HEADER TRANSFERASE 07-JUL-11 3SRH
TITLE HUMAN M2 PYRUVATE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE ISOZYMES M1/M2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CYTOSOLIC THYROID HORMONE-BINDING PROTEIN, CTHBP, OPA-
COMPND 5 INTERACTING PROTEIN 3, OIP-3, PYRUVATE KINASE 2/3, PYRUVATE KINASE
COMPND 6 MUSCLE ISOZYME, THYROID HORMONE-BINDING PROTEIN 1, THBP1, TUMOR M2-
COMPND 7 PK, P58;
COMPND 8 EC: 2.7.1.40;
COMPND 9 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: OIP3, PK2, PK3, PKM, PKM2;
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: PET;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A_M2
KEYWDS TIM BARREL, PHOSPHORYL TRANSFER, PEP BINDING, CYTOSOL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.P.MORGAN,F.O'REILLY,R.PALMER,I.W.MCNAE,M.W.NOWICKI,M.A.WEAR,
AUTHOR 2 L.A.FOTHERGILL-GILMORE,M.D.WALKINSHAW
REVDAT 2 28-FEB-24 3SRH 1 REMARK SEQADV
REVDAT 1 08-AUG-12 3SRH 0
JRNL AUTH H.P.MORGAN,F.O'REILLY,R.PALMER,I.W.MCNAE,M.W.NOWICKI,
JRNL AUTH 2 M.A.WEAR,L.A.FOTHERGILL-GILMORE,M.D.WALKINSHAW
JRNL TITL ALLOSETRIC REGULATION OF M2 PYRUVATE KINASE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 66737
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3558
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4955
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 252
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15860
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 357
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : -0.10000
REMARK 3 B33 (A**2) : 0.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.355
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.311
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.679
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16128 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21790 ; 0.926 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2068 ; 4.345 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 668 ;36.198 ;23.952
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2920 ;16.582 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 124 ;14.459 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2508 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11948 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7775 ; 0.167 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 11148 ; 0.293 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 602 ; 0.119 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 32 ; 0.115 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.169 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 10584 ; 0.788 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16604 ; 1.419 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6109 ; 0.663 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5186 ; 1.143 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3SRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066561.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70424
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 53.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.61800
REMARK 200 R SYM FOR SHELL (I) : 0.42300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 28.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-16% POLYETHYLENEGLYCOL 8000, 20 MM
REMARK 280 TRIETHANOLAMINE-HCL BUFFER (PH 7.2), 50 MM MGCL2, 100 MM KCL, 10%
REMARK 280 GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 77.15500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 73860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 SER A 1
REMARK 465 LYS A 2
REMARK 465 PRO A 3
REMARK 465 HIS A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 ALA A 7
REMARK 465 GLY A 8
REMARK 465 THR A 9
REMARK 465 ALA A 10
REMARK 465 PHE A 11
REMARK 465 ILE A 12
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 SER B 1
REMARK 465 LYS B 2
REMARK 465 PRO B 3
REMARK 465 HIS B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 465 ALA B 7
REMARK 465 GLY B 8
REMARK 465 THR B 9
REMARK 465 ALA B 10
REMARK 465 PHE B 11
REMARK 465 ILE B 12
REMARK 465 MET C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 LEU C -7
REMARK 465 VAL C -6
REMARK 465 PRO C -5
REMARK 465 ARG C -4
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 HIS C -1
REMARK 465 MET C 0
REMARK 465 SER C 1
REMARK 465 LYS C 2
REMARK 465 PRO C 3
REMARK 465 HIS C 4
REMARK 465 SER C 5
REMARK 465 GLU C 6
REMARK 465 ALA C 7
REMARK 465 GLY C 8
REMARK 465 THR C 9
REMARK 465 ALA C 10
REMARK 465 PHE C 11
REMARK 465 ILE C 12
REMARK 465 MET D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 SER D -10
REMARK 465 SER D -9
REMARK 465 GLY D -8
REMARK 465 LEU D -7
REMARK 465 VAL D -6
REMARK 465 PRO D -5
REMARK 465 ARG D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 HIS D -1
REMARK 465 MET D 0
REMARK 465 SER D 1
REMARK 465 LYS D 2
REMARK 465 PRO D 3
REMARK 465 HIS D 4
REMARK 465 SER D 5
REMARK 465 GLU D 6
REMARK 465 ALA D 7
REMARK 465 GLY D 8
REMARK 465 THR D 9
REMARK 465 ALA D 10
REMARK 465 PHE D 11
REMARK 465 ILE D 12
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 SER A 54 18.78 -149.13
REMARK 500 ASP A 176 65.57 63.55
REMARK 500 ASN A 198 -81.01 -94.53
REMARK 500 LYS A 205 60.75 37.71
REMARK 500 ARG A 278 33.37 -95.72
REMARK 500 THR A 327 124.49 75.56
REMARK 500 PRO A 516 75.49 -62.48
REMARK 500 GLN B 15 45.34 36.54
REMARK 500 PHE B 75 38.04 -92.91
REMARK 500 ASP B 152 -169.49 -102.12
REMARK 500 ASP B 176 75.70 55.51
REMARK 500 ASN B 198 -75.88 -125.77
REMARK 500 LYS B 205 56.83 29.77
REMARK 500 GLU B 271 25.47 -149.80
REMARK 500 THR B 327 134.51 68.04
REMARK 500 GLN B 328 17.88 58.89
REMARK 500 LEU B 330 55.62 -116.36
REMARK 500 LYS B 335 -51.02 -124.70
REMARK 500 PRO B 516 58.74 -65.65
REMARK 500 SER B 518 -73.55 -138.34
REMARK 500 PHE B 520 76.94 -69.53
REMARK 500 GLN C 15 51.56 38.14
REMARK 500 LYS C 124 19.03 55.39
REMARK 500 ASP C 176 81.21 58.39
REMARK 500 ASP C 190 22.74 -144.23
REMARK 500 ASN C 198 -85.65 -128.09
REMARK 500 GLU C 271 11.47 -140.29
REMARK 500 THR C 327 130.15 63.38
REMARK 500 ARG C 444 71.28 39.85
REMARK 500 PHE C 520 113.85 64.98
REMARK 500 GLN D 15 39.06 38.85
REMARK 500 ARG D 42 113.96 -170.29
REMARK 500 SER D 54 19.93 -143.76
REMARK 500 LYS D 150 58.76 -113.08
REMARK 500 ASP D 176 69.37 61.53
REMARK 500 ASN D 198 -58.01 -123.12
REMARK 500 LYS D 205 54.76 37.93
REMARK 500 THR D 327 118.48 90.16
REMARK 500 CYS D 423 66.38 38.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 531
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SRD RELATED DB: PDB
REMARK 900 RELATED ID: 3SRF RELATED DB: PDB
DBREF 3SRH A 0 530 UNP P14618 KPYM_HUMAN 1 531
DBREF 3SRH B 0 530 UNP P14618 KPYM_HUMAN 1 531
DBREF 3SRH C 0 530 UNP P14618 KPYM_HUMAN 1 531
DBREF 3SRH D 0 530 UNP P14618 KPYM_HUMAN 1 531
SEQADV 3SRH MET A -20 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY A -19 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER A -18 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER A -17 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS A -16 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS A -15 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS A -14 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS A -13 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS A -12 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS A -11 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER A -10 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER A -9 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY A -8 UNP P14618 EXPRESSION TAG
SEQADV 3SRH LEU A -7 UNP P14618 EXPRESSION TAG
SEQADV 3SRH VAL A -6 UNP P14618 EXPRESSION TAG
SEQADV 3SRH PRO A -5 UNP P14618 EXPRESSION TAG
SEQADV 3SRH ARG A -4 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY A -3 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER A -2 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS A -1 UNP P14618 EXPRESSION TAG
SEQADV 3SRH MET B -20 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY B -19 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER B -18 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER B -17 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS B -16 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS B -15 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS B -14 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS B -13 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS B -12 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS B -11 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER B -10 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER B -9 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY B -8 UNP P14618 EXPRESSION TAG
SEQADV 3SRH LEU B -7 UNP P14618 EXPRESSION TAG
SEQADV 3SRH VAL B -6 UNP P14618 EXPRESSION TAG
SEQADV 3SRH PRO B -5 UNP P14618 EXPRESSION TAG
SEQADV 3SRH ARG B -4 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY B -3 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER B -2 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS B -1 UNP P14618 EXPRESSION TAG
SEQADV 3SRH MET C -20 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY C -19 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER C -18 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER C -17 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS C -16 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS C -15 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS C -14 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS C -13 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS C -12 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS C -11 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER C -10 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER C -9 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY C -8 UNP P14618 EXPRESSION TAG
SEQADV 3SRH LEU C -7 UNP P14618 EXPRESSION TAG
SEQADV 3SRH VAL C -6 UNP P14618 EXPRESSION TAG
SEQADV 3SRH PRO C -5 UNP P14618 EXPRESSION TAG
SEQADV 3SRH ARG C -4 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY C -3 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER C -2 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS C -1 UNP P14618 EXPRESSION TAG
SEQADV 3SRH MET D -20 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY D -19 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER D -18 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER D -17 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS D -16 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS D -15 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS D -14 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS D -13 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS D -12 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS D -11 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER D -10 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER D -9 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY D -8 UNP P14618 EXPRESSION TAG
SEQADV 3SRH LEU D -7 UNP P14618 EXPRESSION TAG
SEQADV 3SRH VAL D -6 UNP P14618 EXPRESSION TAG
SEQADV 3SRH PRO D -5 UNP P14618 EXPRESSION TAG
SEQADV 3SRH ARG D -4 UNP P14618 EXPRESSION TAG
SEQADV 3SRH GLY D -3 UNP P14618 EXPRESSION TAG
SEQADV 3SRH SER D -2 UNP P14618 EXPRESSION TAG
SEQADV 3SRH HIS D -1 UNP P14618 EXPRESSION TAG
SEQRES 1 A 551 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 551 LEU VAL PRO ARG GLY SER HIS MET SER LYS PRO HIS SER
SEQRES 3 A 551 GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU HIS
SEQRES 4 A 551 ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS ARG
SEQRES 5 A 551 LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN THR
SEQRES 6 A 551 GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER VAL
SEQRES 7 A 551 GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN VAL
SEQRES 8 A 551 ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR HIS
SEQRES 9 A 551 ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU SER
SEQRES 10 A 551 PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA VAL
SEQRES 11 A 551 ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY LEU
SEQRES 12 A 551 ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS LYS
SEQRES 13 A 551 GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR MET
SEQRES 14 A 551 GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS
SEQRES 15 A 551 ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE TYR
SEQRES 16 A 551 VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN LYS
SEQRES 17 A 551 GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY GLY
SEQRES 18 A 551 SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY ALA
SEQRES 19 A 551 ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE GLN
SEQRES 20 A 551 ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET VAL
SEQRES 21 A 551 PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS GLU
SEQRES 22 A 551 VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS
SEQRES 23 A 551 ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG
SEQRES 24 A 551 PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET VAL
SEQRES 25 A 551 ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS
SEQRES 26 A 551 VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS ASN
SEQRES 27 A 551 ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET LEU
SEQRES 28 A 551 GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA GLU
SEQRES 29 A 551 GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP
SEQRES 30 A 551 CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP TYR
SEQRES 31 A 551 PRO LEU GLU ALA VAL ARG MET GLN HIS LEU ILE ALA ARG
SEQRES 32 A 551 GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU
SEQRES 33 A 551 GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO THR
SEQRES 34 A 551 GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE LYS
SEQRES 35 A 551 CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER GLY
SEQRES 36 A 551 ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA
SEQRES 37 A 551 PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA ARG
SEQRES 38 A 551 GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS
SEQRES 39 A 551 LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP
SEQRES 40 A 551 LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA ARG
SEQRES 41 A 551 GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU THR
SEQRES 42 A 551 GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET ARG
SEQRES 43 A 551 VAL VAL PRO VAL PRO
SEQRES 1 B 551 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 551 LEU VAL PRO ARG GLY SER HIS MET SER LYS PRO HIS SER
SEQRES 3 B 551 GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU HIS
SEQRES 4 B 551 ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS ARG
SEQRES 5 B 551 LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN THR
SEQRES 6 B 551 GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER VAL
SEQRES 7 B 551 GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN VAL
SEQRES 8 B 551 ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR HIS
SEQRES 9 B 551 ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU SER
SEQRES 10 B 551 PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA VAL
SEQRES 11 B 551 ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY LEU
SEQRES 12 B 551 ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS LYS
SEQRES 13 B 551 GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR MET
SEQRES 14 B 551 GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS
SEQRES 15 B 551 ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE TYR
SEQRES 16 B 551 VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN LYS
SEQRES 17 B 551 GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY GLY
SEQRES 18 B 551 SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY ALA
SEQRES 19 B 551 ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE GLN
SEQRES 20 B 551 ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET VAL
SEQRES 21 B 551 PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS GLU
SEQRES 22 B 551 VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS
SEQRES 23 B 551 ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG
SEQRES 24 B 551 PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET VAL
SEQRES 25 B 551 ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS
SEQRES 26 B 551 VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS ASN
SEQRES 27 B 551 ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET LEU
SEQRES 28 B 551 GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA GLU
SEQRES 29 B 551 GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP
SEQRES 30 B 551 CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP TYR
SEQRES 31 B 551 PRO LEU GLU ALA VAL ARG MET GLN HIS LEU ILE ALA ARG
SEQRES 32 B 551 GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU
SEQRES 33 B 551 GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO THR
SEQRES 34 B 551 GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE LYS
SEQRES 35 B 551 CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER GLY
SEQRES 36 B 551 ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA
SEQRES 37 B 551 PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA ARG
SEQRES 38 B 551 GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS
SEQRES 39 B 551 LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP
SEQRES 40 B 551 LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA ARG
SEQRES 41 B 551 GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU THR
SEQRES 42 B 551 GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET ARG
SEQRES 43 B 551 VAL VAL PRO VAL PRO
SEQRES 1 C 551 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 551 LEU VAL PRO ARG GLY SER HIS MET SER LYS PRO HIS SER
SEQRES 3 C 551 GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU HIS
SEQRES 4 C 551 ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS ARG
SEQRES 5 C 551 LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN THR
SEQRES 6 C 551 GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER VAL
SEQRES 7 C 551 GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN VAL
SEQRES 8 C 551 ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR HIS
SEQRES 9 C 551 ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU SER
SEQRES 10 C 551 PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA VAL
SEQRES 11 C 551 ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY LEU
SEQRES 12 C 551 ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS LYS
SEQRES 13 C 551 GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR MET
SEQRES 14 C 551 GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS
SEQRES 15 C 551 ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE TYR
SEQRES 16 C 551 VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN LYS
SEQRES 17 C 551 GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY GLY
SEQRES 18 C 551 SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY ALA
SEQRES 19 C 551 ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE GLN
SEQRES 20 C 551 ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET VAL
SEQRES 21 C 551 PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS GLU
SEQRES 22 C 551 VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS
SEQRES 23 C 551 ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG
SEQRES 24 C 551 PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET VAL
SEQRES 25 C 551 ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS
SEQRES 26 C 551 VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS ASN
SEQRES 27 C 551 ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET LEU
SEQRES 28 C 551 GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA GLU
SEQRES 29 C 551 GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP
SEQRES 30 C 551 CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP TYR
SEQRES 31 C 551 PRO LEU GLU ALA VAL ARG MET GLN HIS LEU ILE ALA ARG
SEQRES 32 C 551 GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU
SEQRES 33 C 551 GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO THR
SEQRES 34 C 551 GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE LYS
SEQRES 35 C 551 CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER GLY
SEQRES 36 C 551 ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA
SEQRES 37 C 551 PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA ARG
SEQRES 38 C 551 GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS
SEQRES 39 C 551 LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP
SEQRES 40 C 551 LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA ARG
SEQRES 41 C 551 GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU THR
SEQRES 42 C 551 GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET ARG
SEQRES 43 C 551 VAL VAL PRO VAL PRO
SEQRES 1 D 551 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 551 LEU VAL PRO ARG GLY SER HIS MET SER LYS PRO HIS SER
SEQRES 3 D 551 GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU HIS
SEQRES 4 D 551 ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS ARG
SEQRES 5 D 551 LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN THR
SEQRES 6 D 551 GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER VAL
SEQRES 7 D 551 GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN VAL
SEQRES 8 D 551 ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR HIS
SEQRES 9 D 551 ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU SER
SEQRES 10 D 551 PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA VAL
SEQRES 11 D 551 ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY LEU
SEQRES 12 D 551 ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS LYS
SEQRES 13 D 551 GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR MET
SEQRES 14 D 551 GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS
SEQRES 15 D 551 ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE TYR
SEQRES 16 D 551 VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN LYS
SEQRES 17 D 551 GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY GLY
SEQRES 18 D 551 SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY ALA
SEQRES 19 D 551 ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE GLN
SEQRES 20 D 551 ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET VAL
SEQRES 21 D 551 PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS GLU
SEQRES 22 D 551 VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS
SEQRES 23 D 551 ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG
SEQRES 24 D 551 PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET VAL
SEQRES 25 D 551 ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS
SEQRES 26 D 551 VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS ASN
SEQRES 27 D 551 ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET LEU
SEQRES 28 D 551 GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA GLU
SEQRES 29 D 551 GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP
SEQRES 30 D 551 CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP TYR
SEQRES 31 D 551 PRO LEU GLU ALA VAL ARG MET GLN HIS LEU ILE ALA ARG
SEQRES 32 D 551 GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU
SEQRES 33 D 551 GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO THR
SEQRES 34 D 551 GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE LYS
SEQRES 35 D 551 CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER GLY
SEQRES 36 D 551 ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA
SEQRES 37 D 551 PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA ARG
SEQRES 38 D 551 GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS
SEQRES 39 D 551 LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP
SEQRES 40 D 551 LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA ARG
SEQRES 41 D 551 GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU THR
SEQRES 42 D 551 GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET ARG
SEQRES 43 D 551 VAL VAL PRO VAL PRO
HET PO4 A 531 5
HET PO4 B 531 5
HET PO4 D 531 5
HETNAM PO4 PHOSPHATE ION
FORMUL 5 PO4 3(O4 P 3-)
FORMUL 8 HOH *357(H2 O)
HELIX 1 1 GLN A 16 MET A 21 1 6
HELIX 2 2 THR A 24 ARG A 31 1 8
HELIX 3 3 SER A 56 GLY A 67 1 12
HELIX 4 4 THR A 79 SER A 96 1 18
HELIX 5 5 ASP A 144 MET A 148 5 5
HELIX 6 6 ASN A 162 VAL A 167 1 6
HELIX 7 7 SER A 221 GLN A 234 1 14
HELIX 8 8 LYS A 246 GLY A 258 1 13
HELIX 9 9 ASN A 272 ARG A 278 1 7
HELIX 10 10 ARG A 278 SER A 286 1 9
HELIX 11 11 ARG A 293 ILE A 300 1 8
HELIX 12 12 PRO A 301 GLU A 303 5 3
HELIX 13 13 LYS A 304 ALA A 319 1 16
HELIX 14 14 LEU A 330 LYS A 335 5 6
HELIX 15 15 THR A 340 GLY A 354 1 15
HELIX 16 16 TYR A 369 ALA A 387 1 19
HELIX 17 17 TYR A 389 LEU A 400 1 12
HELIX 18 18 ASP A 406 CYS A 422 1 17
HELIX 19 19 GLY A 434 ARG A 442 1 9
HELIX 20 20 ASN A 455 ALA A 462 1 8
HELIX 21 21 HIS A 463 TYR A 465 5 3
HELIX 22 22 ALA A 480 ARG A 499 1 20
HELIX 23 23 GLN B 16 MET B 21 1 6
HELIX 24 24 THR B 24 LEU B 32 1 9
HELIX 25 25 SER B 56 GLY B 67 1 12
HELIX 26 26 THR B 79 PHE B 97 1 19
HELIX 27 27 ALA B 98 ASP B 100 5 3
HELIX 28 28 ASP B 144 MET B 148 5 5
HELIX 29 29 ASN B 162 VAL B 167 1 6
HELIX 30 30 SER B 221 GLN B 234 1 14
HELIX 31 31 LYS B 246 GLY B 258 1 13
HELIX 32 32 GLU B 259 LYS B 262 5 4
HELIX 33 33 ASN B 272 ARG B 278 1 7
HELIX 34 34 ARG B 278 SER B 286 1 9
HELIX 35 35 ALA B 292 ILE B 300 1 9
HELIX 36 36 PRO B 301 GLU B 303 5 3
HELIX 37 37 LYS B 304 GLY B 320 1 17
HELIX 38 38 LEU B 330 LYS B 335 5 6
HELIX 39 39 THR B 340 GLY B 354 1 15
HELIX 40 40 PRO B 370 ALA B 387 1 18
HELIX 41 41 TYR B 389 ALA B 401 1 13
HELIX 42 42 ASP B 406 CYS B 422 1 17
HELIX 43 43 GLY B 434 ARG B 442 1 9
HELIX 44 44 ASN B 455 ALA B 462 1 8
HELIX 45 45 HIS B 463 TYR B 465 5 3
HELIX 46 46 ALA B 480 ARG B 499 1 20
HELIX 47 47 GLN C 16 MET C 21 1 6
HELIX 48 48 THR C 24 ARG C 31 1 8
HELIX 49 49 SER C 56 GLY C 67 1 12
HELIX 50 50 THR C 79 GLU C 95 1 17
HELIX 51 51 SER C 96 ALA C 98 5 3
HELIX 52 52 ASP C 144 MET C 148 5 5
HELIX 53 53 ASN C 162 VAL C 167 1 6
HELIX 54 54 SER C 221 GLN C 234 1 14
HELIX 55 55 LYS C 246 GLY C 258 1 13
HELIX 56 56 ASN C 272 ARG C 278 1 7
HELIX 57 57 ARG C 278 SER C 286 1 9
HELIX 58 58 ALA C 292 ILE C 300 1 9
HELIX 59 59 PRO C 301 GLU C 303 5 3
HELIX 60 60 LYS C 304 GLY C 320 1 17
HELIX 61 61 LEU C 330 LYS C 335 5 6
HELIX 62 62 THR C 340 GLY C 354 1 15
HELIX 63 63 PRO C 370 ALA C 387 1 18
HELIX 64 64 TYR C 389 ALA C 401 1 13
HELIX 65 65 ASP C 406 CYS C 422 1 17
HELIX 66 66 GLY C 434 ARG C 442 1 9
HELIX 67 67 ASN C 455 ALA C 462 1 8
HELIX 68 68 HIS C 463 TYR C 465 5 3
HELIX 69 69 ALA C 480 GLY C 500 1 21
HELIX 70 70 GLN D 16 MET D 21 1 6
HELIX 71 71 THR D 24 ARG D 31 1 8
HELIX 72 72 SER D 56 GLY D 67 1 12
HELIX 73 73 THR D 79 GLU D 95 1 17
HELIX 74 74 ASP D 144 MET D 148 5 5
HELIX 75 75 ASN D 162 VAL D 167 1 6
HELIX 76 76 SER D 221 GLN D 234 1 14
HELIX 77 77 LYS D 246 GLY D 258 1 13
HELIX 78 78 ASN D 272 ARG D 278 1 7
HELIX 79 79 ARG D 278 SER D 286 1 9
HELIX 80 80 ARG D 293 ILE D 300 1 8
HELIX 81 81 PRO D 301 GLU D 303 5 3
HELIX 82 82 LYS D 304 GLY D 320 1 17
HELIX 83 83 LEU D 330 LYS D 335 5 6
HELIX 84 84 THR D 340 GLY D 354 1 15
HELIX 85 85 TYR D 369 ILE D 388 1 20
HELIX 86 86 TYR D 389 LEU D 400 1 12
HELIX 87 87 ASP D 406 CYS D 422 1 17
HELIX 88 88 GLY D 434 ARG D 442 1 9
HELIX 89 89 ASN D 455 ALA D 462 1 8
HELIX 90 90 HIS D 463 TYR D 465 5 3
HELIX 91 91 ALA D 480 GLY D 500 1 21
SHEET 1 A 9 GLY A 45 THR A 49 0
SHEET 2 A 9 VAL A 70 ASN A 74 1 O ARG A 72 N CYS A 48
SHEET 3 A 9 ALA A 108 ASP A 112 1 O ALA A 110 N ALA A 71
SHEET 4 A 9 MET A 238 ALA A 241 1 O PHE A 240 N LEU A 111
SHEET 5 A 9 LYS A 265 ILE A 270 1 O ILE A 267 N VAL A 239
SHEET 6 A 9 GLY A 288 ALA A 292 1 O MET A 290 N SER A 268
SHEET 7 A 9 VAL A 323 ALA A 326 1 O ILE A 324 N VAL A 291
SHEET 8 A 9 CYS A 357 LEU A 360 1 O CYS A 357 N CYS A 325
SHEET 9 A 9 GLY A 45 THR A 49 1 N GLY A 45 O ILE A 358
SHEET 1 B 2 VAL A 131 LEU A 133 0
SHEET 2 B 2 GLY A 200 LEU A 202 -1 O LEU A 202 N VAL A 131
SHEET 1 C 6 ILE A 155 TRP A 157 0
SHEET 2 C 6 THR A 138 THR A 142 1 N THR A 142 O LEU A 156
SHEET 3 C 6 PHE A 191 VAL A 196 -1 O THR A 194 N LEU A 139
SHEET 4 C 6 ILE A 180 GLN A 186 -1 N LYS A 185 O VAL A 193
SHEET 5 C 6 LYS A 172 VAL A 175 -1 N VAL A 175 O ILE A 180
SHEET 6 C 6 VAL A 208 ASN A 209 -1 O ASN A 209 N TYR A 174
SHEET 1 D10 ILE A 468 LEU A 472 0
SHEET 2 D10 ILE A 449 THR A 453 1 N ILE A 449 O PHE A 469
SHEET 3 D10 ILE A 427 LEU A 430 1 N VAL A 429 O ILE A 450
SHEET 4 D10 VAL A 507 GLY A 513 1 O ILE A 509 N ILE A 428
SHEET 5 D10 THR A 521 PRO A 528 -1 O VAL A 527 N VAL A 508
SHEET 6 D10 THR B 521 PRO B 528 -1 O MET B 524 N MET A 524
SHEET 7 D10 VAL B 507 GLY B 513 -1 N VAL B 510 O ARG B 525
SHEET 8 D10 ILE B 427 LEU B 430 1 N ILE B 428 O LEU B 511
SHEET 9 D10 ILE B 449 THR B 453 1 O ILE B 450 N VAL B 429
SHEET 10 D10 ILE B 468 LEU B 472 1 O PHE B 469 N ILE B 449
SHEET 1 E 9 GLY B 45 THR B 49 0
SHEET 2 E 9 VAL B 70 ARG B 72 1 O ARG B 72 N CYS B 48
SHEET 3 E 9 ALA B 108 ASP B 112 1 O ALA B 110 N ALA B 71
SHEET 4 E 9 MET B 238 ALA B 241 1 O PHE B 240 N LEU B 111
SHEET 5 E 9 LYS B 265 ILE B 270 1 O ILE B 267 N VAL B 239
SHEET 6 E 9 GLY B 288 VAL B 291 1 O MET B 290 N SER B 268
SHEET 7 E 9 VAL B 323 CYS B 325 1 O ILE B 324 N VAL B 291
SHEET 8 E 9 CYS B 357 LEU B 360 1 O CYS B 357 N CYS B 325
SHEET 9 E 9 GLY B 45 THR B 49 1 N ILE B 47 O ILE B 358
SHEET 1 F 7 ILE B 118 ARG B 119 0
SHEET 2 F 7 GLY B 207 ASN B 209 -1 O VAL B 208 N ILE B 118
SHEET 3 F 7 LYS B 172 VAL B 175 -1 N TYR B 174 O ASN B 209
SHEET 4 F 7 ILE B 180 VAL B 184 -1 O LEU B 182 N ILE B 173
SHEET 5 F 7 LEU B 192 VAL B 196 -1 O GLU B 195 N GLN B 183
SHEET 6 F 7 THR B 138 THR B 142 -1 N LEU B 139 O THR B 194
SHEET 7 F 7 ILE B 155 TRP B 157 1 O LEU B 156 N THR B 142
SHEET 1 G 2 VAL B 131 GLU B 132 0
SHEET 2 G 2 SER B 201 LEU B 202 -1 O LEU B 202 N VAL B 131
SHEET 1 H 9 GLY C 45 THR C 49 0
SHEET 2 H 9 VAL C 70 ASN C 74 1 O ARG C 72 N CYS C 48
SHEET 3 H 9 ALA C 108 ASP C 112 1 O ALA C 110 N ALA C 71
SHEET 4 H 9 MET C 238 ALA C 241 1 O PHE C 240 N LEU C 111
SHEET 5 H 9 LYS C 265 ILE C 270 1 O ILE C 267 N VAL C 239
SHEET 6 H 9 GLY C 288 VAL C 291 1 O MET C 290 N SER C 268
SHEET 7 H 9 VAL C 323 CYS C 325 1 O ILE C 324 N VAL C 291
SHEET 8 H 9 CYS C 357 LEU C 360 1 O CYS C 357 N CYS C 325
SHEET 9 H 9 GLY C 45 THR C 49 1 N ILE C 47 O ILE C 358
SHEET 1 I 7 ILE C 118 ARG C 119 0
SHEET 2 I 7 GLY C 207 ASN C 209 -1 O VAL C 208 N ILE C 118
SHEET 3 I 7 LYS C 172 VAL C 175 -1 N TYR C 174 O ASN C 209
SHEET 4 I 7 ILE C 180 GLN C 186 -1 O LEU C 182 N ILE C 173
SHEET 5 I 7 PHE C 191 VAL C 196 -1 O GLU C 195 N GLN C 183
SHEET 6 I 7 THR C 138 THR C 142 -1 N ILE C 141 O LEU C 192
SHEET 7 I 7 ILE C 155 TRP C 157 1 O LEU C 156 N LYS C 140
SHEET 1 J 2 VAL C 131 GLU C 132 0
SHEET 2 J 2 SER C 201 LEU C 202 -1 O LEU C 202 N VAL C 131
SHEET 1 K10 ILE C 468 LEU C 472 0
SHEET 2 K10 ILE C 449 THR C 453 1 N ILE C 449 O PHE C 469
SHEET 3 K10 ILE C 427 LEU C 430 1 N VAL C 429 O VAL C 452
SHEET 4 K10 VAL C 507 THR C 512 1 O LEU C 511 N ILE C 428
SHEET 5 K10 THR C 523 PRO C 528 -1 O VAL C 527 N VAL C 508
SHEET 6 K10 THR D 521 PRO D 528 -1 O MET D 524 N MET C 524
SHEET 7 K10 VAL D 507 GLY D 513 -1 N VAL D 510 O ARG D 525
SHEET 8 K10 ILE D 427 LEU D 430 1 N ILE D 428 O LEU D 511
SHEET 9 K10 ILE D 449 THR D 453 1 O ILE D 450 N VAL D 429
SHEET 10 K10 ILE D 468 LEU D 472 1 O PHE D 469 N ILE D 449
SHEET 1 L 9 GLY D 45 THR D 49 0
SHEET 2 L 9 VAL D 70 ASN D 74 1 O ARG D 72 N CYS D 48
SHEET 3 L 9 ALA D 108 ASP D 112 1 O ALA D 108 N ALA D 71
SHEET 4 L 9 MET D 238 ALA D 241 1 O PHE D 240 N LEU D 111
SHEET 5 L 9 LYS D 265 ILE D 270 1 O ILE D 267 N VAL D 239
SHEET 6 L 9 GLY D 288 ALA D 292 1 O MET D 290 N SER D 268
SHEET 7 L 9 VAL D 323 ALA D 326 1 O ILE D 324 N VAL D 291
SHEET 8 L 9 CYS D 357 LEU D 360 1 O CYS D 357 N CYS D 325
SHEET 9 L 9 GLY D 45 THR D 49 1 N ILE D 47 O ILE D 358
SHEET 1 M 2 GLU D 130 LEU D 133 0
SHEET 2 M 2 GLY D 200 GLY D 203 -1 O LEU D 202 N VAL D 131
SHEET 1 N 6 ILE D 155 TRP D 157 0
SHEET 2 N 6 THR D 138 THR D 142 1 N THR D 142 O LEU D 156
SHEET 3 N 6 PHE D 191 VAL D 196 -1 O THR D 194 N LEU D 139
SHEET 4 N 6 ILE D 180 LYS D 187 -1 N LYS D 185 O VAL D 193
SHEET 5 N 6 LYS D 172 VAL D 175 -1 N VAL D 175 O ILE D 180
SHEET 6 N 6 VAL D 208 ASN D 209 -1 O ASN D 209 N TYR D 174
CISPEP 1 GLY A 517 SER A 518 0 -10.11
SITE 1 AC1 6 THR A 431 LYS A 432 SER A 433 SER A 436
SITE 2 AC1 6 SER A 518 GLY A 519
SITE 1 AC2 8 THR B 431 LYS B 432 SER B 433 GLY B 434
SITE 2 AC2 8 ARG B 435 SER B 436 SER B 518 GLY B 519
SITE 1 AC3 7 THR D 431 LYS D 432 SER D 433 ARG D 435
SITE 2 AC3 7 SER D 436 SER D 518 GLY D 519
CRYST1 81.200 154.310 98.590 90.00 105.59 90.00 P 1 21 1 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 0.012315 0.000000 0.003436 0.00000
SCALE2 0.000000 0.006480 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010530 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
