HEADER TRANSFERASE 08-FEB-19 6JFB
TITLE CRYSTAL STRUCTURE OF HUMAN PYRUVATE KINASE M2 ISOFORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE PKM ISOFORM 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-PK,
COMPND 7 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: PKM, OIP3, PK2, PK3, PKM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PYRUVATE KINASE, GLYCOLYSIS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.J.CHEN,W.C.WANG
REVDAT 2 27-MAR-24 6JFB 1 REMARK
REVDAT 1 01-APR-20 6JFB 0
JRNL AUTH T.J.CHEN,W.C.WANG
JRNL TITL CRYSTAL STRUCTURE OF HUMAN PYRUVATE KINASE M2 ISOFORM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 114970
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6128
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) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8229
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 418
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15947
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 488
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.240
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.205
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.306
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
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): 16237 ; 0.011 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 15231 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21929 ; 1.405 ; 1.656
REMARK 3 BOND ANGLES OTHERS (DEGREES): 35693 ; 0.922 ; 1.636
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2073 ; 6.927 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 798 ;34.649 ;21.792
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2933 ;17.925 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 124 ;20.066 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2198 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18207 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2745 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 8331 ; 2.676 ; 3.226
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8330 ; 2.676 ; 3.226
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10391 ; 4.173 ; 4.822
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 10392 ; 4.173 ; 4.822
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7906 ; 3.160 ; 3.615
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 7905 ; 3.160 ; 3.615
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 11539 ; 4.992 ; 5.257
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 17660 ; 7.099 ;38.122
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 17607 ; 7.099 ;38.125
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 : NULL
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 6JFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1300011001.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121473
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 7.5, 0.2 M NACL, 14%
REMARK 280 W/V POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 76.28650
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: 15410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 74710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 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 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 PRO A 4
REMARK 465 HIS A 5
REMARK 465 SER A 6
REMARK 465 SER A 127
REMARK 465 GLY A 128
REMARK 465 THR A 129
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 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 PRO B 4
REMARK 465 HIS B 5
REMARK 465 GLY B 126
REMARK 465 SER B 127
REMARK 465 GLY B 128
REMARK 465 THR B 129
REMARK 465 ALA B 130
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 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 3
REMARK 465 PRO C 4
REMARK 465 HIS C 5
REMARK 465 GLY C 126
REMARK 465 SER C 127
REMARK 465 GLY C 128
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 MET D 1
REMARK 465 SER D 2
REMARK 465 LYS D 3
REMARK 465 PRO D 4
REMARK 465 HIS D 5
REMARK 465 SER D 6
REMARK 465 LYS D 125
REMARK 465 GLY D 126
REMARK 465 SER D 127
REMARK 465 GLY D 128
REMARK 465 THR D 129
REMARK 465 ALA D 147
REMARK 465 TYR D 148
REMARK 465 MET D 149
REMARK 465 GLU D 150
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 NH2 ARG B 278 O LYS D 166 1556 2.12
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 GLU A 364 CB - CA - C ANGL. DEV. = -12.2 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 8 46.61 75.68
REMARK 500 HIS A 19 67.10 -113.30
REMARK 500 LYS A 125 -29.30 173.08
REMARK 500 LYS A 136 129.50 -36.30
REMARK 500 ALA A 138 176.91 59.82
REMARK 500 ALA A 147 5.97 -62.98
REMARK 500 CYS A 152 -116.71 -124.07
REMARK 500 ASP A 153 111.56 71.14
REMARK 500 GLU A 154 -55.83 40.91
REMARK 500 ASP A 178 61.35 28.90
REMARK 500 ALA A 190 76.85 58.42
REMARK 500 ASN A 199 -79.79 -108.49
REMARK 500 ALA A 303 -59.38 -22.29
REMARK 500 THR A 328 143.78 72.95
REMARK 500 MET A 330 -72.25 -96.74
REMARK 500 SER A 362 -108.45 -116.30
REMARK 500 THR A 405 -86.67 60.68
REMARK 500 SER A 406 -6.21 88.86
REMARK 500 ARG A 516 165.04 61.53
REMARK 500 PHE A 521 123.71 103.20
REMARK 500 GLU B 7 101.16 -1.44
REMARK 500 HIS B 19 64.51 -107.80
REMARK 500 ALA B 21 114.64 75.88
REMARK 500 ASN B 146 -38.99 120.18
REMARK 500 LYS B 151 74.77 -113.06
REMARK 500 ASP B 177 78.60 42.80
REMARK 500 ALA B 190 -51.52 71.16
REMARK 500 LYS B 206 85.01 29.29
REMARK 500 ALA B 214 -156.64 -80.08
REMARK 500 ALA B 215 -35.26 75.96
REMARK 500 THR B 328 146.63 75.02
REMARK 500 MET B 330 -80.00 -94.31
REMARK 500 SER B 362 -105.34 -115.35
REMARK 500 LYS B 367 -12.99 -142.17
REMARK 500 SER B 519 72.29 -61.32
REMARK 500 PHE B 521 139.39 -25.51
REMARK 500 GLU C 7 103.70 -19.50
REMARK 500 THR C 10 -23.09 101.91
REMARK 500 HIS C 19 70.31 -118.42
REMARK 500 ASP C 145 114.01 -35.45
REMARK 500 TYR C 148 -7.91 160.52
REMARK 500 ASP C 153 -156.27 -159.57
REMARK 500 ASN C 199 -68.49 -109.45
REMARK 500 THR C 328 137.49 76.28
REMARK 500 MET C 330 -80.43 -96.52
REMARK 500 SER C 362 -109.22 -117.11
REMARK 500 ARG C 445 61.94 62.97
REMARK 500 SER C 519 -78.86 43.94
REMARK 500 HIS D 19 57.99 -94.47
REMARK 500 ALA D 21 102.08 76.86
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 246 0.08 SIDE CHAIN
REMARK 500 ARG A 316 0.08 SIDE CHAIN
REMARK 500 ARG A 339 0.12 SIDE CHAIN
REMARK 500 ARG A 376 0.11 SIDE CHAIN
REMARK 500 ARG A 383 0.08 SIDE CHAIN
REMARK 500 ARG A 400 0.09 SIDE CHAIN
REMARK 500 ARG A 443 0.10 SIDE CHAIN
REMARK 500 ARG A 445 0.11 SIDE CHAIN
REMARK 500 ARG A 467 0.07 SIDE CHAIN
REMARK 500 ARG B 294 0.08 SIDE CHAIN
REMARK 500 ARG B 400 0.12 SIDE CHAIN
REMARK 500 ARG B 445 0.12 SIDE CHAIN
REMARK 500 ARG B 447 0.10 SIDE CHAIN
REMARK 500 ARG B 467 0.12 SIDE CHAIN
REMARK 500 ARG B 489 0.09 SIDE CHAIN
REMARK 500 ARG C 43 0.08 SIDE CHAIN
REMARK 500 ARG C 342 0.08 SIDE CHAIN
REMARK 500 ARG C 376 0.12 SIDE CHAIN
REMARK 500 ARG C 445 0.13 SIDE CHAIN
REMARK 500 ARG C 447 0.09 SIDE CHAIN
REMARK 500 ARG D 56 0.10 SIDE CHAIN
REMARK 500 ARG D 73 0.10 SIDE CHAIN
REMARK 500 ARG D 316 0.10 SIDE CHAIN
REMARK 500 ARG D 400 0.09 SIDE CHAIN
REMARK 500 ARG D 447 0.09 SIDE CHAIN
REMARK 500 ARG D 467 0.09 SIDE CHAIN
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 SER A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SER B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SER C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SER D 601
DBREF 6JFB A 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 6JFB B 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 6JFB C 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 6JFB D 1 531 UNP P14618 KPYM_HUMAN 1 531
SEQADV 6JFB MET A -20 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY A -19 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER A -18 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER A -17 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS A -16 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS A -15 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS A -14 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS A -13 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS A -12 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS A -11 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER A -10 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER A -9 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY A -8 UNP P14618 EXPRESSION TAG
SEQADV 6JFB LEU A -7 UNP P14618 EXPRESSION TAG
SEQADV 6JFB VAL A -6 UNP P14618 EXPRESSION TAG
SEQADV 6JFB PRO A -5 UNP P14618 EXPRESSION TAG
SEQADV 6JFB ARG A -4 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY A -3 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER A -2 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS A -1 UNP P14618 EXPRESSION TAG
SEQADV 6JFB MET A 0 UNP P14618 EXPRESSION TAG
SEQADV 6JFB MET B -20 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY B -19 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER B -18 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER B -17 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS B -16 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS B -15 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS B -14 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS B -13 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS B -12 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS B -11 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER B -10 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER B -9 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY B -8 UNP P14618 EXPRESSION TAG
SEQADV 6JFB LEU B -7 UNP P14618 EXPRESSION TAG
SEQADV 6JFB VAL B -6 UNP P14618 EXPRESSION TAG
SEQADV 6JFB PRO B -5 UNP P14618 EXPRESSION TAG
SEQADV 6JFB ARG B -4 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY B -3 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER B -2 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS B -1 UNP P14618 EXPRESSION TAG
SEQADV 6JFB MET B 0 UNP P14618 EXPRESSION TAG
SEQADV 6JFB MET C -20 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY C -19 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER C -18 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER C -17 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS C -16 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS C -15 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS C -14 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS C -13 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS C -12 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS C -11 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER C -10 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER C -9 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY C -8 UNP P14618 EXPRESSION TAG
SEQADV 6JFB LEU C -7 UNP P14618 EXPRESSION TAG
SEQADV 6JFB VAL C -6 UNP P14618 EXPRESSION TAG
SEQADV 6JFB PRO C -5 UNP P14618 EXPRESSION TAG
SEQADV 6JFB ARG C -4 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY C -3 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER C -2 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS C -1 UNP P14618 EXPRESSION TAG
SEQADV 6JFB MET C 0 UNP P14618 EXPRESSION TAG
SEQADV 6JFB MET D -20 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY D -19 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER D -18 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER D -17 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS D -16 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS D -15 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS D -14 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS D -13 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS D -12 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS D -11 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER D -10 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER D -9 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY D -8 UNP P14618 EXPRESSION TAG
SEQADV 6JFB LEU D -7 UNP P14618 EXPRESSION TAG
SEQADV 6JFB VAL D -6 UNP P14618 EXPRESSION TAG
SEQADV 6JFB PRO D -5 UNP P14618 EXPRESSION TAG
SEQADV 6JFB ARG D -4 UNP P14618 EXPRESSION TAG
SEQADV 6JFB GLY D -3 UNP P14618 EXPRESSION TAG
SEQADV 6JFB SER D -2 UNP P14618 EXPRESSION TAG
SEQADV 6JFB HIS D -1 UNP P14618 EXPRESSION TAG
SEQADV 6JFB MET D 0 UNP P14618 EXPRESSION TAG
SEQRES 1 A 552 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 552 LEU VAL PRO ARG GLY SER HIS MET MET SER LYS PRO HIS
SEQRES 3 A 552 SER GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU
SEQRES 4 A 552 HIS ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS
SEQRES 5 A 552 ARG LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN
SEQRES 6 A 552 THR GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER
SEQRES 7 A 552 VAL GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN
SEQRES 8 A 552 VAL ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR
SEQRES 9 A 552 HIS ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU
SEQRES 10 A 552 SER PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA
SEQRES 11 A 552 VAL ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY
SEQRES 12 A 552 LEU ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS
SEQRES 13 A 552 LYS GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR
SEQRES 14 A 552 MET GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR
SEQRES 15 A 552 LYS ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE
SEQRES 16 A 552 TYR VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN
SEQRES 17 A 552 LYS GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY
SEQRES 18 A 552 GLY SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY
SEQRES 19 A 552 ALA ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE
SEQRES 20 A 552 GLN ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET
SEQRES 21 A 552 VAL PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS
SEQRES 22 A 552 GLU VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE
SEQRES 23 A 552 LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG
SEQRES 24 A 552 ARG PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET
SEQRES 25 A 552 VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU
SEQRES 26 A 552 LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS
SEQRES 27 A 552 ASN ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 28 A 552 LEU GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA
SEQRES 29 A 552 GLU GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA
SEQRES 30 A 552 ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP
SEQRES 31 A 552 TYR PRO LEU GLU ALA VAL ARG MET GLN HIS LEU ILE ALA
SEQRES 32 A 552 ARG GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE
SEQRES 33 A 552 GLU GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO
SEQRES 34 A 552 THR GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE
SEQRES 35 A 552 LYS CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER
SEQRES 36 A 552 GLY ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG
SEQRES 37 A 552 ALA PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA
SEQRES 38 A 552 ARG GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU
SEQRES 39 A 552 CYS LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL
SEQRES 40 A 552 ASP LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA
SEQRES 41 A 552 ARG GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU
SEQRES 42 A 552 THR GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET
SEQRES 43 A 552 ARG VAL VAL PRO VAL PRO
SEQRES 1 B 552 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 552 LEU VAL PRO ARG GLY SER HIS MET MET SER LYS PRO HIS
SEQRES 3 B 552 SER GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU
SEQRES 4 B 552 HIS ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS
SEQRES 5 B 552 ARG LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN
SEQRES 6 B 552 THR GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER
SEQRES 7 B 552 VAL GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN
SEQRES 8 B 552 VAL ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR
SEQRES 9 B 552 HIS ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU
SEQRES 10 B 552 SER PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA
SEQRES 11 B 552 VAL ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY
SEQRES 12 B 552 LEU ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS
SEQRES 13 B 552 LYS GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR
SEQRES 14 B 552 MET GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR
SEQRES 15 B 552 LYS ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE
SEQRES 16 B 552 TYR VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN
SEQRES 17 B 552 LYS GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY
SEQRES 18 B 552 GLY SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY
SEQRES 19 B 552 ALA ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE
SEQRES 20 B 552 GLN ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET
SEQRES 21 B 552 VAL PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS
SEQRES 22 B 552 GLU VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE
SEQRES 23 B 552 LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG
SEQRES 24 B 552 ARG PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET
SEQRES 25 B 552 VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU
SEQRES 26 B 552 LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS
SEQRES 27 B 552 ASN ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 28 B 552 LEU GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA
SEQRES 29 B 552 GLU GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA
SEQRES 30 B 552 ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP
SEQRES 31 B 552 TYR PRO LEU GLU ALA VAL ARG MET GLN HIS LEU ILE ALA
SEQRES 32 B 552 ARG GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE
SEQRES 33 B 552 GLU GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO
SEQRES 34 B 552 THR GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE
SEQRES 35 B 552 LYS CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER
SEQRES 36 B 552 GLY ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG
SEQRES 37 B 552 ALA PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA
SEQRES 38 B 552 ARG GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU
SEQRES 39 B 552 CYS LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL
SEQRES 40 B 552 ASP LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA
SEQRES 41 B 552 ARG GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU
SEQRES 42 B 552 THR GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET
SEQRES 43 B 552 ARG VAL VAL PRO VAL PRO
SEQRES 1 C 552 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 552 LEU VAL PRO ARG GLY SER HIS MET MET SER LYS PRO HIS
SEQRES 3 C 552 SER GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU
SEQRES 4 C 552 HIS ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS
SEQRES 5 C 552 ARG LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN
SEQRES 6 C 552 THR GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER
SEQRES 7 C 552 VAL GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN
SEQRES 8 C 552 VAL ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR
SEQRES 9 C 552 HIS ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU
SEQRES 10 C 552 SER PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA
SEQRES 11 C 552 VAL ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY
SEQRES 12 C 552 LEU ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS
SEQRES 13 C 552 LYS GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR
SEQRES 14 C 552 MET GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR
SEQRES 15 C 552 LYS ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE
SEQRES 16 C 552 TYR VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN
SEQRES 17 C 552 LYS GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY
SEQRES 18 C 552 GLY SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY
SEQRES 19 C 552 ALA ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE
SEQRES 20 C 552 GLN ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET
SEQRES 21 C 552 VAL PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS
SEQRES 22 C 552 GLU VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE
SEQRES 23 C 552 LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG
SEQRES 24 C 552 ARG PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET
SEQRES 25 C 552 VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU
SEQRES 26 C 552 LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS
SEQRES 27 C 552 ASN ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 28 C 552 LEU GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA
SEQRES 29 C 552 GLU GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA
SEQRES 30 C 552 ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP
SEQRES 31 C 552 TYR PRO LEU GLU ALA VAL ARG MET GLN HIS LEU ILE ALA
SEQRES 32 C 552 ARG GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE
SEQRES 33 C 552 GLU GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO
SEQRES 34 C 552 THR GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE
SEQRES 35 C 552 LYS CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER
SEQRES 36 C 552 GLY ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG
SEQRES 37 C 552 ALA PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA
SEQRES 38 C 552 ARG GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU
SEQRES 39 C 552 CYS LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL
SEQRES 40 C 552 ASP LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA
SEQRES 41 C 552 ARG GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU
SEQRES 42 C 552 THR GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET
SEQRES 43 C 552 ARG VAL VAL PRO VAL PRO
SEQRES 1 D 552 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 552 LEU VAL PRO ARG GLY SER HIS MET MET SER LYS PRO HIS
SEQRES 3 D 552 SER GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU
SEQRES 4 D 552 HIS ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS
SEQRES 5 D 552 ARG LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN
SEQRES 6 D 552 THR GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER
SEQRES 7 D 552 VAL GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN
SEQRES 8 D 552 VAL ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR
SEQRES 9 D 552 HIS ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU
SEQRES 10 D 552 SER PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA
SEQRES 11 D 552 VAL ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY
SEQRES 12 D 552 LEU ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS
SEQRES 13 D 552 LYS GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR
SEQRES 14 D 552 MET GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR
SEQRES 15 D 552 LYS ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE
SEQRES 16 D 552 TYR VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN
SEQRES 17 D 552 LYS GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY
SEQRES 18 D 552 GLY SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY
SEQRES 19 D 552 ALA ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE
SEQRES 20 D 552 GLN ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET
SEQRES 21 D 552 VAL PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS
SEQRES 22 D 552 GLU VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE
SEQRES 23 D 552 LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG
SEQRES 24 D 552 ARG PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET
SEQRES 25 D 552 VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU
SEQRES 26 D 552 LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS
SEQRES 27 D 552 ASN ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 28 D 552 LEU GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA
SEQRES 29 D 552 GLU GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA
SEQRES 30 D 552 ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP
SEQRES 31 D 552 TYR PRO LEU GLU ALA VAL ARG MET GLN HIS LEU ILE ALA
SEQRES 32 D 552 ARG GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE
SEQRES 33 D 552 GLU GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO
SEQRES 34 D 552 THR GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE
SEQRES 35 D 552 LYS CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER
SEQRES 36 D 552 GLY ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG
SEQRES 37 D 552 ALA PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA
SEQRES 38 D 552 ARG GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU
SEQRES 39 D 552 CYS LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL
SEQRES 40 D 552 ASP LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA
SEQRES 41 D 552 ARG GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU
SEQRES 42 D 552 THR GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET
SEQRES 43 D 552 ARG VAL VAL PRO VAL PRO
HET SER A 601 7
HET PO4 A 602 5
HET SER B 601 7
HET PO4 B 602 5
HET SER C 601 7
HET PO4 C 602 5
HET SER D 601 7
HETNAM SER SERINE
HETNAM PO4 PHOSPHATE ION
FORMUL 5 SER 4(C3 H7 N O3)
FORMUL 6 PO4 3(O4 P 3-)
FORMUL 12 HOH *488(H2 O)
HELIX 1 AA1 THR A 25 ARG A 32 1 8
HELIX 2 AA2 SER A 57 GLY A 68 1 12
HELIX 3 AA3 THR A 80 SER A 97 1 18
HELIX 4 AA4 ASP A 145 MET A 149 5 5
HELIX 5 AA5 ASN A 163 VAL A 168 1 6
HELIX 6 AA6 SER A 222 GLN A 235 1 14
HELIX 7 AA7 LYS A 247 GLY A 259 1 13
HELIX 8 AA8 ASN A 273 ARG A 279 1 7
HELIX 9 AA9 ARG A 279 SER A 287 1 9
HELIX 10 AB1 ARG A 294 ILE A 301 1 8
HELIX 11 AB2 PRO A 302 GLU A 304 5 3
HELIX 12 AB3 LYS A 305 GLY A 321 1 17
HELIX 13 AB4 LEU A 331 LYS A 336 5 6
HELIX 14 AB5 THR A 341 ASP A 354 1 14
HELIX 15 AB6 SER A 362 LYS A 367 1 6
HELIX 16 AB7 TYR A 370 GLU A 386 1 17
HELIX 17 AB8 ALA A 387 ILE A 389 5 3
HELIX 18 AB9 TYR A 390 LEU A 401 1 12
HELIX 19 AC1 ASP A 407 CYS A 423 1 17
HELIX 20 AC2 GLY A 435 TYR A 444 1 10
HELIX 21 AC3 ASN A 456 ALA A 463 1 8
HELIX 22 AC4 HIS A 464 TYR A 466 5 3
HELIX 23 AC5 ALA A 481 ARG A 500 1 20
HELIX 24 AC6 THR B 25 ARG B 32 1 8
HELIX 25 AC7 SER B 57 GLY B 68 1 12
HELIX 26 AC8 THR B 80 SER B 97 1 18
HELIX 27 AC9 ASN B 163 VAL B 168 1 6
HELIX 28 AD1 SER B 222 GLN B 235 1 14
HELIX 29 AD2 LYS B 247 GLY B 259 1 13
HELIX 30 AD3 ASN B 273 ARG B 279 1 7
HELIX 31 AD4 ARG B 279 SER B 287 1 9
HELIX 32 AD5 ARG B 294 ILE B 301 1 8
HELIX 33 AD6 LYS B 305 GLY B 321 1 17
HELIX 34 AD7 LEU B 331 LYS B 336 5 6
HELIX 35 AD8 THR B 341 GLY B 355 1 15
HELIX 36 AD9 SER B 362 LYS B 367 1 6
HELIX 37 AE1 TYR B 370 ALA B 387 1 18
HELIX 38 AE2 TYR B 390 ALA B 402 1 13
HELIX 39 AE3 ASP B 407 CYS B 423 1 17
HELIX 40 AE4 GLY B 435 ARG B 443 1 9
HELIX 41 AE5 ASN B 456 ALA B 463 1 8
HELIX 42 AE6 HIS B 464 TYR B 466 5 3
HELIX 43 AE7 ALA B 481 ARG B 500 1 20
HELIX 44 AE8 THR C 25 ARG C 32 1 8
HELIX 45 AE9 SER C 57 GLY C 68 1 12
HELIX 46 AF1 THR C 80 SER C 97 1 18
HELIX 47 AF2 ASN C 163 VAL C 168 1 6
HELIX 48 AF3 SER C 222 ASP C 236 1 15
HELIX 49 AF4 LYS C 247 GLY C 259 1 13
HELIX 50 AF5 ASN C 273 ARG C 279 1 7
HELIX 51 AF6 ARG C 279 SER C 287 1 9
HELIX 52 AF7 ARG C 294 ILE C 301 1 8
HELIX 53 AF8 PRO C 302 GLU C 304 5 3
HELIX 54 AF9 LYS C 305 GLY C 321 1 17
HELIX 55 AG1 LEU C 331 LYS C 336 5 6
HELIX 56 AG2 THR C 341 GLY C 355 1 15
HELIX 57 AG3 SER C 362 LYS C 367 1 6
HELIX 58 AG4 TYR C 370 ALA C 388 1 19
HELIX 59 AG5 TYR C 390 ALA C 402 1 13
HELIX 60 AG6 ASP C 407 CYS C 423 1 17
HELIX 61 AG7 GLY C 435 ARG C 443 1 9
HELIX 62 AG8 ASN C 456 ALA C 463 1 8
HELIX 63 AG9 HIS C 464 TYR C 466 5 3
HELIX 64 AH1 ALA C 481 ARG C 500 1 20
HELIX 65 AH2 THR D 25 ARG D 32 1 8
HELIX 66 AH3 SER D 57 SER D 67 1 11
HELIX 67 AH4 THR D 80 SER D 97 1 18
HELIX 68 AH5 ASP D 101 TYR D 105 5 5
HELIX 69 AH6 ASN D 163 VAL D 168 1 6
HELIX 70 AH7 SER D 222 GLN D 235 1 14
HELIX 71 AH8 LYS D 247 GLY D 259 1 13
HELIX 72 AH9 ASN D 273 ARG D 279 1 7
HELIX 73 AI1 ARG D 279 SER D 287 1 9
HELIX 74 AI2 ARG D 294 ILE D 301 1 8
HELIX 75 AI3 PRO D 302 GLY D 321 1 20
HELIX 76 AI4 LEU D 331 LYS D 336 5 6
HELIX 77 AI5 THR D 341 GLY D 355 1 15
HELIX 78 AI6 SER D 362 LYS D 367 1 6
HELIX 79 AI7 TYR D 370 GLU D 386 1 17
HELIX 80 AI8 ALA D 387 ILE D 389 5 3
HELIX 81 AI9 TYR D 390 ALA D 402 1 13
HELIX 82 AJ1 ASP D 407 CYS D 423 1 17
HELIX 83 AJ2 GLY D 435 TYR D 444 1 10
HELIX 84 AJ3 ASN D 456 ALA D 463 1 8
HELIX 85 AJ4 HIS D 464 TYR D 466 5 3
HELIX 86 AJ5 ALA D 481 ARG D 500 1 20
SHEET 1 AA1 9 GLY A 46 THR A 50 0
SHEET 2 AA1 9 VAL A 71 ASN A 75 1 O ARG A 73 N CYS A 49
SHEET 3 AA1 9 ALA A 109 ASP A 113 1 O ALA A 109 N ALA A 72
SHEET 4 AA1 9 MET A 239 ALA A 242 1 O PHE A 241 N LEU A 112
SHEET 5 AA1 9 LYS A 266 ILE A 271 1 O ILE A 268 N VAL A 240
SHEET 6 AA1 9 GLY A 289 ALA A 293 1 O MET A 291 N ILE A 271
SHEET 7 AA1 9 VAL A 324 ALA A 327 1 O ILE A 325 N VAL A 292
SHEET 8 AA1 9 CYS A 358 LEU A 361 1 O CYS A 358 N CYS A 326
SHEET 9 AA1 9 GLY A 46 THR A 50 1 N ILE A 48 O LEU A 361
SHEET 1 AA2 2 VAL A 132 GLU A 133 0
SHEET 2 AA2 2 SER A 202 LEU A 203 -1 O LEU A 203 N VAL A 132
SHEET 1 AA3 6 ILE A 156 TRP A 158 0
SHEET 2 AA3 6 GLY A 137 THR A 143 1 N THR A 143 O LEU A 157
SHEET 3 AA3 6 LEU A 193 VAL A 197 -1 O THR A 195 N LEU A 140
SHEET 4 AA3 6 ILE A 181 LYS A 188 -1 N GLN A 184 O GLU A 196
SHEET 5 AA3 6 LYS A 173 VAL A 176 -1 N VAL A 176 O ILE A 181
SHEET 6 AA3 6 VAL A 209 ASN A 210 -1 O ASN A 210 N TYR A 175
SHEET 1 AA410 ILE A 469 LEU A 473 0
SHEET 2 AA410 ILE A 450 THR A 454 1 N ILE A 450 O PHE A 470
SHEET 3 AA410 ILE A 428 LEU A 431 1 N VAL A 430 O ILE A 451
SHEET 4 AA410 VAL A 508 THR A 513 1 O ILE A 510 N ILE A 429
SHEET 5 AA410 THR A 524 PRO A 529 -1 O ARG A 526 N VAL A 511
SHEET 6 AA410 THR C 524 PRO C 529 -1 O MET C 525 N MET A 525
SHEET 7 AA410 VAL C 508 THR C 513 -1 N VAL C 509 O VAL C 528
SHEET 8 AA410 ILE C 428 LEU C 431 1 N ILE C 429 O ILE C 510
SHEET 9 AA410 ILE C 450 THR C 454 1 O VAL C 453 N VAL C 430
SHEET 10 AA410 ILE C 469 LEU C 473 1 O PHE C 470 N ILE C 450
SHEET 1 AA5 9 GLY B 46 THR B 50 0
SHEET 2 AA5 9 VAL B 71 ASN B 75 1 O ARG B 73 N CYS B 49
SHEET 3 AA5 9 ALA B 109 ASP B 113 1 O ALA B 109 N ALA B 72
SHEET 4 AA5 9 MET B 239 ALA B 242 1 O PHE B 241 N LEU B 112
SHEET 5 AA5 9 LYS B 266 ILE B 271 1 O ILE B 268 N VAL B 240
SHEET 6 AA5 9 GLY B 289 ALA B 293 1 O MET B 291 N ILE B 271
SHEET 7 AA5 9 VAL B 324 ALA B 327 1 O ILE B 325 N VAL B 292
SHEET 8 AA5 9 CYS B 358 LEU B 361 1 O CYS B 358 N CYS B 326
SHEET 9 AA5 9 GLY B 46 THR B 50 1 N ILE B 48 O LEU B 361
SHEET 1 AA6 2 VAL B 132 LEU B 134 0
SHEET 2 AA6 2 GLY B 201 LEU B 203 -1 O GLY B 201 N LEU B 134
SHEET 1 AA7 6 ILE B 156 TRP B 158 0
SHEET 2 AA7 6 THR B 139 THR B 143 1 N THR B 143 O LEU B 157
SHEET 3 AA7 6 PHE B 192 ASN B 199 -1 O THR B 195 N LEU B 140
SHEET 4 AA7 6 ILE B 181 LYS B 188 -1 N SER B 182 O GLU B 198
SHEET 5 AA7 6 LYS B 173 VAL B 176 -1 N ILE B 174 O LEU B 183
SHEET 6 AA7 6 VAL B 209 ASN B 210 -1 O ASN B 210 N TYR B 175
SHEET 1 AA810 ILE B 469 LEU B 473 0
SHEET 2 AA810 ILE B 450 THR B 454 1 N ILE B 450 O PHE B 470
SHEET 3 AA810 ILE B 428 LEU B 431 1 N VAL B 430 O ILE B 451
SHEET 4 AA810 VAL B 508 THR B 513 1 O ILE B 510 N ILE B 429
SHEET 5 AA810 THR B 524 PRO B 529 -1 O ARG B 526 N VAL B 511
SHEET 6 AA810 THR D 524 PRO D 529 -1 O MET D 525 N MET B 525
SHEET 7 AA810 VAL D 508 THR D 513 -1 N VAL D 511 O ARG D 526
SHEET 8 AA810 ILE D 428 LEU D 431 1 N ILE D 429 O ILE D 510
SHEET 9 AA810 ILE D 450 THR D 454 1 O VAL D 453 N VAL D 430
SHEET 10 AA810 ILE D 469 LEU D 473 1 O PHE D 470 N ILE D 450
SHEET 1 AA9 9 GLY C 46 THR C 50 0
SHEET 2 AA9 9 VAL C 71 ASN C 75 1 O VAL C 71 N CYS C 49
SHEET 3 AA9 9 ALA C 109 ASP C 113 1 O ASP C 113 N LEU C 74
SHEET 4 AA9 9 MET C 239 ALA C 242 1 O PHE C 241 N LEU C 112
SHEET 5 AA9 9 LYS C 266 ILE C 271 1 O ILE C 268 N VAL C 240
SHEET 6 AA9 9 GLY C 289 ALA C 293 1 O MET C 291 N ILE C 271
SHEET 7 AA9 9 VAL C 324 ALA C 327 1 O ILE C 325 N VAL C 292
SHEET 8 AA9 9 CYS C 358 LEU C 361 1 O CYS C 358 N CYS C 326
SHEET 9 AA9 9 GLY C 46 THR C 50 1 N ILE C 48 O ILE C 359
SHEET 1 AB1 2 VAL C 132 LEU C 134 0
SHEET 2 AB1 2 GLY C 201 LEU C 203 -1 O GLY C 201 N LEU C 134
SHEET 1 AB2 6 ILE C 156 TRP C 158 0
SHEET 2 AB2 6 THR C 139 THR C 143 1 N LYS C 141 O LEU C 157
SHEET 3 AB2 6 PHE C 192 VAL C 197 -1 O THR C 195 N LEU C 140
SHEET 4 AB2 6 ILE C 181 LYS C 188 -1 N LYS C 186 O VAL C 194
SHEET 5 AB2 6 LYS C 173 VAL C 176 -1 N ILE C 174 O LEU C 183
SHEET 6 AB2 6 VAL C 209 ASN C 210 -1 O ASN C 210 N TYR C 175
SHEET 1 AB3 9 GLY D 46 THR D 50 0
SHEET 2 AB3 9 VAL D 71 ASN D 75 1 O ARG D 73 N CYS D 49
SHEET 3 AB3 9 ALA D 109 ASP D 113 1 O ALA D 111 N ALA D 72
SHEET 4 AB3 9 MET D 239 ALA D 242 1 O PHE D 241 N LEU D 112
SHEET 5 AB3 9 LYS D 266 ILE D 271 1 O ILE D 268 N VAL D 240
SHEET 6 AB3 9 GLY D 289 ALA D 293 1 O MET D 291 N ILE D 271
SHEET 7 AB3 9 VAL D 324 ALA D 327 1 O ILE D 325 N VAL D 292
SHEET 8 AB3 9 CYS D 358 LEU D 361 1 O MET D 360 N CYS D 326
SHEET 9 AB3 9 GLY D 46 THR D 50 1 N ILE D 48 O LEU D 361
SHEET 1 AB4 7 ILE D 119 ARG D 120 0
SHEET 2 AB4 7 GLY D 208 ASN D 210 -1 O VAL D 209 N ILE D 119
SHEET 3 AB4 7 LYS D 173 VAL D 176 -1 N TYR D 175 O ASN D 210
SHEET 4 AB4 7 ILE D 181 LYS D 188 -1 O LEU D 183 N ILE D 174
SHEET 5 AB4 7 PHE D 192 ASN D 199 -1 O GLU D 198 N SER D 182
SHEET 6 AB4 7 LYS D 141 THR D 143 -1 N ILE D 142 O LEU D 193
SHEET 7 AB4 7 ILE D 156 TRP D 158 1 O LEU D 157 N THR D 143
SHEET 1 AB5 2 VAL D 132 LEU D 134 0
SHEET 2 AB5 2 GLY D 201 LEU D 203 -1 O LEU D 203 N VAL D 132
SITE 1 AC1 9 ARG A 43 ASN A 44 ASN A 70 HIS A 464
SITE 2 AC1 9 ILE A 469 PHE A 470 HOH A 713 HOH A 747
SITE 3 AC1 9 HOH A 777
SITE 1 AC2 7 THR A 432 LYS A 433 SER A 434 GLY A 435
SITE 2 AC2 7 ARG A 436 SER A 437 THR A 522
SITE 1 AC3 9 ARG B 43 ASN B 44 THR B 45 ASN B 70
SITE 2 AC3 9 HIS B 464 ILE B 469 PHE B 470 HOH B 723
SITE 3 AC3 9 HOH B 774
SITE 1 AC4 6 THR B 432 LYS B 433 SER B 434 GLY B 435
SITE 2 AC4 6 ARG B 436 SER B 437
SITE 1 AC5 10 ARG C 43 ASN C 44 ASN C 70 HIS C 464
SITE 2 AC5 10 ILE C 469 PHE C 470 HOH C 703 HOH C 730
SITE 3 AC5 10 HOH C 742 HOH C 748
SITE 1 AC6 5 THR C 432 LYS C 433 SER C 434 ARG C 436
SITE 2 AC6 5 SER C 437
SITE 1 AC7 7 ARG D 43 ASN D 44 ASN D 70 HIS D 464
SITE 2 AC7 7 ILE D 469 PHE D 470 HOH D 722
CRYST1 76.763 152.573 94.405 90.00 97.88 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 0.013027 0.000000 0.001804 0.00000
SCALE2 0.000000 0.006554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010694 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
