HEADER TRANSFERASE 06-MAR-12 4E1J
TITLE CRYSTAL STRUCTURE OF GLYCEROL KINASE IN COMPLEX WITH GLYCEROL FROM
TITLE 2 SINORHIZOBIUM MELILOTI 1021
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCEROL KINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ATP:GLYCEROL 3-PHOSPHOTRANSFERASE, GLYCEROKINASE, GK;
COMPND 5 EC: 2.7.1.30;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI;
SOURCE 3 ORGANISM_COMMON: ENSIFER MELILOTI;
SOURCE 4 ORGANISM_TAXID: 266834;
SOURCE 5 STRAIN: 1021;
SOURCE 6 GENE: GLPK, RB1135, SMB21009;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIPL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, NEW YORK STRUCTURAL GENOMICS
KEYWDS 2 RESEARCH CONSORTIUM, NYSGRC, GLYCEROL KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.AGARWAL,S.CHAMALA,B.EVANS,R.FOTI,A.GIZZI,B.HILLERICH,A.KAR,
AUTHOR 2 J.LAFLEUR,R.SIEDEL,G.VILLIGAS,W.ZENCHECK,S.C.ALMO,S.SWAMINATHAN,NEW
AUTHOR 3 YORK STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NYSGRC)
REVDAT 2 15-NOV-17 4E1J 1 REMARK
REVDAT 1 21-MAR-12 4E1J 0
JRNL AUTH R.AGARWAL,S.C.ALMO,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF GLYCEROL KINASE IN COMPLEX WITH
JRNL TITL 2 GLYCEROL FROM SINORHIZOBIUM MELILOTI 1021
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 81631
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4303
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) : 2.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5920
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 317
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14215
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.419
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.288
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.228
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.202
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14527 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19793 ; 1.671 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1903 ; 7.097 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 599 ;40.607 ;23.773
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2109 ;20.666 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 94 ;22.575 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2252 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11118 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 9498 ; 0.833 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14972 ; 1.526 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5029 ; 2.651 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4821 ; 3.828 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4E1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071051.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : SI-III
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86871
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.320
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AUTOSOL, PHENIX, CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NA-MALONATE, PH 7.0, 20% PEG
REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 50.98750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 MSE A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 VAL A 11
REMARK 465 LYS A 345
REMARK 465 ALA A 346
REMARK 465 ALA A 347
REMARK 465 PRO A 348
REMARK 465 ASP A 349
REMARK 465 ARG A 422
REMARK 465 ASN A 423
REMARK 465 GLY A 424
REMARK 465 ASN A 425
REMARK 465 ASP A 426
REMARK 465 ALA A 520
REMARK 465 MSE B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 VAL B 11
REMARK 465 ASP B 12
REMARK 465 LEU B 13
REMARK 465 GLY B 14
REMARK 465 THR B 15
REMARK 465 GLU B 16
REMARK 465 ASN B 17
REMARK 465 LEU B 18
REMARK 465 TYR B 19
REMARK 465 PHE B 20
REMARK 465 GLN B 21
REMARK 465 SER B 22
REMARK 465 MSE B 23
REMARK 465 MSE B 24
REMARK 465 GLY B 25
REMARK 465 LYS B 345
REMARK 465 ALA B 346
REMARK 465 ALA B 347
REMARK 465 PRO B 348
REMARK 465 ASP B 349
REMARK 465 ARG B 422
REMARK 465 ASN B 423
REMARK 465 GLY B 424
REMARK 465 ASN B 425
REMARK 465 ASP B 426
REMARK 465 ALA B 520
REMARK 465 MSE C 1
REMARK 465 HIS C 2
REMARK 465 HIS C 3
REMARK 465 HIS C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 LYS C 345
REMARK 465 ALA C 346
REMARK 465 ALA C 347
REMARK 465 PRO C 348
REMARK 465 ASP C 349
REMARK 465 ARG C 422
REMARK 465 ASN C 423
REMARK 465 GLY C 424
REMARK 465 ASN C 425
REMARK 465 ASP C 426
REMARK 465 ALA C 520
REMARK 465 MSE D 1
REMARK 465 HIS D 2
REMARK 465 HIS D 3
REMARK 465 HIS D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 SER D 8
REMARK 465 SER D 9
REMARK 465 GLY D 10
REMARK 465 VAL D 11
REMARK 465 ASP D 12
REMARK 465 LEU D 13
REMARK 465 GLY D 14
REMARK 465 THR D 15
REMARK 465 GLU D 16
REMARK 465 ASN D 17
REMARK 465 LEU D 18
REMARK 465 TYR D 19
REMARK 465 PHE D 20
REMARK 465 GLN D 21
REMARK 465 SER D 22
REMARK 465 MSE D 23
REMARK 465 MSE D 24
REMARK 465 GLY D 25
REMARK 465 ASP D 44
REMARK 465 GLY D 45
REMARK 465 ASN D 46
REMARK 465 GLN D 47
REMARK 465 SER D 64
REMARK 465 GLY D 65
REMARK 465 SER D 89
REMARK 465 GLY D 90
REMARK 465 ILE D 91
REMARK 465 PRO D 251
REMARK 465 SER D 252
REMARK 465 LEU D 253
REMARK 465 PHE D 254
REMARK 465 PRO D 279
REMARK 465 GLY D 280
REMARK 465 MSE D 281
REMARK 465 ASP D 299
REMARK 465 ALA D 346
REMARK 465 ALA D 347
REMARK 465 PRO D 348
REMARK 465 ASP D 349
REMARK 465 ARG D 421
REMARK 465 ARG D 422
REMARK 465 ASN D 423
REMARK 465 GLY D 424
REMARK 465 ASN D 425
REMARK 465 ASP D 426
REMARK 465 THR D 427
REMARK 465 VAL D 428
REMARK 465 LEU D 429
REMARK 465 VAL D 457
REMARK 465 ILE D 458
REMARK 465 LEU D 459
REMARK 465 GLU D 460
REMARK 465 THR D 461
REMARK 465 THR D 462
REMARK 465 ALA D 463
REMARK 465 LEU D 464
REMARK 465 GLY D 465
REMARK 465 VAL D 466
REMARK 465 ALA D 467
REMARK 465 TRP D 468
REMARK 465 LEU D 469
REMARK 465 ALA D 470
REMARK 465 GLY D 471
REMARK 465 SER D 472
REMARK 465 ARG D 473
REMARK 465 ALA D 474
REMARK 465 GLY D 475
REMARK 465 VAL D 476
REMARK 465 TRP D 477
REMARK 465 PRO D 478
REMARK 465 ASN D 479
REMARK 465 GLN D 480
REMARK 465 GLU D 481
REMARK 465 ALA D 482
REMARK 465 PHE D 483
REMARK 465 ALA D 520
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MSE A 23 CG SE CE
REMARK 470 MSE A 24 CG SE CE
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 LYS A 117 CG CD CE NZ
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 ARG A 230 CD NE CZ NH1 NH2
REMARK 470 LYS A 233 CG CD CE NZ
REMARK 470 LYS A 278 CG CD CE NZ
REMARK 470 LYS A 298 CG CD CE NZ
REMARK 470 LYS A 304 CG CD CE NZ
REMARK 470 ASP A 316 CG OD1 OD2
REMARK 470 LYS A 342 CG CD CE NZ
REMARK 470 VAL A 343 CG1 CG2
REMARK 470 ILE A 344 CG1 CG2 CD1
REMARK 470 THR A 350 OG1 CG2
REMARK 470 SER A 352 OG
REMARK 470 LEU A 353 CG CD1 CD2
REMARK 470 GLU A 355 CG CD OE1 OE2
REMARK 470 SER A 356 OG
REMARK 470 SER A 360 OG
REMARK 470 GLU A 362 CG CD OE1 OE2
REMARK 470 ARG A 390 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 421 CG CD NE CZ NH1 NH2
REMARK 470 THR A 427 OG1 CG2
REMARK 470 LYS A 485 CG CD CE NZ
REMARK 470 LYS A 503 CG CD CE NZ
REMARK 470 LYS A 507 CG CD CE NZ
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 GLU B 87 CG CD OE1 OE2
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 LYS B 140 CG CD CE NZ
REMARK 470 LYS B 144 CG CD CE NZ
REMARK 470 ARG B 230 CZ NH1 NH2
REMARK 470 LYS B 298 CG CD CE NZ
REMARK 470 LYS B 304 CE NZ
REMARK 470 LYS B 342 CG CD CE NZ
REMARK 470 VAL B 343 CG1 CG2
REMARK 470 ILE B 344 CG1 CG2 CD1
REMARK 470 THR B 350 OG1 CG2
REMARK 470 SER B 352 OG
REMARK 470 LEU B 353 CG CD1 CD2
REMARK 470 GLU B 355 CG CD OE1 OE2
REMARK 470 SER B 360 OG
REMARK 470 THR B 427 OG1 CG2
REMARK 470 LYS B 485 CG CD CE NZ
REMARK 470 LYS B 503 CG CD CE NZ
REMARK 470 LYS B 507 CG CD CE NZ
REMARK 470 HIS C 7 CG ND1 CD2 CE1 NE2
REMARK 470 SER C 8 OG
REMARK 470 VAL C 11 CG1 CG2
REMARK 470 LEU C 13 CG CD1 CD2
REMARK 470 MSE C 24 CG SE CE
REMARK 470 LYS C 48 CG CD CE NZ
REMARK 470 LYS C 83 CG CD CE NZ
REMARK 470 GLU C 87 CG CD OE1 OE2
REMARK 470 LYS C 117 CG CD CE NZ
REMARK 470 LYS C 136 CD CE NZ
REMARK 470 LYS C 139 CD CE NZ
REMARK 470 LYS C 140 CD CE NZ
REMARK 470 LYS C 144 CG CD CE NZ
REMARK 470 LYS C 148 CE NZ
REMARK 470 LYS C 233 CG CD CE NZ
REMARK 470 LEU C 253 CG CD1 CD2
REMARK 470 LYS C 278 CD CE NZ
REMARK 470 LYS C 298 CG CD CE NZ
REMARK 470 LYS C 304 CE NZ
REMARK 470 LYS C 342 CG CD CE NZ
REMARK 470 VAL C 343 CG1 CG2
REMARK 470 ILE C 344 CG1 CG2 CD1
REMARK 470 THR C 350 OG1 CG2
REMARK 470 SER C 352 OG
REMARK 470 LEU C 353 CG CD1 CD2
REMARK 470 GLU C 355 CG CD OE1 OE2
REMARK 470 SER C 360 OG
REMARK 470 ASN C 391 CG OD1 ND2
REMARK 470 ARG C 421 CG CD NE CZ NH1 NH2
REMARK 470 THR C 427 OG1 CG2
REMARK 470 ILE C 458 CG1 CG2 CD1
REMARK 470 LYS C 485 CG CD CE NZ
REMARK 470 LYS C 503 CG CD CE NZ
REMARK 470 LYS C 507 CG CD CE NZ
REMARK 470 LYS C 514 CD CE NZ
REMARK 470 ILE D 28 CG1 CG2 CD1
REMARK 470 LEU D 29 CG CD1 CD2
REMARK 470 ILE D 31 CG1 CG2 CD1
REMARK 470 ARG D 39 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 41 CG1 CG2 CD1
REMARK 470 VAL D 42 CG1 CG2
REMARK 470 PHE D 43 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 48 CG CD CE NZ
REMARK 470 ILE D 49 CG1 CG2 CD1
REMARK 470 VAL D 52 CG1 CG2
REMARK 470 GLN D 54 CG CD OE1 NE2
REMARK 470 LYS D 55 CG CD CE NZ
REMARK 470 PHE D 57 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 58 CG CD CE NZ
REMARK 470 GLN D 59 CG CD OE1 NE2
REMARK 470 HIS D 60 CG ND1 CD2 CE1 NE2
REMARK 470 PHE D 61 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 63 CG CD CE NZ
REMARK 470 GLU D 68 CG CD OE1 OE2
REMARK 470 GLU D 72 CG CD OE1 OE2
REMARK 470 GLU D 73 CG CD OE1 OE2
REMARK 470 ILE D 74 CG1 CG2 CD1
REMARK 470 GLN D 76 CG CD OE1 NE2
REMARK 470 THR D 77 OG1 CG2
REMARK 470 VAL D 78 CG1 CG2
REMARK 470 VAL D 79 CG1 CG2
REMARK 470 THR D 81 OG1 CG2
REMARK 470 VAL D 82 CG1 CG2
REMARK 470 LYS D 83 CG CD CE NZ
REMARK 470 GLU D 84 CG CD OE1 OE2
REMARK 470 ILE D 86 CG1 CG2 CD1
REMARK 470 GLU D 87 CG CD OE1 OE2
REMARK 470 LYS D 88 CG CD CE NZ
REMARK 470 THR D 92 OG1 CG2
REMARK 470 ILE D 96 CG1 CG2 CD1
REMARK 470 ILE D 99 CG1 CG2 CD1
REMARK 470 ILE D 101 CG1 CG2 CD1
REMARK 470 VAL D 109 CG1 CG2
REMARK 470 VAL D 110 CG1 CG2
REMARK 470 THR D 115 OG1 CG2
REMARK 470 LYS D 117 CG CD CE NZ
REMARK 470 ILE D 119 CG1 CG2 CD1
REMARK 470 ILE D 123 CG1 CG2 CD1
REMARK 470 LYS D 136 CG CD CE NZ
REMARK 470 LYS D 140 CG CD CE NZ
REMARK 470 LYS D 144 CG CD CE NZ
REMARK 470 VAL D 170 CG1 CG2
REMARK 470 LYS D 171 CG CD CE NZ
REMARK 470 ARG D 176 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 179 CG CD CE NZ
REMARK 470 PHE D 184 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE D 192 CG1 CG2 CD1
REMARK 470 LEU D 212 CG CD1 CD2
REMARK 470 ILE D 216 CG1 CG2 CD1
REMARK 470 GLU D 227 CG CD OE1 OE2
REMARK 470 VAL D 228 CG1 CG2
REMARK 470 ARG D 230 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 233 CG CD CE NZ
REMARK 470 GLU D 238 CG CD OE1 OE2
REMARK 470 LYS D 240 CG CD CE NZ
REMARK 470 ASP D 245 CG OD1 OD2
REMARK 470 PHE D 246 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL D 248 CG1 CG2
REMARK 470 ILE D 260 CG1 CG2 CD1
REMARK 470 VAL D 263 CG1 CG2
REMARK 470 PHE D 277 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU D 294 CG CD1 CD2
REMARK 470 LYS D 298 CG CD CE NZ
REMARK 470 ARG D 302 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 304 CE NZ
REMARK 470 ILE D 311 CG1 CG2 CD1
REMARK 470 THR D 319 OG1 CG2
REMARK 470 THR D 320 OG1 CG2
REMARK 470 ARG D 338 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 342 CG CD CE NZ
REMARK 470 VAL D 343 CG1 CG2
REMARK 470 ILE D 344 CG1 CG2 CD1
REMARK 470 THR D 350 OG1 CG2
REMARK 470 SER D 352 OG
REMARK 470 LEU D 353 CG CD1 CD2
REMARK 470 GLU D 355 CG CD OE1 OE2
REMARK 470 SER D 360 OG
REMARK 470 ARG D 382 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 390 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 412 CG CD1 CD2
REMARK 470 LYS D 418 CG CD CE NZ
REMARK 470 ARG D 430 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 431 CG1 CG2
REMARK 470 MSE D 435 CG SE CE
REMARK 470 VAL D 436 CG1 CG2
REMARK 470 ASP D 439 CG OD1 OD2
REMARK 470 GLN D 443 CG CD OE1 NE2
REMARK 470 SER D 446 OG
REMARK 470 LEU D 449 CG CD1 CD2
REMARK 470 ASP D 450 CG OD1 OD2
REMARK 470 VAL D 453 CG1 CG2
REMARK 470 ASP D 454 CG OD1 OD2
REMARK 470 ARG D 455 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 485 CG CD CE NZ
REMARK 470 ARG D 492 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 494 CG CD OE1 OE2
REMARK 470 HIS D 496 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 499 CG CD OE1 OE2
REMARK 470 LYS D 503 CG CD CE NZ
REMARK 470 LEU D 506 CG CD1 CD2
REMARK 470 LYS D 507 CG CD CE NZ
REMARK 470 ARG D 510 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 514 CG CD CE NZ
REMARK 470 THR D 516 OG1 CG2
REMARK 470 ILE D 518 CG1 CG2 CD1
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 MSE A 23 -134.95 40.38
REMARK 500 MSE A 24 -36.56 143.84
REMARK 500 LYS A 55 119.44 -165.17
REMARK 500 SER A 64 122.41 -36.20
REMARK 500 GLU A 106 -47.29 66.49
REMARK 500 THR A 107 125.72 -32.55
REMARK 500 HIS A 120 157.33 178.50
REMARK 500 LEU A 152 -155.78 -110.88
REMARK 500 SER A 209 -33.52 -39.51
REMARK 500 TYR A 313 156.76 174.97
REMARK 500 ALA A 330 -88.00 -131.24
REMARK 500 ALA A 368 43.28 -77.87
REMARK 500 HIS A 496 53.34 -141.90
REMARK 500 LYS B 55 116.99 -161.63
REMARK 500 GLU B 106 -45.03 65.19
REMARK 500 THR B 107 133.12 -37.98
REMARK 500 ASN B 121 155.23 -43.52
REMARK 500 THR B 150 -31.45 -135.43
REMARK 500 LEU B 152 -156.45 -107.94
REMARK 500 LEU B 212 -3.73 80.63
REMARK 500 ALA B 330 -89.99 -124.06
REMARK 500 ALA B 368 45.78 -78.40
REMARK 500 HIS B 496 57.41 -141.92
REMARK 500 GLU B 499 -40.46 -29.73
REMARK 500 MSE C 23 -71.84 -63.78
REMARK 500 GLN C 47 32.58 75.44
REMARK 500 GLU C 87 1.66 -67.80
REMARK 500 ILE C 91 -167.80 -110.88
REMARK 500 GLU C 106 -36.86 58.72
REMARK 500 THR C 107 136.02 -39.20
REMARK 500 LEU C 152 -146.03 -107.97
REMARK 500 TYR C 313 147.43 179.75
REMARK 500 ASP C 316 58.72 37.01
REMARK 500 ALA C 330 -91.43 -116.74
REMARK 500 ALA C 368 40.83 -96.96
REMARK 500 ILE C 518 127.09 -24.84
REMARK 500 VAL D 42 49.95 -75.47
REMARK 500 VAL D 52 93.20 -161.98
REMARK 500 HIS D 60 102.83 -56.24
REMARK 500 ALA D 85 -20.01 -140.47
REMARK 500 ASN D 94 72.54 -114.50
REMARK 500 GLU D 106 -13.82 60.66
REMARK 500 THR D 115 -84.58 -143.03
REMARK 500 LEU D 152 -147.99 -120.53
REMARK 500 PRO D 156 -19.68 -47.52
REMARK 500 LYS D 171 103.76 -54.75
REMARK 500 LYS D 233 -19.63 -48.88
REMARK 500 PHE D 246 36.44 -96.73
REMARK 500 THR D 249 -173.16 -69.37
REMARK 500 ALA D 257 64.96 -117.11
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
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 GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGRC-012403 RELATED DB: TARGETTRACK
DBREF 4E1J A 24 520 UNP O86033 GLPK_RHIME 1 497
DBREF 4E1J B 24 520 UNP O86033 GLPK_RHIME 1 497
DBREF 4E1J C 24 520 UNP O86033 GLPK_RHIME 1 497
DBREF 4E1J D 24 520 UNP O86033 GLPK_RHIME 1 497
SEQADV 4E1J MSE A 1 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS A 2 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS A 3 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS A 4 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS A 5 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS A 6 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS A 7 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER A 8 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER A 9 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLY A 10 UNP O86033 EXPRESSION TAG
SEQADV 4E1J VAL A 11 UNP O86033 EXPRESSION TAG
SEQADV 4E1J ASP A 12 UNP O86033 EXPRESSION TAG
SEQADV 4E1J LEU A 13 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLY A 14 UNP O86033 EXPRESSION TAG
SEQADV 4E1J THR A 15 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLU A 16 UNP O86033 EXPRESSION TAG
SEQADV 4E1J ASN A 17 UNP O86033 EXPRESSION TAG
SEQADV 4E1J LEU A 18 UNP O86033 EXPRESSION TAG
SEQADV 4E1J TYR A 19 UNP O86033 EXPRESSION TAG
SEQADV 4E1J PHE A 20 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLN A 21 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER A 22 UNP O86033 EXPRESSION TAG
SEQADV 4E1J MSE A 23 UNP O86033 EXPRESSION TAG
SEQADV 4E1J MSE B 1 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS B 2 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS B 3 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS B 4 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS B 5 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS B 6 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS B 7 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER B 8 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER B 9 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLY B 10 UNP O86033 EXPRESSION TAG
SEQADV 4E1J VAL B 11 UNP O86033 EXPRESSION TAG
SEQADV 4E1J ASP B 12 UNP O86033 EXPRESSION TAG
SEQADV 4E1J LEU B 13 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLY B 14 UNP O86033 EXPRESSION TAG
SEQADV 4E1J THR B 15 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLU B 16 UNP O86033 EXPRESSION TAG
SEQADV 4E1J ASN B 17 UNP O86033 EXPRESSION TAG
SEQADV 4E1J LEU B 18 UNP O86033 EXPRESSION TAG
SEQADV 4E1J TYR B 19 UNP O86033 EXPRESSION TAG
SEQADV 4E1J PHE B 20 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLN B 21 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER B 22 UNP O86033 EXPRESSION TAG
SEQADV 4E1J MSE B 23 UNP O86033 EXPRESSION TAG
SEQADV 4E1J MSE C 1 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS C 2 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS C 3 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS C 4 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS C 5 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS C 6 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS C 7 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER C 8 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER C 9 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLY C 10 UNP O86033 EXPRESSION TAG
SEQADV 4E1J VAL C 11 UNP O86033 EXPRESSION TAG
SEQADV 4E1J ASP C 12 UNP O86033 EXPRESSION TAG
SEQADV 4E1J LEU C 13 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLY C 14 UNP O86033 EXPRESSION TAG
SEQADV 4E1J THR C 15 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLU C 16 UNP O86033 EXPRESSION TAG
SEQADV 4E1J ASN C 17 UNP O86033 EXPRESSION TAG
SEQADV 4E1J LEU C 18 UNP O86033 EXPRESSION TAG
SEQADV 4E1J TYR C 19 UNP O86033 EXPRESSION TAG
SEQADV 4E1J PHE C 20 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLN C 21 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER C 22 UNP O86033 EXPRESSION TAG
SEQADV 4E1J MSE C 23 UNP O86033 EXPRESSION TAG
SEQADV 4E1J MSE D 1 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS D 2 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS D 3 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS D 4 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS D 5 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS D 6 UNP O86033 EXPRESSION TAG
SEQADV 4E1J HIS D 7 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER D 8 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER D 9 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLY D 10 UNP O86033 EXPRESSION TAG
SEQADV 4E1J VAL D 11 UNP O86033 EXPRESSION TAG
SEQADV 4E1J ASP D 12 UNP O86033 EXPRESSION TAG
SEQADV 4E1J LEU D 13 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLY D 14 UNP O86033 EXPRESSION TAG
SEQADV 4E1J THR D 15 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLU D 16 UNP O86033 EXPRESSION TAG
SEQADV 4E1J ASN D 17 UNP O86033 EXPRESSION TAG
SEQADV 4E1J LEU D 18 UNP O86033 EXPRESSION TAG
SEQADV 4E1J TYR D 19 UNP O86033 EXPRESSION TAG
SEQADV 4E1J PHE D 20 UNP O86033 EXPRESSION TAG
SEQADV 4E1J GLN D 21 UNP O86033 EXPRESSION TAG
SEQADV 4E1J SER D 22 UNP O86033 EXPRESSION TAG
SEQADV 4E1J MSE D 23 UNP O86033 EXPRESSION TAG
SEQRES 1 A 520 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 520 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE GLY GLY
SEQRES 3 A 520 TYR ILE LEU ALA ILE ASP GLN GLY THR THR SER THR ARG
SEQRES 4 A 520 ALA ILE VAL PHE ASP GLY ASN GLN LYS ILE ALA GLY VAL
SEQRES 5 A 520 GLY GLN LYS GLU PHE LYS GLN HIS PHE PRO LYS SER GLY
SEQRES 6 A 520 TRP VAL GLU HIS ASP PRO GLU GLU ILE TRP GLN THR VAL
SEQRES 7 A 520 VAL SER THR VAL LYS GLU ALA ILE GLU LYS SER GLY ILE
SEQRES 8 A 520 THR ALA ASN ASP ILE ALA ALA ILE GLY ILE THR ASN GLN
SEQRES 9 A 520 ARG GLU THR VAL VAL VAL TRP ASP ARG GLU THR GLY LYS
SEQRES 10 A 520 PRO ILE HIS ASN ALA ILE VAL TRP GLN ASP ARG ARG THR
SEQRES 11 A 520 ALA ALA PHE CYS ASP LYS LEU LYS LYS LYS GLY LEU GLU
SEQRES 12 A 520 LYS THR PHE VAL LYS LYS THR GLY LEU LEU LEU ASP PRO
SEQRES 13 A 520 TYR PHE SER GLY THR LYS LEU ASN TRP LEU LEU SER ASN
SEQRES 14 A 520 VAL LYS GLY ALA GLN VAL ARG ALA ALA LYS GLY GLU LEU
SEQRES 15 A 520 CYS PHE GLY THR ILE ASP THR PHE LEU ILE TRP ARG LEU
SEQRES 16 A 520 THR GLY GLY GLU CYS PHE CYS THR ASP ALA THR ASN ALA
SEQRES 17 A 520 SER ARG THR LEU LEU TYR ASN ILE ALA GLU ASN ALA TRP
SEQRES 18 A 520 ASP ASP GLU LEU THR GLU VAL LEU ARG VAL PRO LYS GLU
SEQRES 19 A 520 MSE LEU PRO GLU VAL LYS ASP CYS ALA ALA ASP PHE GLY
SEQRES 20 A 520 VAL THR ASP PRO SER LEU PHE GLY ALA ALA ILE PRO ILE
SEQRES 21 A 520 LEU GLY VAL ALA GLY ASP GLN GLN ALA ALA THR ILE GLY
SEQRES 22 A 520 GLN ALA CYS PHE LYS PRO GLY MSE LEU LYS SER THR TYR
SEQRES 23 A 520 GLY THR GLY CYS PHE ALA LEU LEU ASN THR GLY LYS ASP
SEQRES 24 A 520 MSE VAL ARG SER LYS ASN ARG LEU LEU THR THR ILE ALA
SEQRES 25 A 520 TYR ARG LEU ASP GLY GLU THR THR TYR ALA LEU GLU GLY
SEQRES 26 A 520 SER ILE PHE VAL ALA GLY ALA ALA VAL GLN TRP LEU ARG
SEQRES 27 A 520 ASP GLY LEU LYS VAL ILE LYS ALA ALA PRO ASP THR GLY
SEQRES 28 A 520 SER LEU ALA GLU SER ALA ASP PRO SER GLN GLU VAL TYR
SEQRES 29 A 520 LEU VAL PRO ALA PHE THR GLY LEU GLY ALA PRO HIS TRP
SEQRES 30 A 520 ASP PRO ASP ALA ARG GLY ALA ILE PHE GLY MSE THR ARG
SEQRES 31 A 520 ASN THR GLY PRO ALA GLU PHE ALA ARG ALA ALA LEU GLU
SEQRES 32 A 520 ALA VAL CYS TYR GLN THR ARG ASP LEU LEU GLU ALA MSE
SEQRES 33 A 520 HIS LYS ASP TRP ARG ARG ASN GLY ASN ASP THR VAL LEU
SEQRES 34 A 520 ARG VAL ASP GLY GLY MSE VAL ALA SER ASP TRP THR MSE
SEQRES 35 A 520 GLN ARG LEU SER ASP LEU LEU ASP ALA PRO VAL ASP ARG
SEQRES 36 A 520 PRO VAL ILE LEU GLU THR THR ALA LEU GLY VAL ALA TRP
SEQRES 37 A 520 LEU ALA GLY SER ARG ALA GLY VAL TRP PRO ASN GLN GLU
SEQRES 38 A 520 ALA PHE ALA LYS SER TRP ALA ARG ASP ARG ARG PHE GLU
SEQRES 39 A 520 PRO HIS MSE ASP GLU ALA THR ARG LYS VAL LYS LEU LYS
SEQRES 40 A 520 GLY TRP ARG SER ALA VAL LYS ARG THR LEU ILE ALA ALA
SEQRES 1 B 520 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 520 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE GLY GLY
SEQRES 3 B 520 TYR ILE LEU ALA ILE ASP GLN GLY THR THR SER THR ARG
SEQRES 4 B 520 ALA ILE VAL PHE ASP GLY ASN GLN LYS ILE ALA GLY VAL
SEQRES 5 B 520 GLY GLN LYS GLU PHE LYS GLN HIS PHE PRO LYS SER GLY
SEQRES 6 B 520 TRP VAL GLU HIS ASP PRO GLU GLU ILE TRP GLN THR VAL
SEQRES 7 B 520 VAL SER THR VAL LYS GLU ALA ILE GLU LYS SER GLY ILE
SEQRES 8 B 520 THR ALA ASN ASP ILE ALA ALA ILE GLY ILE THR ASN GLN
SEQRES 9 B 520 ARG GLU THR VAL VAL VAL TRP ASP ARG GLU THR GLY LYS
SEQRES 10 B 520 PRO ILE HIS ASN ALA ILE VAL TRP GLN ASP ARG ARG THR
SEQRES 11 B 520 ALA ALA PHE CYS ASP LYS LEU LYS LYS LYS GLY LEU GLU
SEQRES 12 B 520 LYS THR PHE VAL LYS LYS THR GLY LEU LEU LEU ASP PRO
SEQRES 13 B 520 TYR PHE SER GLY THR LYS LEU ASN TRP LEU LEU SER ASN
SEQRES 14 B 520 VAL LYS GLY ALA GLN VAL ARG ALA ALA LYS GLY GLU LEU
SEQRES 15 B 520 CYS PHE GLY THR ILE ASP THR PHE LEU ILE TRP ARG LEU
SEQRES 16 B 520 THR GLY GLY GLU CYS PHE CYS THR ASP ALA THR ASN ALA
SEQRES 17 B 520 SER ARG THR LEU LEU TYR ASN ILE ALA GLU ASN ALA TRP
SEQRES 18 B 520 ASP ASP GLU LEU THR GLU VAL LEU ARG VAL PRO LYS GLU
SEQRES 19 B 520 MSE LEU PRO GLU VAL LYS ASP CYS ALA ALA ASP PHE GLY
SEQRES 20 B 520 VAL THR ASP PRO SER LEU PHE GLY ALA ALA ILE PRO ILE
SEQRES 21 B 520 LEU GLY VAL ALA GLY ASP GLN GLN ALA ALA THR ILE GLY
SEQRES 22 B 520 GLN ALA CYS PHE LYS PRO GLY MSE LEU LYS SER THR TYR
SEQRES 23 B 520 GLY THR GLY CYS PHE ALA LEU LEU ASN THR GLY LYS ASP
SEQRES 24 B 520 MSE VAL ARG SER LYS ASN ARG LEU LEU THR THR ILE ALA
SEQRES 25 B 520 TYR ARG LEU ASP GLY GLU THR THR TYR ALA LEU GLU GLY
SEQRES 26 B 520 SER ILE PHE VAL ALA GLY ALA ALA VAL GLN TRP LEU ARG
SEQRES 27 B 520 ASP GLY LEU LYS VAL ILE LYS ALA ALA PRO ASP THR GLY
SEQRES 28 B 520 SER LEU ALA GLU SER ALA ASP PRO SER GLN GLU VAL TYR
SEQRES 29 B 520 LEU VAL PRO ALA PHE THR GLY LEU GLY ALA PRO HIS TRP
SEQRES 30 B 520 ASP PRO ASP ALA ARG GLY ALA ILE PHE GLY MSE THR ARG
SEQRES 31 B 520 ASN THR GLY PRO ALA GLU PHE ALA ARG ALA ALA LEU GLU
SEQRES 32 B 520 ALA VAL CYS TYR GLN THR ARG ASP LEU LEU GLU ALA MSE
SEQRES 33 B 520 HIS LYS ASP TRP ARG ARG ASN GLY ASN ASP THR VAL LEU
SEQRES 34 B 520 ARG VAL ASP GLY GLY MSE VAL ALA SER ASP TRP THR MSE
SEQRES 35 B 520 GLN ARG LEU SER ASP LEU LEU ASP ALA PRO VAL ASP ARG
SEQRES 36 B 520 PRO VAL ILE LEU GLU THR THR ALA LEU GLY VAL ALA TRP
SEQRES 37 B 520 LEU ALA GLY SER ARG ALA GLY VAL TRP PRO ASN GLN GLU
SEQRES 38 B 520 ALA PHE ALA LYS SER TRP ALA ARG ASP ARG ARG PHE GLU
SEQRES 39 B 520 PRO HIS MSE ASP GLU ALA THR ARG LYS VAL LYS LEU LYS
SEQRES 40 B 520 GLY TRP ARG SER ALA VAL LYS ARG THR LEU ILE ALA ALA
SEQRES 1 C 520 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 520 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE GLY GLY
SEQRES 3 C 520 TYR ILE LEU ALA ILE ASP GLN GLY THR THR SER THR ARG
SEQRES 4 C 520 ALA ILE VAL PHE ASP GLY ASN GLN LYS ILE ALA GLY VAL
SEQRES 5 C 520 GLY GLN LYS GLU PHE LYS GLN HIS PHE PRO LYS SER GLY
SEQRES 6 C 520 TRP VAL GLU HIS ASP PRO GLU GLU ILE TRP GLN THR VAL
SEQRES 7 C 520 VAL SER THR VAL LYS GLU ALA ILE GLU LYS SER GLY ILE
SEQRES 8 C 520 THR ALA ASN ASP ILE ALA ALA ILE GLY ILE THR ASN GLN
SEQRES 9 C 520 ARG GLU THR VAL VAL VAL TRP ASP ARG GLU THR GLY LYS
SEQRES 10 C 520 PRO ILE HIS ASN ALA ILE VAL TRP GLN ASP ARG ARG THR
SEQRES 11 C 520 ALA ALA PHE CYS ASP LYS LEU LYS LYS LYS GLY LEU GLU
SEQRES 12 C 520 LYS THR PHE VAL LYS LYS THR GLY LEU LEU LEU ASP PRO
SEQRES 13 C 520 TYR PHE SER GLY THR LYS LEU ASN TRP LEU LEU SER ASN
SEQRES 14 C 520 VAL LYS GLY ALA GLN VAL ARG ALA ALA LYS GLY GLU LEU
SEQRES 15 C 520 CYS PHE GLY THR ILE ASP THR PHE LEU ILE TRP ARG LEU
SEQRES 16 C 520 THR GLY GLY GLU CYS PHE CYS THR ASP ALA THR ASN ALA
SEQRES 17 C 520 SER ARG THR LEU LEU TYR ASN ILE ALA GLU ASN ALA TRP
SEQRES 18 C 520 ASP ASP GLU LEU THR GLU VAL LEU ARG VAL PRO LYS GLU
SEQRES 19 C 520 MSE LEU PRO GLU VAL LYS ASP CYS ALA ALA ASP PHE GLY
SEQRES 20 C 520 VAL THR ASP PRO SER LEU PHE GLY ALA ALA ILE PRO ILE
SEQRES 21 C 520 LEU GLY VAL ALA GLY ASP GLN GLN ALA ALA THR ILE GLY
SEQRES 22 C 520 GLN ALA CYS PHE LYS PRO GLY MSE LEU LYS SER THR TYR
SEQRES 23 C 520 GLY THR GLY CYS PHE ALA LEU LEU ASN THR GLY LYS ASP
SEQRES 24 C 520 MSE VAL ARG SER LYS ASN ARG LEU LEU THR THR ILE ALA
SEQRES 25 C 520 TYR ARG LEU ASP GLY GLU THR THR TYR ALA LEU GLU GLY
SEQRES 26 C 520 SER ILE PHE VAL ALA GLY ALA ALA VAL GLN TRP LEU ARG
SEQRES 27 C 520 ASP GLY LEU LYS VAL ILE LYS ALA ALA PRO ASP THR GLY
SEQRES 28 C 520 SER LEU ALA GLU SER ALA ASP PRO SER GLN GLU VAL TYR
SEQRES 29 C 520 LEU VAL PRO ALA PHE THR GLY LEU GLY ALA PRO HIS TRP
SEQRES 30 C 520 ASP PRO ASP ALA ARG GLY ALA ILE PHE GLY MSE THR ARG
SEQRES 31 C 520 ASN THR GLY PRO ALA GLU PHE ALA ARG ALA ALA LEU GLU
SEQRES 32 C 520 ALA VAL CYS TYR GLN THR ARG ASP LEU LEU GLU ALA MSE
SEQRES 33 C 520 HIS LYS ASP TRP ARG ARG ASN GLY ASN ASP THR VAL LEU
SEQRES 34 C 520 ARG VAL ASP GLY GLY MSE VAL ALA SER ASP TRP THR MSE
SEQRES 35 C 520 GLN ARG LEU SER ASP LEU LEU ASP ALA PRO VAL ASP ARG
SEQRES 36 C 520 PRO VAL ILE LEU GLU THR THR ALA LEU GLY VAL ALA TRP
SEQRES 37 C 520 LEU ALA GLY SER ARG ALA GLY VAL TRP PRO ASN GLN GLU
SEQRES 38 C 520 ALA PHE ALA LYS SER TRP ALA ARG ASP ARG ARG PHE GLU
SEQRES 39 C 520 PRO HIS MSE ASP GLU ALA THR ARG LYS VAL LYS LEU LYS
SEQRES 40 C 520 GLY TRP ARG SER ALA VAL LYS ARG THR LEU ILE ALA ALA
SEQRES 1 D 520 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 520 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE GLY GLY
SEQRES 3 D 520 TYR ILE LEU ALA ILE ASP GLN GLY THR THR SER THR ARG
SEQRES 4 D 520 ALA ILE VAL PHE ASP GLY ASN GLN LYS ILE ALA GLY VAL
SEQRES 5 D 520 GLY GLN LYS GLU PHE LYS GLN HIS PHE PRO LYS SER GLY
SEQRES 6 D 520 TRP VAL GLU HIS ASP PRO GLU GLU ILE TRP GLN THR VAL
SEQRES 7 D 520 VAL SER THR VAL LYS GLU ALA ILE GLU LYS SER GLY ILE
SEQRES 8 D 520 THR ALA ASN ASP ILE ALA ALA ILE GLY ILE THR ASN GLN
SEQRES 9 D 520 ARG GLU THR VAL VAL VAL TRP ASP ARG GLU THR GLY LYS
SEQRES 10 D 520 PRO ILE HIS ASN ALA ILE VAL TRP GLN ASP ARG ARG THR
SEQRES 11 D 520 ALA ALA PHE CYS ASP LYS LEU LYS LYS LYS GLY LEU GLU
SEQRES 12 D 520 LYS THR PHE VAL LYS LYS THR GLY LEU LEU LEU ASP PRO
SEQRES 13 D 520 TYR PHE SER GLY THR LYS LEU ASN TRP LEU LEU SER ASN
SEQRES 14 D 520 VAL LYS GLY ALA GLN VAL ARG ALA ALA LYS GLY GLU LEU
SEQRES 15 D 520 CYS PHE GLY THR ILE ASP THR PHE LEU ILE TRP ARG LEU
SEQRES 16 D 520 THR GLY GLY GLU CYS PHE CYS THR ASP ALA THR ASN ALA
SEQRES 17 D 520 SER ARG THR LEU LEU TYR ASN ILE ALA GLU ASN ALA TRP
SEQRES 18 D 520 ASP ASP GLU LEU THR GLU VAL LEU ARG VAL PRO LYS GLU
SEQRES 19 D 520 MSE LEU PRO GLU VAL LYS ASP CYS ALA ALA ASP PHE GLY
SEQRES 20 D 520 VAL THR ASP PRO SER LEU PHE GLY ALA ALA ILE PRO ILE
SEQRES 21 D 520 LEU GLY VAL ALA GLY ASP GLN GLN ALA ALA THR ILE GLY
SEQRES 22 D 520 GLN ALA CYS PHE LYS PRO GLY MSE LEU LYS SER THR TYR
SEQRES 23 D 520 GLY THR GLY CYS PHE ALA LEU LEU ASN THR GLY LYS ASP
SEQRES 24 D 520 MSE VAL ARG SER LYS ASN ARG LEU LEU THR THR ILE ALA
SEQRES 25 D 520 TYR ARG LEU ASP GLY GLU THR THR TYR ALA LEU GLU GLY
SEQRES 26 D 520 SER ILE PHE VAL ALA GLY ALA ALA VAL GLN TRP LEU ARG
SEQRES 27 D 520 ASP GLY LEU LYS VAL ILE LYS ALA ALA PRO ASP THR GLY
SEQRES 28 D 520 SER LEU ALA GLU SER ALA ASP PRO SER GLN GLU VAL TYR
SEQRES 29 D 520 LEU VAL PRO ALA PHE THR GLY LEU GLY ALA PRO HIS TRP
SEQRES 30 D 520 ASP PRO ASP ALA ARG GLY ALA ILE PHE GLY MSE THR ARG
SEQRES 31 D 520 ASN THR GLY PRO ALA GLU PHE ALA ARG ALA ALA LEU GLU
SEQRES 32 D 520 ALA VAL CYS TYR GLN THR ARG ASP LEU LEU GLU ALA MSE
SEQRES 33 D 520 HIS LYS ASP TRP ARG ARG ASN GLY ASN ASP THR VAL LEU
SEQRES 34 D 520 ARG VAL ASP GLY GLY MSE VAL ALA SER ASP TRP THR MSE
SEQRES 35 D 520 GLN ARG LEU SER ASP LEU LEU ASP ALA PRO VAL ASP ARG
SEQRES 36 D 520 PRO VAL ILE LEU GLU THR THR ALA LEU GLY VAL ALA TRP
SEQRES 37 D 520 LEU ALA GLY SER ARG ALA GLY VAL TRP PRO ASN GLN GLU
SEQRES 38 D 520 ALA PHE ALA LYS SER TRP ALA ARG ASP ARG ARG PHE GLU
SEQRES 39 D 520 PRO HIS MSE ASP GLU ALA THR ARG LYS VAL LYS LEU LYS
SEQRES 40 D 520 GLY TRP ARG SER ALA VAL LYS ARG THR LEU ILE ALA ALA
MODRES 4E1J MSE A 23 MET SELENOMETHIONINE
MODRES 4E1J MSE A 24 MET SELENOMETHIONINE
MODRES 4E1J MSE A 235 MET SELENOMETHIONINE
MODRES 4E1J MSE A 281 MET SELENOMETHIONINE
MODRES 4E1J MSE A 300 MET SELENOMETHIONINE
MODRES 4E1J MSE A 388 MET SELENOMETHIONINE
MODRES 4E1J MSE A 416 MET SELENOMETHIONINE
MODRES 4E1J MSE A 435 MET SELENOMETHIONINE
MODRES 4E1J MSE A 442 MET SELENOMETHIONINE
MODRES 4E1J MSE A 497 MET SELENOMETHIONINE
MODRES 4E1J MSE B 235 MET SELENOMETHIONINE
MODRES 4E1J MSE B 281 MET SELENOMETHIONINE
MODRES 4E1J MSE B 300 MET SELENOMETHIONINE
MODRES 4E1J MSE B 388 MET SELENOMETHIONINE
MODRES 4E1J MSE B 416 MET SELENOMETHIONINE
MODRES 4E1J MSE B 435 MET SELENOMETHIONINE
MODRES 4E1J MSE B 442 MET SELENOMETHIONINE
MODRES 4E1J MSE B 497 MET SELENOMETHIONINE
MODRES 4E1J MSE C 23 MET SELENOMETHIONINE
MODRES 4E1J MSE C 24 MET SELENOMETHIONINE
MODRES 4E1J MSE C 235 MET SELENOMETHIONINE
MODRES 4E1J MSE C 281 MET SELENOMETHIONINE
MODRES 4E1J MSE C 300 MET SELENOMETHIONINE
MODRES 4E1J MSE C 388 MET SELENOMETHIONINE
MODRES 4E1J MSE C 416 MET SELENOMETHIONINE
MODRES 4E1J MSE C 435 MET SELENOMETHIONINE
MODRES 4E1J MSE C 442 MET SELENOMETHIONINE
MODRES 4E1J MSE C 497 MET SELENOMETHIONINE
MODRES 4E1J MSE D 235 MET SELENOMETHIONINE
MODRES 4E1J MSE D 300 MET SELENOMETHIONINE
MODRES 4E1J MSE D 388 MET SELENOMETHIONINE
MODRES 4E1J MSE D 416 MET SELENOMETHIONINE
MODRES 4E1J MSE D 435 MET SELENOMETHIONINE
MODRES 4E1J MSE D 442 MET SELENOMETHIONINE
MODRES 4E1J MSE D 497 MET SELENOMETHIONINE
HET MSE A 23 5
HET MSE A 24 5
HET MSE A 235 8
HET MSE A 281 8
HET MSE A 300 8
HET MSE A 388 8
HET MSE A 416 8
HET MSE A 435 8
HET MSE A 442 8
HET MSE A 497 8
HET MSE B 235 8
HET MSE B 281 8
HET MSE B 300 8
HET MSE B 388 8
HET MSE B 416 8
HET MSE B 435 8
HET MSE B 442 8
HET MSE B 497 8
HET MSE C 23 8
HET MSE C 24 5
HET MSE C 235 8
HET MSE C 281 8
HET MSE C 300 8
HET MSE C 388 8
HET MSE C 416 8
HET MSE C 435 8
HET MSE C 442 8
HET MSE C 497 8
HET MSE D 235 8
HET MSE D 300 8
HET MSE D 388 8
HET MSE D 416 8
HET MSE D 435 5
HET MSE D 442 8
HET MSE D 497 8
HET GOL A 601 6
HET NA A 602 1
HET GOL B 601 6
HET CL C 601 1
HET GOL C 602 6
HET NA C 603 1
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 35(C5 H11 N O2 SE)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 6 NA 2(NA 1+)
FORMUL 8 CL CL 1-
FORMUL 11 HOH *97(H2 O)
HELIX 1 1 ASP A 70 LYS A 88 1 19
HELIX 2 2 THR A 92 ASN A 94 5 3
HELIX 3 3 THR A 130 LYS A 140 1 11
HELIX 4 4 LEU A 142 GLY A 151 1 10
HELIX 5 5 PHE A 158 VAL A 170 1 13
HELIX 6 6 GLY A 172 LYS A 179 1 8
HELIX 7 7 ILE A 187 THR A 196 1 10
HELIX 8 8 ALA A 205 SER A 209 1 5
HELIX 9 9 ASP A 222 ARG A 230 1 9
HELIX 10 10 PRO A 232 LEU A 236 5 5
HELIX 11 11 ASP A 250 GLY A 255 1 6
HELIX 12 12 GLY A 265 GLN A 274 1 10
HELIX 13 13 ALA A 330 GLY A 340 1 11
HELIX 14 14 GLY A 351 SER A 356 1 6
HELIX 15 15 GLY A 393 TRP A 420 1 28
HELIX 16 16 GLY A 433 ALA A 437 5 5
HELIX 17 17 SER A 438 ASP A 450 1 13
HELIX 18 18 GLU A 460 GLY A 475 1 16
HELIX 19 19 ASN A 479 SER A 486 1 8
HELIX 20 20 ASP A 498 ILE A 518 1 21
HELIX 21 21 ASP B 70 LYS B 88 1 19
HELIX 22 22 THR B 92 ASN B 94 5 3
HELIX 23 23 THR B 130 LYS B 140 1 11
HELIX 24 24 LEU B 142 GLY B 151 1 10
HELIX 25 25 PHE B 158 VAL B 170 1 13
HELIX 26 26 GLY B 172 LYS B 179 1 8
HELIX 27 27 THR B 186 THR B 196 1 11
HELIX 28 28 ALA B 205 SER B 209 1 5
HELIX 29 29 ASP B 222 LEU B 229 1 8
HELIX 30 30 PRO B 232 LEU B 236 5 5
HELIX 31 31 ASP B 266 GLN B 274 1 9
HELIX 32 32 ALA B 330 GLY B 340 1 11
HELIX 33 33 GLY B 351 ALA B 357 1 7
HELIX 34 34 GLY B 393 TRP B 420 1 28
HELIX 35 35 GLY B 433 ALA B 437 5 5
HELIX 36 36 SER B 438 ASP B 450 1 13
HELIX 37 37 GLU B 460 GLY B 475 1 16
HELIX 38 38 ASN B 479 SER B 486 1 8
HELIX 39 39 ASP B 498 ILE B 518 1 21
HELIX 40 40 ASP C 12 MSE C 24 1 13
HELIX 41 41 ASP C 70 GLU C 87 1 18
HELIX 42 42 THR C 130 LYS C 140 1 11
HELIX 43 43 LEU C 142 GLY C 151 1 10
HELIX 44 44 PHE C 158 VAL C 170 1 13
HELIX 45 45 GLY C 172 LYS C 179 1 8
HELIX 46 46 THR C 186 THR C 196 1 11
HELIX 47 47 ALA C 205 SER C 209 1 5
HELIX 48 48 ASP C 222 LEU C 229 1 8
HELIX 49 49 PRO C 232 LEU C 236 5 5
HELIX 50 50 ASP C 266 GLN C 274 1 9
HELIX 51 51 ALA C 330 GLY C 340 1 11
HELIX 52 52 GLY C 351 SER C 356 1 6
HELIX 53 53 GLY C 393 TRP C 420 1 28
HELIX 54 54 GLY C 433 ALA C 437 5 5
HELIX 55 55 SER C 438 ASP C 450 1 13
HELIX 56 56 GLU C 460 ALA C 474 1 15
HELIX 57 57 ASN C 479 SER C 486 1 8
HELIX 58 58 ASP C 498 ILE C 518 1 21
HELIX 59 59 ASP D 70 VAL D 82 1 13
HELIX 60 60 THR D 130 LYS D 140 1 11
HELIX 61 61 LEU D 142 GLY D 151 1 10
HELIX 62 62 PHE D 158 VAL D 170 1 13
HELIX 63 63 GLY D 172 ALA D 178 1 7
HELIX 64 64 THR D 186 THR D 196 1 11
HELIX 65 65 ASP D 204 ARG D 210 1 7
HELIX 66 66 ASP D 222 LEU D 229 1 8
HELIX 67 67 PRO D 232 LEU D 236 5 5
HELIX 68 68 GLN D 267 ILE D 272 1 6
HELIX 69 69 GLY D 331 GLY D 340 1 10
HELIX 70 70 SER D 352 ALA D 357 5 6
HELIX 71 71 GLY D 393 HIS D 417 1 25
HELIX 72 72 GLY D 433 ALA D 437 5 5
HELIX 73 73 SER D 438 ASP D 450 1 13
HELIX 74 74 ASP D 498 ILE D 518 1 21
SHEET 1 A 5 ILE A 49 GLU A 56 0
SHEET 2 A 5 SER A 37 PHE A 43 -1 N VAL A 42 O ALA A 50
SHEET 3 A 5 TYR A 27 GLN A 33 -1 N ASP A 32 O ARG A 39
SHEET 4 A 5 ILE A 96 ASN A 103 1 O GLY A 100 N LEU A 29
SHEET 5 A 5 ILE A 260 VAL A 263 1 O GLY A 262 N ILE A 101
SHEET 1 B 2 GLU A 68 HIS A 69 0
SHEET 2 B 2 ALA A 122 ILE A 123 -1 O ALA A 122 N HIS A 69
SHEET 1 C 2 VAL A 108 ASP A 112 0
SHEET 2 C 2 LEU A 182 THR A 186 -1 O GLY A 185 N VAL A 109
SHEET 1 D 2 CYS A 202 ASP A 204 0
SHEET 2 D 2 GLU A 238 LYS A 240 1 O LYS A 240 N THR A 203
SHEET 1 E 2 TYR A 214 ASN A 215 0
SHEET 2 E 2 ALA A 220 TRP A 221 -1 O ALA A 220 N ASN A 215
SHEET 1 F 7 LEU A 308 LEU A 315 0
SHEET 2 F 7 GLU A 318 ILE A 327 -1 O ALA A 322 N THR A 310
SHEET 3 F 7 CYS A 290 ASN A 295 -1 N CYS A 290 O ILE A 327
SHEET 4 F 7 LEU A 282 TYR A 286 -1 N THR A 285 O PHE A 291
SHEET 5 F 7 LEU A 429 ASP A 432 1 O ASP A 432 N TYR A 286
SHEET 6 F 7 VAL A 453 PRO A 456 1 O ASP A 454 N LEU A 429
SHEET 7 F 7 ARG A 489 PHE A 493 -1 O ARG A 491 N ARG A 455
SHEET 1 G 2 TYR A 364 VAL A 366 0
SHEET 2 G 2 ALA A 384 PHE A 386 -1 O PHE A 386 N TYR A 364
SHEET 1 H 5 ILE B 49 GLU B 56 0
SHEET 2 H 5 SER B 37 PHE B 43 -1 N VAL B 42 O ALA B 50
SHEET 3 H 5 TYR B 27 GLN B 33 -1 N ASP B 32 O ARG B 39
SHEET 4 H 5 ILE B 96 ASN B 103 1 O GLY B 100 N LEU B 29
SHEET 5 H 5 ILE B 260 GLY B 265 1 O GLY B 262 N ILE B 101
SHEET 1 I 2 GLU B 68 HIS B 69 0
SHEET 2 I 2 ALA B 122 ILE B 123 -1 O ALA B 122 N HIS B 69
SHEET 1 J 2 VAL B 109 ASP B 112 0
SHEET 2 J 2 LEU B 182 GLY B 185 -1 O GLY B 185 N VAL B 109
SHEET 1 K 2 CYS B 202 ASP B 204 0
SHEET 2 K 2 GLU B 238 LYS B 240 1 O LYS B 240 N THR B 203
SHEET 1 L 2 TYR B 214 ASN B 215 0
SHEET 2 L 2 ALA B 220 TRP B 221 -1 O ALA B 220 N ASN B 215
SHEET 1 M 7 LEU B 308 LEU B 315 0
SHEET 2 M 7 GLU B 318 ILE B 327 -1 O THR B 320 N TYR B 313
SHEET 3 M 7 CYS B 290 GLY B 297 -1 N CYS B 290 O ILE B 327
SHEET 4 M 7 LEU B 282 TYR B 286 -1 N LYS B 283 O LEU B 293
SHEET 5 M 7 LEU B 429 ASP B 432 1 O ASP B 432 N TYR B 286
SHEET 6 M 7 VAL B 453 PRO B 456 1 O ASP B 454 N LEU B 429
SHEET 7 M 7 ARG B 489 PHE B 493 -1 O PHE B 493 N VAL B 453
SHEET 1 N 2 TYR B 364 VAL B 366 0
SHEET 2 N 2 ALA B 384 PHE B 386 -1 O ALA B 384 N VAL B 366
SHEET 1 O 5 ILE C 49 GLU C 56 0
SHEET 2 O 5 SER C 37 PHE C 43 -1 N ALA C 40 O GLY C 53
SHEET 3 O 5 ILE C 28 GLN C 33 -1 N ASP C 32 O ARG C 39
SHEET 4 O 5 ALA C 98 ASN C 103 1 O GLY C 100 N LEU C 29
SHEET 5 O 5 ILE C 260 GLY C 265 1 O GLY C 262 N ILE C 101
SHEET 1 P 2 GLU C 68 HIS C 69 0
SHEET 2 P 2 ALA C 122 ILE C 123 -1 O ALA C 122 N HIS C 69
SHEET 1 Q 2 VAL C 109 ASP C 112 0
SHEET 2 Q 2 LEU C 182 GLY C 185 -1 O GLY C 185 N VAL C 109
SHEET 1 R 2 CYS C 202 ASP C 204 0
SHEET 2 R 2 GLU C 238 LYS C 240 1 O LYS C 240 N THR C 203
SHEET 1 S 2 TYR C 214 ASN C 215 0
SHEET 2 S 2 ALA C 220 TRP C 221 -1 O ALA C 220 N ASN C 215
SHEET 1 T 7 LEU C 308 LEU C 315 0
SHEET 2 T 7 GLU C 318 ILE C 327 -1 O GLU C 324 N LEU C 308
SHEET 3 T 7 CYS C 290 ASN C 295 -1 N CYS C 290 O ILE C 327
SHEET 4 T 7 LEU C 282 TYR C 286 -1 N LYS C 283 O LEU C 293
SHEET 5 T 7 LEU C 429 ASP C 432 1 O ASP C 432 N TYR C 286
SHEET 6 T 7 VAL C 453 PRO C 456 1 O ASP C 454 N LEU C 429
SHEET 7 T 7 ARG C 489 PHE C 493 -1 O ASP C 490 N ARG C 455
SHEET 1 U 2 TYR C 364 VAL C 366 0
SHEET 2 U 2 ALA C 384 PHE C 386 -1 O ALA C 384 N VAL C 366
SHEET 1 V 5 GLY D 53 GLU D 56 0
SHEET 2 V 5 SER D 37 ALA D 40 -1 N ALA D 40 O GLY D 53
SHEET 3 V 5 ILE D 28 GLN D 33 -1 N ASP D 32 O ARG D 39
SHEET 4 V 5 ALA D 98 ASN D 103 1 O ALA D 98 N LEU D 29
SHEET 5 V 5 ILE D 260 GLY D 265 1 O GLY D 262 N ILE D 101
SHEET 1 W 2 GLU D 68 HIS D 69 0
SHEET 2 W 2 ALA D 122 ILE D 123 -1 O ALA D 122 N HIS D 69
SHEET 1 X 2 CYS D 202 THR D 203 0
SHEET 2 X 2 GLU D 238 VAL D 239 1 O GLU D 238 N THR D 203
SHEET 1 Y 2 TYR D 214 ASN D 215 0
SHEET 2 Y 2 ALA D 220 TRP D 221 -1 O ALA D 220 N ASN D 215
SHEET 1 Z 5 LEU D 308 LEU D 315 0
SHEET 2 Z 5 GLU D 318 ILE D 327 -1 O GLU D 324 N LEU D 308
SHEET 3 Z 5 CYS D 290 GLY D 297 -1 N ALA D 292 O GLY D 325
SHEET 4 Z 5 LYS D 283 TYR D 286 -1 N THR D 285 O PHE D 291
SHEET 5 Z 5 VAL D 431 ASP D 432 1 O ASP D 432 N SER D 284
SHEET 1 AA 2 TYR D 364 VAL D 366 0
SHEET 2 AA 2 ALA D 384 PHE D 386 -1 O PHE D 386 N TYR D 364
SHEET 1 AB 2 ASP D 454 ARG D 455 0
SHEET 2 AB 2 ARG D 491 ARG D 492 -1 O ARG D 491 N ARG D 455
SSBOND 1 CYS B 200 CYS B 202 1555 1555 2.94
SSBOND 2 CYS C 200 CYS C 202 1555 1555 2.96
LINK C SER A 22 N MSE A 23 1555 1555 1.33
LINK C MSE A 23 N MSE A 24 1555 1555 1.34
LINK C MSE A 24 N GLY A 25 1555 1555 1.34
LINK C GLU A 234 N MSE A 235 1555 1555 1.35
LINK C MSE A 235 N LEU A 236 1555 1555 1.32
LINK C GLY A 280 N MSE A 281 1555 1555 1.34
LINK C MSE A 281 N LEU A 282 1555 1555 1.34
LINK C ASP A 299 N MSE A 300 1555 1555 1.31
LINK C MSE A 300 N VAL A 301 1555 1555 1.33
LINK C GLY A 387 N MSE A 388 1555 1555 1.33
LINK C MSE A 388 N THR A 389 1555 1555 1.32
LINK C ALA A 415 N MSE A 416 1555 1555 1.33
LINK C MSE A 416 N HIS A 417 1555 1555 1.34
LINK C GLY A 434 N MSE A 435 1555 1555 1.34
LINK C MSE A 435 N VAL A 436 1555 1555 1.33
LINK C THR A 441 N MSE A 442 1555 1555 1.32
LINK C MSE A 442 N GLN A 443 1555 1555 1.33
LINK C HIS A 496 N MSE A 497 1555 1555 1.33
LINK C MSE A 497 N ASP A 498 1555 1555 1.32
LINK C GLU B 234 N MSE B 235 1555 1555 1.33
LINK C MSE B 235 N LEU B 236 1555 1555 1.32
LINK C GLY B 280 N MSE B 281 1555 1555 1.33
LINK C MSE B 281 N LEU B 282 1555 1555 1.33
LINK C ASP B 299 N MSE B 300 1555 1555 1.32
LINK C MSE B 300 N VAL B 301 1555 1555 1.32
LINK C GLY B 387 N MSE B 388 1555 1555 1.32
LINK C MSE B 388 N THR B 389 1555 1555 1.32
LINK C ALA B 415 N MSE B 416 1555 1555 1.33
LINK C MSE B 416 N HIS B 417 1555 1555 1.34
LINK C GLY B 434 N MSE B 435 1555 1555 1.32
LINK C MSE B 435 N VAL B 436 1555 1555 1.33
LINK C THR B 441 N MSE B 442 1555 1555 1.33
LINK C MSE B 442 N GLN B 443 1555 1555 1.34
LINK C HIS B 496 N MSE B 497 1555 1555 1.32
LINK C MSE B 497 N ASP B 498 1555 1555 1.33
LINK C SER C 22 N MSE C 23 1555 1555 1.34
LINK C MSE C 23 N MSE C 24 1555 1555 1.34
LINK C MSE C 24 N GLY C 25 1555 1555 1.33
LINK C GLU C 234 N MSE C 235 1555 1555 1.35
LINK C MSE C 235 N LEU C 236 1555 1555 1.33
LINK C GLY C 280 N MSE C 281 1555 1555 1.33
LINK C MSE C 281 N LEU C 282 1555 1555 1.33
LINK C ASP C 299 N MSE C 300 1555 1555 1.33
LINK C MSE C 300 N VAL C 301 1555 1555 1.33
LINK C GLY C 387 N MSE C 388 1555 1555 1.34
LINK C MSE C 388 N THR C 389 1555 1555 1.33
LINK C ALA C 415 N MSE C 416 1555 1555 1.33
LINK C MSE C 416 N HIS C 417 1555 1555 1.34
LINK C GLY C 434 N MSE C 435 1555 1555 1.33
LINK C MSE C 435 N VAL C 436 1555 1555 1.32
LINK C THR C 441 N MSE C 442 1555 1555 1.33
LINK C MSE C 442 N GLN C 443 1555 1555 1.33
LINK C HIS C 496 N MSE C 497 1555 1555 1.33
LINK C MSE C 497 N ASP C 498 1555 1555 1.33
LINK C GLU D 234 N MSE D 235 1555 1555 1.33
LINK C MSE D 235 N LEU D 236 1555 1555 1.34
LINK C MSE D 300 N VAL D 301 1555 1555 1.34
LINK C GLY D 387 N MSE D 388 1555 1555 1.34
LINK C MSE D 388 N THR D 389 1555 1555 1.33
LINK C ALA D 415 N MSE D 416 1555 1555 1.33
LINK C MSE D 416 N HIS D 417 1555 1555 1.34
LINK C GLY D 434 N MSE D 435 1555 1555 1.34
LINK C MSE D 435 N VAL D 436 1555 1555 1.34
LINK C THR D 441 N MSE D 442 1555 1555 1.33
LINK C MSE D 442 N GLN D 443 1555 1555 1.33
LINK C HIS D 496 N MSE D 497 1555 1555 1.34
LINK C MSE D 497 N ASP D 498 1555 1555 1.33
LINK NA NA C 603 O HOH C 704 1555 1555 2.81
LINK O MSE A 23 NA NA A 602 1555 1555 3.05
CISPEP 1 LEU A 13 GLY A 14 0 -14.58
CISPEP 2 ALA A 374 PRO A 375 0 1.95
CISPEP 3 ALA B 374 PRO B 375 0 -2.59
CISPEP 4 ALA C 374 PRO C 375 0 -2.88
CISPEP 5 GLY D 26 TYR D 27 0 -1.20
CISPEP 6 ALA D 374 PRO D 375 0 -0.39
SITE 1 AC1 7 ARG A 105 GLU A 106 TRP A 125 TYR A 157
SITE 2 AC1 7 ASP A 266 GLN A 267 PHE A 291
SITE 1 AC2 1 MSE A 23
SITE 1 AC3 7 ARG B 105 GLU B 106 TRP B 125 TYR B 157
SITE 2 AC3 7 ASP B 266 GLN B 267 PHE B 291
SITE 1 AC4 1 ALA C 488
SITE 1 AC5 7 ARG C 105 GLU C 106 TRP C 125 TYR C 157
SITE 2 AC5 7 ASP C 266 GLN C 267 PHE C 291
SITE 1 AC6 2 SER C 486 HOH C 704
CRYST1 93.220 101.975 107.548 90.00 90.03 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 0.010727 0.000000 0.000006 0.00000
SCALE2 0.000000 0.009806 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009298 0.00000
(ATOM LINES ARE NOT SHOWN.)
END