HEADER TRANSFERASE 02-MAY-18 6GG4
TITLE CRYSTAL STRUCTURE OF M2 PYK IN COMPLEX WITH PHENYALANINE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE PKM;
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 GLYCOLYSIS, PYRUVATE KINASE ACTIVITY, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.W.MCNAE,M.YUAN,M.D.WALKINSHAW
REVDAT 3 17-JAN-24 6GG4 1 LINK
REVDAT 2 13-JUN-18 6GG4 1 JRNL
REVDAT 1 23-MAY-18 6GG4 0
JRNL AUTH M.YUAN,I.W.MCNAE,Y.CHEN,E.A.BLACKBURN,M.A.WEAR,
JRNL AUTH 2 P.A.M.MICHELS,L.A.FOTHERGILL-GILMORE,T.HUPP,M.D.WALKINSHAW
JRNL TITL AN ALLOSTATIC MECHANISM FOR M2 PYRUVATE KINASE AS AN
JRNL TITL 2 AMINO-ACID SENSOR.
JRNL REF BIOCHEM. J. V. 475 1821 2018
JRNL REFN ESSN 1470-8728
JRNL PMID 29748232
JRNL DOI 10.1042/BCJ20180171
REMARK 2
REMARK 2 RESOLUTION. 2.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 2.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 162.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 75137
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3904
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) : 2.46
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5603
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 270
REMARK 3 BIN FREE R VALUE : 0.2950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14102
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 353
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.23000
REMARK 3 B22 (A**2) : -1.35000
REMARK 3 B33 (A**2) : -0.39000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.461
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.249
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.184
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.742
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14470 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 14001 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19556 ; 1.272 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 32411 ; 0.898 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1844 ; 5.302 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 608 ;35.893 ;23.421
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2591 ;13.615 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 127 ;16.768 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2234 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 16005 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2846 ; 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): 7370 ; 1.892 ; 5.249
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7369 ; 1.892 ; 5.249
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9198 ; 3.214 ; 7.868
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 9199 ; 3.214 ; 7.868
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7100 ; 1.975 ; 5.549
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 7100 ; 1.975 ; 5.549
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 10353 ; 3.362 ; 8.223
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 15363 ; 5.361 ;61.742
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 15328 ; 5.347 ;61.696
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 23 531 B 23 531 31478 0.05 0.05
REMARK 3 2 A 23 530 C 23 530 25584 0.06 0.05
REMARK 3 3 A 23 530 D 23 530 25676 0.05 0.05
REMARK 3 4 B 23 530 C 23 530 25634 0.05 0.05
REMARK 3 5 B 23 530 D 23 530 25690 0.05 0.05
REMARK 3 6 C 23 531 D 23 531 25712 0.05 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 23 A 605
REMARK 3 ORIGIN FOR THE GROUP (A): 377.6890 -76.5902 205.7526
REMARK 3 T TENSOR
REMARK 3 T11: 0.0731 T22: 0.1223
REMARK 3 T33: 0.0330 T12: 0.0624
REMARK 3 T13: -0.0085 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.4732 L22: 0.1653
REMARK 3 L33: 0.7426 L12: -0.2648
REMARK 3 L13: 0.2391 L23: -0.1889
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: 0.0126 S13: 0.0231
REMARK 3 S21: -0.0126 S22: 0.0041 S23: 0.0028
REMARK 3 S31: 0.0266 S32: 0.0779 S33: -0.0149
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 23 B 605
REMARK 3 ORIGIN FOR THE GROUP (A): 318.7491 -36.1165 207.9760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0460 T22: 0.1075
REMARK 3 T33: 0.0810 T12: 0.0570
REMARK 3 T13: 0.0161 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.3504 L22: 0.4754
REMARK 3 L33: 0.7839 L12: -0.3969
REMARK 3 L13: 0.0587 L23: -0.1124
REMARK 3 S TENSOR
REMARK 3 S11: 0.0234 S12: 0.0173 S13: -0.0223
REMARK 3 S21: -0.0189 S22: -0.0032 S23: -0.0135
REMARK 3 S31: -0.0489 S32: -0.1431 S33: -0.0202
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 23 C 531
REMARK 3 ORIGIN FOR THE GROUP (A): 337.0282 -48.3493 175.7193
REMARK 3 T TENSOR
REMARK 3 T11: 0.1254 T22: 0.0811
REMARK 3 T33: 0.0274 T12: 0.0218
REMARK 3 T13: -0.0132 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.2444 L22: 0.3458
REMARK 3 L33: 0.6337 L12: -0.2490
REMARK 3 L13: -0.0245 L23: -0.0246
REMARK 3 S TENSOR
REMARK 3 S11: -0.0564 S12: 0.0168 S13: 0.0148
REMARK 3 S21: 0.0390 S22: 0.0519 S23: 0.0161
REMARK 3 S31: 0.0144 S32: -0.0066 S33: 0.0045
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 23 D 531
REMARK 3 ORIGIN FOR THE GROUP (A): 347.7482 -80.6729 230.6611
REMARK 3 T TENSOR
REMARK 3 T11: 0.0946 T22: 0.0813
REMARK 3 T33: 0.0220 T12: 0.0311
REMARK 3 T13: -0.0059 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.6838 L22: 0.4189
REMARK 3 L33: 0.6505 L12: -0.2646
REMARK 3 L13: -0.1624 L23: -0.0656
REMARK 3 S TENSOR
REMARK 3 S11: -0.0265 S12: -0.1008 S13: -0.0201
REMARK 3 S21: 0.0391 S22: 0.0113 S23: 0.0353
REMARK 3 S31: -0.0067 S32: 0.0367 S33: 0.0153
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 6GG4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1200009886.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2-7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9174
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80146
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.460
REMARK 200 RESOLUTION RANGE LOW (A) : 162.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.52
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4FXJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-16% PEG 3350, 100 MM SODIUM
REMARK 280 CACODYLATE, 50 MM MGCL2, 100 MM KCL,, VAPOR DIFFUSION, HANGING
REMARK 280 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 35.17000
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: 17110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER 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 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS 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 GLU A 7
REMARK 465 ALA A 8
REMARK 465 GLY A 9
REMARK 465 THR A 10
REMARK 465 ALA A 11
REMARK 465 PHE A 12
REMARK 465 ILE A 13
REMARK 465 GLN A 14
REMARK 465 THR A 15
REMARK 465 GLN A 16
REMARK 465 GLN A 17
REMARK 465 LEU A 18
REMARK 465 HIS A 19
REMARK 465 ALA A 20
REMARK 465 ALA A 21
REMARK 465 MET A 22
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER 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 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS 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 SER B 6
REMARK 465 GLU B 7
REMARK 465 ALA B 8
REMARK 465 GLY B 9
REMARK 465 THR B 10
REMARK 465 ALA B 11
REMARK 465 PHE B 12
REMARK 465 ILE B 13
REMARK 465 GLN B 14
REMARK 465 THR B 15
REMARK 465 GLN B 16
REMARK 465 GLN B 17
REMARK 465 LEU B 18
REMARK 465 HIS B 19
REMARK 465 ALA B 20
REMARK 465 ALA B 21
REMARK 465 MET B 22
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER 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 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS 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 SER C 6
REMARK 465 GLU C 7
REMARK 465 ALA C 8
REMARK 465 GLY C 9
REMARK 465 THR C 10
REMARK 465 ALA C 11
REMARK 465 PHE C 12
REMARK 465 ILE C 13
REMARK 465 GLN C 14
REMARK 465 THR C 15
REMARK 465 GLN C 16
REMARK 465 GLN C 17
REMARK 465 LEU C 18
REMARK 465 HIS C 19
REMARK 465 ALA C 20
REMARK 465 ALA C 21
REMARK 465 MET C 22
REMARK 465 ILE C 119
REMARK 465 ARG C 120
REMARK 465 THR C 121
REMARK 465 GLY C 122
REMARK 465 LEU C 123
REMARK 465 ILE C 124
REMARK 465 LYS C 125
REMARK 465 GLY C 126
REMARK 465 SER C 127
REMARK 465 GLY C 128
REMARK 465 THR C 129
REMARK 465 ALA C 130
REMARK 465 GLU C 131
REMARK 465 VAL C 132
REMARK 465 GLU C 133
REMARK 465 LEU C 134
REMARK 465 LYS C 135
REMARK 465 LYS C 136
REMARK 465 GLY C 137
REMARK 465 ALA C 138
REMARK 465 THR C 139
REMARK 465 LEU C 140
REMARK 465 LYS C 141
REMARK 465 ILE C 142
REMARK 465 THR C 143
REMARK 465 LEU C 144
REMARK 465 ASP C 145
REMARK 465 ASN C 146
REMARK 465 ALA C 147
REMARK 465 TYR C 148
REMARK 465 MET C 149
REMARK 465 GLU C 150
REMARK 465 LYS C 151
REMARK 465 CYS C 152
REMARK 465 ASP C 153
REMARK 465 GLU C 154
REMARK 465 ASN C 155
REMARK 465 ILE C 156
REMARK 465 LEU C 157
REMARK 465 TRP C 158
REMARK 465 LEU C 159
REMARK 465 ASP C 160
REMARK 465 TYR C 161
REMARK 465 LYS C 162
REMARK 465 ASN C 163
REMARK 465 ILE C 164
REMARK 465 CYS C 165
REMARK 465 LYS C 166
REMARK 465 VAL C 167
REMARK 465 VAL C 168
REMARK 465 GLU C 169
REMARK 465 VAL C 170
REMARK 465 GLY C 171
REMARK 465 SER C 172
REMARK 465 LYS C 173
REMARK 465 ILE C 174
REMARK 465 TYR C 175
REMARK 465 VAL C 176
REMARK 465 ASP C 177
REMARK 465 ASP C 178
REMARK 465 GLY C 179
REMARK 465 LEU C 180
REMARK 465 ILE C 181
REMARK 465 SER C 182
REMARK 465 LEU C 183
REMARK 465 GLN C 184
REMARK 465 VAL C 185
REMARK 465 LYS C 186
REMARK 465 GLN C 187
REMARK 465 LYS C 188
REMARK 465 GLY C 189
REMARK 465 ALA C 190
REMARK 465 ASP C 191
REMARK 465 PHE C 192
REMARK 465 LEU C 193
REMARK 465 VAL C 194
REMARK 465 THR C 195
REMARK 465 GLU C 196
REMARK 465 VAL C 197
REMARK 465 GLU C 198
REMARK 465 ASN C 199
REMARK 465 GLY C 200
REMARK 465 GLY C 201
REMARK 465 SER C 202
REMARK 465 LEU C 203
REMARK 465 GLY C 204
REMARK 465 SER C 205
REMARK 465 LYS C 206
REMARK 465 LYS C 207
REMARK 465 GLY C 208
REMARK 465 VAL C 209
REMARK 465 ASN C 210
REMARK 465 LEU C 211
REMARK 465 PRO C 212
REMARK 465 GLY C 213
REMARK 465 ALA C 214
REMARK 465 ALA C 215
REMARK 465 VAL C 216
REMARK 465 ASP C 217
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER 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 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS 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 GLU D 7
REMARK 465 ALA D 8
REMARK 465 GLY D 9
REMARK 465 THR D 10
REMARK 465 ALA D 11
REMARK 465 PHE D 12
REMARK 465 ILE D 13
REMARK 465 GLN D 14
REMARK 465 THR D 15
REMARK 465 GLN D 16
REMARK 465 GLN D 17
REMARK 465 LEU D 18
REMARK 465 HIS D 19
REMARK 465 ALA D 20
REMARK 465 ALA D 21
REMARK 465 MET D 22
REMARK 465 ILE D 119
REMARK 465 ARG D 120
REMARK 465 THR D 121
REMARK 465 GLY D 122
REMARK 465 LEU D 123
REMARK 465 ILE D 124
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 130
REMARK 465 GLU D 131
REMARK 465 VAL D 132
REMARK 465 GLU D 133
REMARK 465 LEU D 134
REMARK 465 LYS D 135
REMARK 465 LYS D 136
REMARK 465 GLY D 137
REMARK 465 ALA D 138
REMARK 465 THR D 139
REMARK 465 LEU D 140
REMARK 465 LYS D 141
REMARK 465 ILE D 142
REMARK 465 THR D 143
REMARK 465 LEU D 144
REMARK 465 ASP D 145
REMARK 465 ASN D 146
REMARK 465 ALA D 147
REMARK 465 TYR D 148
REMARK 465 MET D 149
REMARK 465 GLU D 150
REMARK 465 LYS D 151
REMARK 465 CYS D 152
REMARK 465 ASP D 153
REMARK 465 GLU D 154
REMARK 465 ASN D 155
REMARK 465 ILE D 156
REMARK 465 LEU D 157
REMARK 465 TRP D 158
REMARK 465 LEU D 159
REMARK 465 ASP D 160
REMARK 465 TYR D 161
REMARK 465 LYS D 162
REMARK 465 ASN D 163
REMARK 465 ILE D 164
REMARK 465 CYS D 165
REMARK 465 LYS D 166
REMARK 465 VAL D 167
REMARK 465 VAL D 168
REMARK 465 GLU D 169
REMARK 465 VAL D 170
REMARK 465 GLY D 171
REMARK 465 SER D 172
REMARK 465 LYS D 173
REMARK 465 ILE D 174
REMARK 465 TYR D 175
REMARK 465 VAL D 176
REMARK 465 ASP D 177
REMARK 465 ASP D 178
REMARK 465 GLY D 179
REMARK 465 LEU D 180
REMARK 465 ILE D 181
REMARK 465 SER D 182
REMARK 465 LEU D 183
REMARK 465 GLN D 184
REMARK 465 VAL D 185
REMARK 465 LYS D 186
REMARK 465 GLN D 187
REMARK 465 LYS D 188
REMARK 465 GLY D 189
REMARK 465 ALA D 190
REMARK 465 ASP D 191
REMARK 465 PHE D 192
REMARK 465 LEU D 193
REMARK 465 VAL D 194
REMARK 465 THR D 195
REMARK 465 GLU D 196
REMARK 465 VAL D 197
REMARK 465 GLU D 198
REMARK 465 ASN D 199
REMARK 465 GLY D 200
REMARK 465 GLY D 201
REMARK 465 SER D 202
REMARK 465 LEU D 203
REMARK 465 GLY D 204
REMARK 465 SER D 205
REMARK 465 LYS D 206
REMARK 465 LYS D 207
REMARK 465 GLY D 208
REMARK 465 VAL D 209
REMARK 465 ASN D 210
REMARK 465 LEU D 211
REMARK 465 PRO D 212
REMARK 465 GLY D 213
REMARK 465 ALA D 214
REMARK 465 ALA D 215
REMARK 465 VAL D 216
REMARK 465 ASP D 217
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 ARG B 443 NE - CZ - NH2 ANGL. DEV. = -3.3 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 130 37.99 -85.66
REMARK 500 ASP A 153 -154.58 -154.06
REMARK 500 ASP A 177 69.27 60.85
REMARK 500 THR A 328 145.41 72.77
REMARK 500 MET A 330 -75.07 -89.60
REMARK 500 SER A 362 -111.13 -107.10
REMARK 500 LYS A 422 -75.78 -77.14
REMARK 500 CYS A 424 67.31 -21.57
REMARK 500 ARG A 516 157.09 82.12
REMARK 500 ALA B 130 31.72 -83.66
REMARK 500 ASP B 153 -154.78 -153.38
REMARK 500 ASP B 177 69.21 61.52
REMARK 500 THR B 328 146.74 72.98
REMARK 500 MET B 330 -74.15 -90.72
REMARK 500 SER B 362 -111.07 -106.72
REMARK 500 LYS B 422 -75.79 -77.38
REMARK 500 CYS B 424 67.37 -20.81
REMARK 500 ARG B 516 156.42 82.22
REMARK 500 THR C 328 146.72 72.02
REMARK 500 MET C 330 -73.96 -90.30
REMARK 500 SER C 362 -110.84 -106.99
REMARK 500 LYS C 422 -75.50 -77.24
REMARK 500 CYS C 424 67.25 -21.08
REMARK 500 THR D 328 146.22 71.84
REMARK 500 MET D 330 -73.65 -90.01
REMARK 500 SER D 362 -111.54 -106.61
REMARK 500 LYS D 422 -75.50 -77.25
REMARK 500 CYS D 424 67.17 -21.53
REMARK 500 ARG D 516 155.55 84.56
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 K A 605 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 75 OD1
REMARK 620 2 SER A 77 OG 70.1
REMARK 620 3 ASP A 113 OD1 103.1 164.6
REMARK 620 4 THR A 114 O 123.8 105.2 66.4
REMARK 620 5 HOH A 708 O 142.0 74.9 114.4 79.3
REMARK 620 6 HOH A 770 O 85.0 105.7 87.0 143.6 90.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 605 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 75 OD1
REMARK 620 2 SER B 77 OG 70.2
REMARK 620 3 ASP B 113 OD1 102.3 165.5
REMARK 620 4 THR B 114 O 123.8 105.5 67.8
REMARK 620 5 HOH B 715 O 139.5 73.2 117.1 82.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 75 OD1
REMARK 620 2 SER C 77 OG 65.2
REMARK 620 3 ASP C 113 OD1 96.6 148.8
REMARK 620 4 THR C 114 O 110.1 99.9 61.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 75 OD1
REMARK 620 2 SER D 77 OG 65.7
REMARK 620 3 ASP D 113 OD1 101.9 156.4
REMARK 620 4 THR D 114 O 116.2 99.6 66.8
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 PO4 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 PHE A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHE B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHE C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PHE D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K D 603
DBREF 6GG4 A 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 6GG4 B 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 6GG4 C 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 6GG4 D 1 531 UNP P14618 KPYM_HUMAN 1 531
SEQADV 6GG4 MET A -19 UNP P14618 INITIATING METHIONINE
SEQADV 6GG4 GLY A -18 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER A -17 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER A -16 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS A -15 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS A -14 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS A -13 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS A -12 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS A -11 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS A -10 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER A -9 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER A -8 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 GLY A -7 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 LEU A -6 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 VAL A -5 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 PRO A -4 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 ARG A -3 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 GLY A -2 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER A -1 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS A 0 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 MET B -19 UNP P14618 INITIATING METHIONINE
SEQADV 6GG4 GLY B -18 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER B -17 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER B -16 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS B -15 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS B -14 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS B -13 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS B -12 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS B -11 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS B -10 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER B -9 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER B -8 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 GLY B -7 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 LEU B -6 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 VAL B -5 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 PRO B -4 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 ARG B -3 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 GLY B -2 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER B -1 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS B 0 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 MET C -19 UNP P14618 INITIATING METHIONINE
SEQADV 6GG4 GLY C -18 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER C -17 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER C -16 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS C -15 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS C -14 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS C -13 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS C -12 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS C -11 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS C -10 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER C -9 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER C -8 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 GLY C -7 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 LEU C -6 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 VAL C -5 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 PRO C -4 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 ARG C -3 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 GLY C -2 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER C -1 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS C 0 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 MET D -19 UNP P14618 INITIATING METHIONINE
SEQADV 6GG4 GLY D -18 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER D -17 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER D -16 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS D -15 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS D -14 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS D -13 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS D -12 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS D -11 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS D -10 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER D -9 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER D -8 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 GLY D -7 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 LEU D -6 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 VAL D -5 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 PRO D -4 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 ARG D -3 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 GLY D -2 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 SER D -1 UNP P14618 EXPRESSION TAG
SEQADV 6GG4 HIS D 0 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 CSO
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 CSO
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 CSO
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 CSO
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
MODRES 6GG4 CSO A 474 CYS MODIFIED RESIDUE
MODRES 6GG4 CSO B 474 CYS MODIFIED RESIDUE
MODRES 6GG4 CSO C 474 CYS MODIFIED RESIDUE
MODRES 6GG4 CSO D 474 CYS MODIFIED RESIDUE
HET CSO A 474 7
HET CSO B 474 7
HET CSO C 474 7
HET CSO D 474 7
HET PO4 A 601 5
HET PO4 A 602 5
HET PHE A 603 12
HET PO4 A 604 5
HET K A 605 1
HET PO4 B 601 5
HET PO4 B 602 5
HET PHE B 603 12
HET PO4 B 604 5
HET K B 605 1
HET PO4 C 601 5
HET PHE C 602 12
HET K C 603 1
HET PO4 D 601 5
HET PHE D 602 12
HET K D 603 1
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM PO4 PHOSPHATE ION
HETNAM PHE PHENYLALANINE
HETNAM K POTASSIUM ION
FORMUL 1 CSO 4(C3 H7 N O3 S)
FORMUL 5 PO4 8(O4 P 3-)
FORMUL 7 PHE 4(C9 H11 N O2)
FORMUL 9 K 4(K 1+)
FORMUL 21 HOH *353(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 GLY A 321 1 20
HELIX 12 AB3 LEU A 331 LYS A 336 5 6
HELIX 13 AB4 THR A 341 GLY A 355 1 15
HELIX 14 AB5 SER A 362 LYS A 367 1 6
HELIX 15 AB6 TYR A 370 GLU A 386 1 17
HELIX 16 AB7 ALA A 387 ILE A 389 5 3
HELIX 17 AB8 TYR A 390 ALA A 402 1 13
HELIX 18 AB9 ASP A 407 CYS A 423 1 17
HELIX 19 AC1 GLY A 435 ARG A 443 1 9
HELIX 20 AC2 ASN A 456 ALA A 463 1 8
HELIX 21 AC3 HIS A 464 TYR A 466 5 3
HELIX 22 AC4 ALA A 481 ARG A 500 1 20
HELIX 23 AC5 THR B 25 ARG B 32 1 8
HELIX 24 AC6 SER B 57 GLY B 68 1 12
HELIX 25 AC7 THR B 80 SER B 97 1 18
HELIX 26 AC8 ASP B 145 MET B 149 5 5
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 PRO B 302 GLY B 321 1 20
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 GLU B 386 1 17
HELIX 38 AE2 ALA B 387 ILE B 389 5 3
HELIX 39 AE3 TYR B 390 ALA B 402 1 13
HELIX 40 AE4 ASP B 407 CYS B 423 1 17
HELIX 41 AE5 GLY B 435 ARG B 443 1 9
HELIX 42 AE6 ASN B 456 ALA B 463 1 8
HELIX 43 AE7 HIS B 464 TYR B 466 5 3
HELIX 44 AE8 ALA B 481 ARG B 500 1 20
HELIX 45 AE9 THR C 25 ARG C 32 1 8
HELIX 46 AF1 SER C 57 GLY C 68 1 12
HELIX 47 AF2 THR C 80 SER C 97 1 18
HELIX 48 AF3 SER C 222 GLN C 235 1 14
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 GLY C 321 1 20
HELIX 54 AF9 LEU C 331 LYS C 336 5 6
HELIX 55 AG1 THR C 341 GLY C 355 1 15
HELIX 56 AG2 SER C 362 LYS C 367 1 6
HELIX 57 AG3 TYR C 370 GLU C 386 1 17
HELIX 58 AG4 ALA C 387 ILE C 389 5 3
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 GLY D 68 1 12
HELIX 67 AH4 THR D 80 SER D 97 1 18
HELIX 68 AH5 SER D 222 GLN D 235 1 14
HELIX 69 AH6 LYS D 247 GLY D 259 1 13
HELIX 70 AH7 ASN D 273 ARG D 279 1 7
HELIX 71 AH8 ARG D 279 SER D 287 1 9
HELIX 72 AH9 ARG D 294 ILE D 301 1 8
HELIX 73 AI1 PRO D 302 GLY D 321 1 20
HELIX 74 AI2 LEU D 331 LYS D 336 5 6
HELIX 75 AI3 THR D 341 GLY D 355 1 15
HELIX 76 AI4 SER D 362 LYS D 367 1 6
HELIX 77 AI5 TYR D 370 GLU D 386 1 17
HELIX 78 AI6 ALA D 387 ILE D 389 5 3
HELIX 79 AI7 TYR D 390 ALA D 402 1 13
HELIX 80 AI8 ASP D 407 CYS D 423 1 17
HELIX 81 AI9 GLY D 435 ARG D 443 1 9
HELIX 82 AJ1 ASN D 456 ALA D 463 1 8
HELIX 83 AJ2 HIS D 464 TYR D 466 5 3
HELIX 84 AJ3 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 111 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 MET A 360 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 7 ILE A 119 ARG A 120 0
SHEET 2 AA2 7 GLY A 208 ASN A 210 -1 O VAL A 209 N ILE A 119
SHEET 3 AA2 7 LYS A 173 VAL A 176 -1 N TYR A 175 O ASN A 210
SHEET 4 AA2 7 ILE A 181 LYS A 188 -1 O LEU A 183 N ILE A 174
SHEET 5 AA2 7 PHE A 192 ASN A 199 -1 O VAL A 194 N LYS A 186
SHEET 6 AA2 7 THR A 139 THR A 143 -1 N ILE A 142 O LEU A 193
SHEET 7 AA2 7 ILE A 156 TRP A 158 1 O LEU A 157 N LYS A 141
SHEET 1 AA3 2 VAL A 132 LEU A 134 0
SHEET 2 AA3 2 GLY A 201 LEU A 203 -1 O LEU A 203 N VAL A 132
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 VAL A 528 N VAL A 509
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 ILE C 451 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 111 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 MET B 360 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 LEU B 203 N VAL B 132
SHEET 1 AA7 6 ILE B 156 TRP B 158 0
SHEET 2 AA7 6 THR B 139 THR B 143 1 N LYS B 141 O LEU B 157
SHEET 3 AA7 6 PHE B 192 ASN B 199 -1 O LEU B 193 N ILE B 142
SHEET 4 AA7 6 ILE B 181 LYS B 188 -1 N LYS B 186 O VAL B 194
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 VAL B 528 N VAL B 509
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 509 O VAL D 528
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 ILE D 451 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 ARG C 73 N CYS C 49
SHEET 3 AA9 9 ALA C 109 ASP C 113 1 O ALA C 109 N ALA C 72
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 MET C 360 N CYS C 326
SHEET 9 AA9 9 GLY C 46 THR C 50 1 N ILE C 48 O LEU C 361
SHEET 1 AB1 9 GLY D 46 THR D 50 0
SHEET 2 AB1 9 VAL D 71 ASN D 75 1 O ARG D 73 N CYS D 49
SHEET 3 AB1 9 ALA D 109 ASP D 113 1 O ALA D 109 N ALA D 72
SHEET 4 AB1 9 MET D 239 ALA D 242 1 O PHE D 241 N LEU D 112
SHEET 5 AB1 9 LYS D 266 ILE D 271 1 O ILE D 268 N VAL D 240
SHEET 6 AB1 9 GLY D 289 ALA D 293 1 O MET D 291 N ILE D 271
SHEET 7 AB1 9 VAL D 324 ALA D 327 1 O ILE D 325 N VAL D 292
SHEET 8 AB1 9 CYS D 358 LEU D 361 1 O MET D 360 N CYS D 326
SHEET 9 AB1 9 GLY D 46 THR D 50 1 N ILE D 48 O LEU D 361
LINK C LEU A 473 N CSO A 474 1555 1555 1.33
LINK C CSO A 474 N LYS A 475 1555 1555 1.33
LINK C LEU B 473 N CSO B 474 1555 1555 1.33
LINK C CSO B 474 N LYS B 475 1555 1555 1.33
LINK C LEU C 473 N CSO C 474 1555 1555 1.33
LINK C CSO C 474 N LYS C 475 1555 1555 1.33
LINK C LEU D 473 N CSO D 474 1555 1555 1.33
LINK C CSO D 474 N LYS D 475 1555 1555 1.34
LINK OD1 ASN A 75 K K A 605 1555 1555 2.74
LINK OG SER A 77 K K A 605 1555 1555 2.85
LINK OD1 ASP A 113 K K A 605 1555 1555 3.06
LINK O THR A 114 K K A 605 1555 1555 2.73
LINK K K A 605 O HOH A 708 1555 1555 2.67
LINK K K A 605 O HOH A 770 1555 1555 2.98
LINK OD1 ASN B 75 K K B 605 1555 1555 2.75
LINK OG SER B 77 K K B 605 1555 1555 2.86
LINK OD1 ASP B 113 K K B 605 1555 1555 3.02
LINK O THR B 114 K K B 605 1555 1555 2.68
LINK K K B 605 O HOH B 715 1555 1555 2.81
LINK OD1 ASN C 75 K K C 603 1555 1555 3.00
LINK OG SER C 77 K K C 603 1555 1555 2.95
LINK OD1 ASP C 113 K K C 603 1555 1555 3.24
LINK O THR C 114 K K C 603 1555 1555 2.98
LINK OD1 ASN D 75 K K D 603 1555 1555 2.90
LINK OG SER D 77 K K D 603 1555 1555 3.04
LINK OD1 ASP D 113 K K D 603 1555 1555 2.96
LINK O THR D 114 K K D 603 1555 1555 2.81
SITE 1 AC1 7 THR A 432 LYS A 433 SER A 434 ARG A 436
SITE 2 AC1 7 SER A 437 HOH A 777 HOH A 782
SITE 1 AC2 4 ASN A 75 HIS A 78 ARG A 120 HOH A 715
SITE 1 AC3 8 ARG A 43 ASN A 44 ASN A 70 ARG A 106
SITE 2 AC3 8 HIS A 464 ILE A 469 PHE A 470 HOH A 755
SITE 1 AC4 6 SER A 77 HIS A 78 GLY A 79 LYS A 206
SITE 2 AC4 6 HOH A 713 THR B 80
SITE 1 AC5 6 ASN A 75 SER A 77 ASP A 113 THR A 114
SITE 2 AC5 6 HOH A 708 HOH A 770
SITE 1 AC6 6 THR B 432 LYS B 433 SER B 434 ARG B 436
SITE 2 AC6 6 SER B 437 HOH B 742
SITE 1 AC7 4 HIS B 78 ARG B 120 ASP B 178 HOH B 707
SITE 1 AC8 10 ARG B 43 ASN B 44 ASN B 70 ARG B 106
SITE 2 AC8 10 HIS B 464 GLY B 468 ILE B 469 PHE B 470
SITE 3 AC8 10 PRO B 471 HOH B 737
SITE 1 AC9 4 SER B 77 HIS B 78 GLY B 79 LYS B 206
SITE 1 AD1 5 ASN B 75 SER B 77 ASP B 113 THR B 114
SITE 2 AD1 5 HOH B 715
SITE 1 AD2 8 THR C 432 LYS C 433 SER C 434 ARG C 436
SITE 2 AD2 8 SER C 437 HOH C 707 HOH C 761 HOH C 762
SITE 1 AD3 11 ARG C 43 ASN C 44 ASN C 70 ARG C 106
SITE 2 AD3 11 HIS C 464 GLY C 468 ILE C 469 PHE C 470
SITE 3 AD3 11 PRO C 471 HOH C 701 HOH C 720
SITE 1 AD4 4 ASN C 75 SER C 77 ASP C 113 THR C 114
SITE 1 AD5 5 THR D 432 LYS D 433 SER D 434 SER D 437
SITE 2 AD5 5 HOH D 720
SITE 1 AD6 9 ARG D 43 ASN D 44 ASN D 70 ARG D 106
SITE 2 AD6 9 HIS D 464 GLY D 468 ILE D 469 PHE D 470
SITE 3 AD6 9 HOH D 726
SITE 1 AD7 4 ASN D 75 SER D 77 ASP D 113 THR D 114
CRYST1 97.370 70.340 168.640 90.00 106.06 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 0.010270 0.000000 0.002957 0.00000
SCALE2 0.000000 0.014217 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006171 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
