 THR A 98 1 10
HELIX 10 10 GLU A 101 HIS A 117 1 17
HELIX 11 11 SER A 120 HIS A 127 1 8
HELIX 12 12 HIS A 127 GLY A 137 1 11
HELIX 13 13 TRP A 140 CYS A 148 1 9
HELIX 14 14 LEU A 150 TYR A 155 1 6
HELIX 15 15 SER A 159 SER A 175 1 17
HELIX 16 16 THR A 178 LEU A 196 1 19
HELIX 17 17 GLU A 197 GLU A 204 1 8
HELIX 18 18 GLU A 204 SER A 214 1 11
HELIX 19 19 GLN A 217 LEU A 235 1 19
HELIX 20 20 PRO A 236 VAL A 244 1 9
HELIX 21 21 VAL A 244 ASP A 254 1 11
HELIX 22 22 SER A 256 LYS A 266 1 11
HELIX 23 23 LYS A 266 GLY A 275 1 10
HELIX 24 24 GLY A 275 ASP A 282 1 8
HELIX 25 25 ASP A 282 MET A 291 1 10
HELIX 26 26 GLU A 295 LYS A 305 1 11
HELIX 27 27 LYS A 305 ASN A 312 1 8
HELIX 28 28 CYS A 317 ILE A 326 1 10
HELIX 29 29 ILE A 326 VAL A 334 1 9
HELIX 30 30 ASN A 338 SER A 347 1 10
HELIX 31 31 VAL A 348 GLY A 351 5 4
HELIX 32 32 LEU A 352 LYS A 374 1 23
HELIX 33 33 CYS A 377 SER A 386 1 10
HELIX 34 34 LEU A 388 ILE A 395 1 8
HELIX 35 35 GLY A 396 GLU A 413 1 18
HELIX 36 36 LYS A 416 GLY A 435 1 20
HELIX 37 37 GLY A 435 LEU A 443 1 9
HELIX 38 38 LEU A 443 TRP A 450 1 8
HELIX 39 39 LEU A 451 ASP A 453 5 3
HELIX 40 40 VAL A 455 ILE A 482 1 28
HELIX 41 41 ILE A 482 MET A 489 1 8
HELIX 42 42 SER A 490 ASP A 492 5 3
HELIX 43 43 ASN A 494 MET A 521 1 28
HELIX 44 44 MET A 521 MET A 528 1 8
HELIX 45 45 ALA A 529 ASP A 531 5 3
HELIX 46 46 VAL A 533 GLY A 548 1 16
HELIX 47 47 PRO A 549 LEU A 551 5 3
HELIX 48 48 ASP A 552 GLU A 559 1 8
HELIX 49 49 GLU A 559 THR A 568 1 10
HELIX 50 50 ASP A 572 SER A 587 1 16
HELIX 51 51 PHE C 6 ASN C 18 1 13
HELIX 52 52 SER C 24 GLU C 42 1 19
HELIX 53 53 GLN C 61 GLY C 73 1 13
HELIX 54 54 TYR C 92 TYR C 107 1 16
HELIX 55 55 SER C 120 GLN C 125 1 6
HELIX 56 56 GLY C 128 TYR C 137 1 10
HELIX 57 57 ALA C 140 ASP C 151 1 12
HELIX 58 58 THR C 176 ALA C 182 1 7
HELIX 59 59 GLY C 193 SER C 201 1 9
HELIX 60 60 GLY C 221 ASN C 232 1 12
HELIX 61 61 ASN C 264 ARG C 268 5 5
SHEET 1 A 6 GLN C 46 VAL C 48 0
SHEET 2 A 6 ALA C 157 VAL C 159 1 O LEU C 158 N GLN C 46
SHEET 3 A 6 ILE C 163 CYS C 165 -1 O ILE C 163 N VAL C 159
SHEET 4 A 6 LEU C 236 ARG C 239 1 O SER C 238 N PHE C 164
SHEET 5 A 6 VAL C 256 ILE C 259 1 O VAL C 257 N ARG C 239
SHEET 6 A 6 TYR C 248 CYS C 251 -1 N ASN C 249 O THR C 258
SHEET 1 B 5 ILE C 111 ILE C 113 0
SHEET 2 B 5 TYR C 80 PHE C 82 1 N PHE C 82 O THR C 112
SHEET 3 B 5 VAL C 52 CYS C 55 1 N THR C 53 O LEU C 81
SHEET 4 B 5 ALA C 273 LEU C 278 -1 O MET C 276 N VAL C 54
SHEET 5 B 5 TYR C 284 PHE C 289 -1 O SER C 285 N GLU C 277
SHEET 1 C 3 ASP C 202 PRO C 203 0
SHEET 2 C 3 TYR C 218 PHE C 220 1 O TYR C 218 N ASP C 202
SHEET 3 C 3 TRP C 209 ILE C 211 -1 N GLY C 210 O THR C 219
LINK SG CYS C 269 CB DAM I 7 1555 1555 1.79
LINK C DAL I 1 N LEU I 2 1555 1555 1.32
LINK N DAL I 1 C DAM I 7 1555 1555 1.33
LINK CG ACB I 3 N ARG I 4 1555 1555 1.33
LINK C ARG I 4 N 1ZN I 5 1555 1555 1.33
LINK C 1ZN I 5 N FGA I 6 1555 1555 1.34
LINK CD FGA I 6 N DAM I 7 1555 1555 1.34
LINK OD2 ASP C 57 MN MN C 502 1555 1555 2.15
LINK NE2 HIS C 59 MN MN C 502 1555 1555 2.31
LINK OD2 ASP C 85 MN MN C 501 1555 1555 2.66
LINK OD2 ASP C 85 MN MN C 502 1555 1555 1.98
LINK OD1 ASN C 117 MN MN C 501 1555 1555 2.02
LINK NE2 HIS C 167 MN MN C 501 1555 1555 2.11
LINK ND1 HIS C 241 MN MN C 501 1555 1555 2.13
CISPEP 1 CYS C 50 PRO C 51 0 -0.08
CISPEP 2 SER C 75 PRO C 76 0 -0.10
SITE 1 AC1 5 ASP C 85 ASN C 117 HIS C 167 HIS C 241
SITE 2 AC1 5 MN C 502
SITE 1 AC2 4 ASP C 57 HIS C 59 ASP C 85 MN C 501
CRYST1 93.070 195.090 201.910 90.00 90.00 90.00 I 2 2 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 0.010745 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005126 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004953 0.00000
(ATOM LINES ARE NOT SHOWN.)
END