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HEADER HYDROLASE 16-NOV-16 5TXE
TITLE ATXE2 ISOPEPTIDASE - S527A VARIANT WITH ASTEXIN3-DC4 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATXE2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ASTEXIN3-DC4;
COMPND 8 CHAIN: C, D;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASTICCACAULIS EXCENTRICUS (STRAIN ATCC 15261 /
SOURCE 3 DSM 4724 / VKM B-1370 / CB 48);
SOURCE 4 ORGANISM_TAXID: 573065;
SOURCE 5 STRAIN: ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48;
SOURCE 6 GENE: ASTEX_2444;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ASTICCACAULIS EXCENTRICUS (STRAIN ATCC 15261 /
SOURCE 11 DSM 4724 / VKM B-1370 / CB 48);
SOURCE 12 ORGANISM_TAXID: 573065;
SOURCE 13 STRAIN: ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48;
SOURCE 14 GENE: ASTEX_2447;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ISOPEPTIDASE, LASSO PEPTIDE, NATURAL PRODUCT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.CHEKAN,S.K.NAIR
REVDAT 1 21-DEC-16 5TXE 0
JRNL AUTH J.R.CHEKAN,J.D.KOOS,C.ZONG,M.O.MAKSIMOV,J.A.LINK,S.K.NAIR
JRNL TITL STRUCTURE OF THE LASSO PEPTIDE ISOPEPTIDASE IDENTIFIES A
JRNL TITL 2 TOPOLOGY FOR PROCESSING THREADED SUBSTRATES
JRNL REF J.AM.CHEM.SOC. 2016
JRNL REFN ESSN 1520-5126
JRNL DOI 10.1021/JACS.6B10389
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 81764
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) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4255
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5980
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 331
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10555
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.03000
REMARK 3 B22 (A**2) : -0.90000
REMARK 3 B33 (A**2) : -0.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.196
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.166
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.647
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10868 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10188 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14838 ; 1.748 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 23343 ; 1.191 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1349 ; 6.834 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 522 ;33.905 ;22.605
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1703 ;15.201 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 124 ;19.764 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1621 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12458 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2608 ; 0.005 ; 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): 5372 ; 2.986 ; 3.156
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5371 ; 2.985 ; 3.155
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6714 ; 4.287 ; 4.719
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6715 ; 4.287 ; 4.720
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5495 ; 4.139 ; 3.674
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5496 ; 4.139 ; 3.674
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8120 ; 6.345 ; 5.308
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 12942 ; 8.274 ;26.341
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 12520 ; 8.219 ;26.029
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 : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 35 1016 B 35 1016 40295 0.10 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5TXE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000224986.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97853
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86021
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 29.817
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.73700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 0.3 M AMMONIUM CITRATE
REMARK 280 DIBASIC, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 75.62650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 101.42700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 75.62650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 101.42700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 75.62650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 101.42700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 75.62650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 101.42700
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 2000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 2070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, 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 1
REMARK 465 ARG A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 ILE A 6
REMARK 465 ARG A 7
REMARK 465 CYS A 8
REMARK 465 PRO A 9
REMARK 465 GLY A 10
REMARK 465 ALA A 11
REMARK 465 ILE A 12
REMARK 465 ARG A 13
REMARK 465 VAL A 14
REMARK 465 GLY A 15
REMARK 465 THR A 16
REMARK 465 LEU A 17
REMARK 465 VAL A 18
REMARK 465 THR A 19
REMARK 465 ALA A 20
REMARK 465 PHE A 21
REMARK 465 GLY A 22
REMARK 465 CYS A 23
REMARK 465 LEU A 24
REMARK 465 PRO A 25
REMARK 465 HIS A 26
REMARK 465 VAL A 27
REMARK 465 ALA A 28
REMARK 465 PHE A 29
REMARK 465 ALA A 30
REMARK 465 ALA A 31
REMARK 465 ALA A 32
REMARK 465 ARG A 33
REMARK 465 GLU A 34
REMARK 465 LYS A 687
REMARK 465 SER A 688
REMARK 465 PRO A 689
REMARK 465 SER A 690
REMARK 465 PRO A 691
REMARK 465 THR A 692
REMARK 465 PRO A 693
REMARK 465 ALA A 694
REMARK 465 PRO A 695
REMARK 465 GLY A 696
REMARK 465 SER A 697
REMARK 465 ARG A 698
REMARK 465 SER A 699
REMARK 465 HIS A 700
REMARK 465 HIS A 701
REMARK 465 HIS A 702
REMARK 465 HIS A 703
REMARK 465 HIS A 704
REMARK 465 HIS A 705
REMARK 465 GLN C 1018
REMARK 465 HIS C 1019
REMARK 465 ALA C 1020
REMARK 465 PRO C 1021
REMARK 465 LEU C 1022
REMARK 465 ALA C 1023
REMARK 465 ASP C 1024
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 LYS B 5
REMARK 465 ILE B 6
REMARK 465 ARG B 7
REMARK 465 CYS B 8
REMARK 465 PRO B 9
REMARK 465 GLY B 10
REMARK 465 ALA B 11
REMARK 465 ILE B 12
REMARK 465 ARG B 13
REMARK 465 VAL B 14
REMARK 465 GLY B 15
REMARK 465 THR B 16
REMARK 465 LEU B 17
REMARK 465 VAL B 18
REMARK 465 THR B 19
REMARK 465 ALA B 20
REMARK 465 PHE B 21
REMARK 465 GLY B 22
REMARK 465 CYS B 23
REMARK 465 LEU B 24
REMARK 465 PRO B 25
REMARK 465 HIS B 26
REMARK 465 VAL B 27
REMARK 465 ALA B 28
REMARK 465 PHE B 29
REMARK 465 ALA B 30
REMARK 465 ALA B 31
REMARK 465 ALA B 32
REMARK 465 ARG B 33
REMARK 465 GLU B 34
REMARK 465 LYS B 687
REMARK 465 SER B 688
REMARK 465 PRO B 689
REMARK 465 SER B 690
REMARK 465 PRO B 691
REMARK 465 THR B 692
REMARK 465 PRO B 693
REMARK 465 ALA B 694
REMARK 465 PRO B 695
REMARK 465 GLY B 696
REMARK 465 SER B 697
REMARK 465 ARG B 698
REMARK 465 SER B 699
REMARK 465 HIS B 700
REMARK 465 HIS B 701
REMARK 465 HIS B 702
REMARK 465 HIS B 703
REMARK 465 HIS B 704
REMARK 465 HIS B 705
REMARK 465 HIS D 1019
REMARK 465 ALA D 1020
REMARK 465 PRO D 1021
REMARK 465 LEU D 1022
REMARK 465 ALA D 1023
REMARK 465 ASP D 1024
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 1289 O HOH B 1316 1.89
REMARK 500 C THR B 348 O HOH B 802 1.91
REMARK 500 O HOH A 1039 O HOH A 1113 1.99
REMARK 500 OE2 GLU B 202 O HOH B 801 2.00
REMARK 500 O HOH B 1099 O HOH B 1256 2.01
REMARK 500 O HOH B 1159 O HOH B 1277 2.08
REMARK 500 OG SER A 157 O HOH A 801 2.09
REMARK 500 O HOH A 1088 O HOH A 1110 2.09
REMARK 500 OG1 THR B 348 O HOH B 802 2.13
REMARK 500 O HOH B 901 O HOH B 1171 2.17
REMARK 500 O HOH B 812 O HOH B 1232 2.17
REMARK 500 O HOH A 855 O HOH B 805 2.18
REMARK 500 O HOH B 1042 O HOH B 1214 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU B 403 OE2 GLU B 403 6565 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG B 241 CD ARG B 241 NE -0.110
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 133 CG - CD - NE ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG A 222 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 677 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 677 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 679 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 679 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 TRP C1016 CB - CA - C ANGL. DEV. = 13.4 DEGREES
REMARK 500 TRP C1016 CA - C - N ANGL. DEV. = 13.4 DEGREES
REMARK 500 ARG B 152 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 241 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 241 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG B 253 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 260 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 360 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 360 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 373 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 430 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 441 CG - CD - NE ANGL. DEV. = -13.7 DEGREES
REMARK 500 ARG B 441 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 445 CD - NE - CZ ANGL. DEV. = 12.0 DEGREES
REMARK 500 ARG B 445 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG B 445 NE - CZ - NH2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG B 625 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 679 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 679 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG B 685 NE - CZ - NH1 ANGL. DEV. = 3.1 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 ASP A 210 -155.19 -156.74
REMARK 500 ALA A 338 -168.92 -128.51
REMARK 500 ALA A 358 -111.99 49.08
REMARK 500 ARG A 445 -88.31 -110.03
REMARK 500 ALA A 527 -120.04 61.95
REMARK 500 SER A 559 -64.02 -103.44
REMARK 500 MET C1005 -102.33 -125.52
REMARK 500 SER C1010 -165.81 66.19
REMARK 500 ASP B 210 -155.21 -154.91
REMARK 500 ALA B 338 -167.06 -129.01
REMARK 500 ALA B 358 -113.91 55.14
REMARK 500 ARG B 445 -87.60 -114.89
REMARK 500 ALA B 527 -122.17 60.36
REMARK 500 SER B 559 -65.76 -101.67
REMARK 500 ARG B 685 2.53 -69.39
REMARK 500 MET D1005 -102.25 -126.56
REMARK 500 SER D1010 -164.04 66.77
REMARK 500 TRP D1016 -142.64 -112.53
REMARK 500 ASP D1017 56.36 -160.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TRP C 1016 ASP C 1017 64.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TXC RELATED DB: PDB
DBREF 5TXE A 1 695 UNP E8RUP5 E8RUP5_ASTEC 1 695
DBREF 5TXE C 1001 1024 UNP E8RUP8 E8RUP8_ASTEC 26 49
DBREF 5TXE B 1 695 UNP E8RUP5 E8RUP5_ASTEC 1 695
DBREF 5TXE D 1001 1024 UNP E8RUP8 E8RUP8_ASTEC 26 49
SEQADV 5TXE ALA A 527 UNP E8RUP5 SER 527 ENGINEERED MUTATION
SEQADV 5TXE GLY A 696 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE SER A 697 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE ARG A 698 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE SER A 699 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS A 700 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS A 701 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS A 702 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS A 703 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS A 704 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS A 705 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE ALA B 527 UNP E8RUP5 SER 527 ENGINEERED MUTATION
SEQADV 5TXE GLY B 696 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE SER B 697 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE ARG B 698 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE SER B 699 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS B 700 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS B 701 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS B 702 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS B 703 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS B 704 UNP E8RUP5 EXPRESSION TAG
SEQADV 5TXE HIS B 705 UNP E8RUP5 EXPRESSION TAG
SEQRES 1 A 705 MET ARG SER SER LYS ILE ARG CYS PRO GLY ALA ILE ARG
SEQRES 2 A 705 VAL GLY THR LEU VAL THR ALA PHE GLY CYS LEU PRO HIS
SEQRES 3 A 705 VAL ALA PHE ALA ALA ALA ARG GLU ALA PRO PRO VAL THR
SEQRES 4 A 705 PRO GLU VAL LEU VAL ARG LEU ALA ASP ILE GLY THR MET
SEQRES 5 A 705 SER ALA SER GLU THR THR PRO LEU LEU SER LEU SER PRO
SEQRES 6 A 705 ASP GLY ARG TYR VAL ALA PHE GLN VAL ARG GLN ALA ASP
SEQRES 7 A 705 PRO VAL THR ASN LEU ASN VAL PHE ARG MET VAL VAL LYS
SEQRES 8 A 705 ALA THR ASP GLY ALA THR ASP ALA ILE ASP VAL ASP VAL
SEQRES 9 A 705 GLY GLY GLU TYR LEU PHE TRP THR ILE PRO SER TRP GLY
SEQRES 10 A 705 TYR ALA ARG ASN ALA PRO SER GLY ALA ASN LEU THR ILE
SEQRES 11 A 705 GLN PRO ARG TRP SER PRO SER GLY THR HIS LEU ALA TYR
SEQRES 12 A 705 LEU ARG GLN ASP GLN GLY ARG VAL ARG VAL TRP ARG ALA
SEQRES 13 A 705 SER VAL LYS GLY GLU GLY ALA SER PRO VAL ILE GLU ASP
SEQRES 14 A 705 ALA TYR ASP ILE GLU ASP VAL GLN TRP LEU ASP ASP ASN
SEQRES 15 A 705 THR LEU ILE TYR SER GLY ARG PRO GLY PHE VAL GLU ALA
SEQRES 16 A 705 GLU ALA GLU ILE GLU ARG GLU GLY ARG ARG GLY TRP VAL
SEQRES 17 A 705 TYR ASP GLU ARG PHE HIS PRO LEU THR GLY ALA ARG PRO
SEQRES 18 A 705 ARG VAL LEU GLU PRO ILE SER ILE VAL TYR GLN VAL LEU
SEQRES 19 A 705 ASP LEU LYS THR GLY THR ARG ARG ALA ALA THR PRO THR
SEQRES 20 A 705 GLU VAL ALA ARG LEU ARG GLU LYS PRO ASP PRO LEU ARG
SEQRES 21 A 705 ALA MET VAL GLY ARG THR THR PHE SER VAL SER ARG THR
SEQRES 22 A 705 ASP PRO GLN ASN ILE ASN ALA PRO THR THR LEU VAL ALA
SEQRES 23 A 705 ARG ARG GLY GLU GLY GLU PRO VAL ARG CYS ASP GLU GLU
SEQRES 24 A 705 ALA CYS GLN ASN ILE THR ARG MET TRP GLY ASP GLU THR
SEQRES 25 A 705 ALA ASN VAL LEU TYR PHE LEU ARG ARG GLU GLY TRP ALA
SEQRES 26 A 705 SER ASN GLU MET ALA LEU TYR ARG MET PRO ALA ASP ALA
SEQRES 27 A 705 LEU LYS PRO VAL ARG ILE TRP HIS ALA THR GLY LEU LEU
SEQRES 28 A 705 GLN GLY CYS GLU ARG GLN ALA LYS ARG LEU ILE CYS ALA
SEQRES 29 A 705 GLN GLU SER ALA LEU GLN PRO ARG ARG LEU VAL THR LEU
SEQRES 30 A 705 ASN LEU THR SER GLY GLN MET SER PRO LEU TYR ASP PRO
SEQRES 31 A 705 ASN PRO ASP LEU SER ARG TYR ARG LEU PRO LYS VAL GLU
SEQRES 32 A 705 ARG LEU THR LEU ARG ASN ARG ASN GLY ILE GLU VAL PHE
SEQRES 33 A 705 SER ASP LEU VAL LEU PRO PRO ASP TYR GLN LEU GLY THR
SEQRES 34 A 705 ARG LEU PRO LEU VAL ILE VAL GLN TYR SER SER ARG GLY
SEQRES 35 A 705 PHE LEU ARG GLY GLY THR GLY ASP GLU ASN PRO ILE LEU
SEQRES 36 A 705 PRO LEU ALA THR ALA GLY PHE ALA VAL LEU SER PHE HIS
SEQRES 37 A 705 SER PRO ARG SER GLU ALA SER TYR GLN ARG PHE THR SER
SEQRES 38 A 705 PRO ILE ALA GLN SER LYS ALA GLU TYR SER ASN TRP ARG
SEQRES 39 A 705 ASN ARG TRP ASN ILE LEU HIS THR LEU GLU ASP LEU ILE
SEQRES 40 A 705 ASP ASP LEU ASP ARG ARG GLY VAL ILE ASP PRO ALA ARG
SEQRES 41 A 705 VAL GLY LEU THR GLY LEU ALA ASP GLY ALA THR THR VAL
SEQRES 42 A 705 HIS PHE GLY LEU ILE ASN SER HIS ARG PHE ALA ALA ALA
SEQRES 43 A 705 VAL THR SER SER CYS CYS THR ASP SER PHE THR ALA SER
SEQRES 44 A 705 VAL MET ASN GLY PRO ARG ILE SER GLY ALA LEU LYS ALA
SEQRES 45 A 705 TYR GLY ILE GLU THR ASP GLN ALA ASP ASP GLY PRO PHE
SEQRES 46 A 705 TRP ALA ALA THR SER PHE VAL VAL ASN ALA SER ARG LEU
SEQRES 47 A 705 ASP THR PRO LEU LEU ILE GLN SER ALA ASP GLU GLU TYR
SEQRES 48 A 705 LEU GLY ALA LEU PRO GLY PHE THR ALA LEU GLN GLN ALA
SEQRES 49 A 705 ARG LYS PRO VAL GLU LEU ILE ILE TYR PRO ASN GLU HIS
SEQRES 50 A 705 HIS VAL LYS TRP GLN PRO ALA HIS ARG LEU ALA VAL TYR
SEQRES 51 A 705 ASN ARG THR ILE ASP TRP PHE ARG PHE TRP LEU MET ASP
SEQRES 52 A 705 GLN SER ASP PRO ALA PRO ASP LYS ALA ALA GLN TYR ASP
SEQRES 53 A 705 ARG TRP ARG ALA LEU ARG ALA LEU ARG GLN LYS SER PRO
SEQRES 54 A 705 SER PRO THR PRO ALA PRO GLY SER ARG SER HIS HIS HIS
SEQRES 55 A 705 HIS HIS HIS
SEQRES 1 C 24 GLY PRO THR PRO MET VAL GLY LEU ASP SER VAL SER GLY
SEQRES 2 C 24 GLN TYR TRP ASP GLN HIS ALA PRO LEU ALA ASP
SEQRES 1 B 705 MET ARG SER SER LYS ILE ARG CYS PRO GLY ALA ILE ARG
SEQRES 2 B 705 VAL GLY THR LEU VAL THR ALA PHE GLY CYS LEU PRO HIS
SEQRES 3 B 705 VAL ALA PHE ALA ALA ALA ARG GLU ALA PRO PRO VAL THR
SEQRES 4 B 705 PRO GLU VAL LEU VAL ARG LEU ALA ASP ILE GLY THR MET
SEQRES 5 B 705 SER ALA SER GLU THR THR PRO LEU LEU SER LEU SER PRO
SEQRES 6 B 705 ASP GLY ARG TYR VAL ALA PHE GLN VAL ARG GLN ALA ASP
SEQRES 7 B 705 PRO VAL THR ASN LEU ASN VAL PHE ARG MET VAL VAL LYS
SEQRES 8 B 705 ALA THR ASP GLY ALA THR ASP ALA ILE ASP VAL ASP VAL
SEQRES 9 B 705 GLY GLY GLU TYR LEU PHE TRP THR ILE PRO SER TRP GLY
SEQRES 10 B 705 TYR ALA ARG ASN ALA PRO SER GLY ALA ASN LEU THR ILE
SEQRES 11 B 705 GLN PRO ARG TRP SER PRO SER GLY THR HIS LEU ALA TYR
SEQRES 12 B 705 LEU ARG GLN ASP GLN GLY ARG VAL ARG VAL TRP ARG ALA
SEQRES 13 B 705 SER VAL LYS GLY GLU GLY ALA SER PRO VAL ILE GLU ASP
SEQRES 14 B 705 ALA TYR ASP ILE GLU ASP VAL GLN TRP LEU ASP ASP ASN
SEQRES 15 B 705 THR LEU ILE TYR SER GLY ARG PRO GLY PHE VAL GLU ALA
SEQRES 16 B 705 GLU ALA GLU ILE GLU ARG GLU GLY ARG ARG GLY TRP VAL
SEQRES 17 B 705 TYR ASP GLU ARG PHE HIS PRO LEU THR GLY ALA ARG PRO
SEQRES 18 B 705 ARG VAL LEU GLU PRO ILE SER ILE VAL TYR GLN VAL LEU
SEQRES 19 B 705 ASP LEU LYS THR GLY THR ARG ARG ALA ALA THR PRO THR
SEQRES 20 B 705 GLU VAL ALA ARG LEU ARG GLU LYS PRO ASP PRO LEU ARG
SEQRES 21 B 705 ALA MET VAL GLY ARG THR THR PHE SER VAL SER ARG THR
SEQRES 22 B 705 ASP PRO GLN ASN ILE ASN ALA PRO THR THR LEU VAL ALA
SEQRES 23 B 705 ARG ARG GLY GLU GLY GLU PRO VAL ARG CYS ASP GLU GLU
SEQRES 24 B 705 ALA CYS GLN ASN ILE THR ARG MET TRP GLY ASP GLU THR
SEQRES 25 B 705 ALA ASN VAL LEU TYR PHE LEU ARG ARG GLU GLY TRP ALA
SEQRES 26 B 705 SER ASN GLU MET ALA LEU TYR ARG MET PRO ALA ASP ALA
SEQRES 27 B 705 LEU LYS PRO VAL ARG ILE TRP HIS ALA THR GLY LEU LEU
SEQRES 28 B 705 GLN GLY CYS GLU ARG GLN ALA LYS ARG LEU ILE CYS ALA
SEQRES 29 B 705 GLN GLU SER ALA LEU GLN PRO ARG ARG LEU VAL THR LEU
SEQRES 30 B 705 ASN LEU THR SER GLY GLN MET SER PRO LEU TYR ASP PRO
SEQRES 31 B 705 ASN PRO ASP LEU SER ARG TYR ARG LEU PRO LYS VAL GLU
SEQRES 32 B 705 ARG LEU THR LEU ARG ASN ARG ASN GLY ILE GLU VAL PHE
SEQRES 33 B 705 SER ASP LEU VAL LEU PRO PRO ASP TYR GLN LEU GLY THR
SEQRES 34 B 705 ARG LEU PRO LEU VAL ILE VAL GLN TYR SER SER ARG GLY
SEQRES 35 B 705 PHE LEU ARG GLY GLY THR GLY ASP GLU ASN PRO ILE LEU
SEQRES 36 B 705 PRO LEU ALA THR ALA GLY PHE ALA VAL LEU SER PHE HIS
SEQRES 37 B 705 SER PRO ARG SER GLU ALA SER TYR GLN ARG PHE THR SER
SEQRES 38 B 705 PRO ILE ALA GLN SER LYS ALA GLU TYR SER ASN TRP ARG
SEQRES 39 B 705 ASN ARG TRP ASN ILE LEU HIS THR LEU GLU ASP LEU ILE
SEQRES 40 B 705 ASP ASP LEU ASP ARG ARG GLY VAL ILE ASP PRO ALA ARG
SEQRES 41 B 705 VAL GLY LEU THR GLY LEU ALA ASP GLY ALA THR THR VAL
SEQRES 42 B 705 HIS PHE GLY LEU ILE ASN SER HIS ARG PHE ALA ALA ALA
SEQRES 43 B 705 VAL THR SER SER CYS CYS THR ASP SER PHE THR ALA SER
SEQRES 44 B 705 VAL MET ASN GLY PRO ARG ILE SER GLY ALA LEU LYS ALA
SEQRES 45 B 705 TYR GLY ILE GLU THR ASP GLN ALA ASP ASP GLY PRO PHE
SEQRES 46 B 705 TRP ALA ALA THR SER PHE VAL VAL ASN ALA SER ARG LEU
SEQRES 47 B 705 ASP THR PRO LEU LEU ILE GLN SER ALA ASP GLU GLU TYR
SEQRES 48 B 705 LEU GLY ALA LEU PRO GLY PHE THR ALA LEU GLN GLN ALA
SEQRES 49 B 705 ARG LYS PRO VAL GLU LEU ILE ILE TYR PRO ASN GLU HIS
SEQRES 50 B 705 HIS VAL LYS TRP GLN PRO ALA HIS ARG LEU ALA VAL TYR
SEQRES 51 B 705 ASN ARG THR ILE ASP TRP PHE ARG PHE TRP LEU MET ASP
SEQRES 52 B 705 GLN SER ASP PRO ALA PRO ASP LYS ALA ALA GLN TYR ASP
SEQRES 53 B 705 ARG TRP ARG ALA LEU ARG ALA LEU ARG GLN LYS SER PRO
SEQRES 54 B 705 SER PRO THR PRO ALA PRO GLY SER ARG SER HIS HIS HIS
SEQRES 55 B 705 HIS HIS HIS
SEQRES 1 D 24 GLY PRO THR PRO MET VAL GLY LEU ASP SER VAL SER GLY
SEQRES 2 D 24 GLN TYR TRP ASP GLN HIS ALA PRO LEU ALA ASP
FORMUL 5 HOH *910(H2 O)
HELIX 1 AA1 THR A 39 ARG A 45 1 7
HELIX 2 AA2 ARG A 189 GLY A 203 1 15
HELIX 3 AA3 ARG A 204 GLY A 206 5 3
HELIX 4 AA4 THR A 245 GLU A 254 1 10
HELIX 5 AA5 GLU A 298 GLN A 302 5 5
HELIX 6 AA6 GLY A 323 ASN A 327 5 5
HELIX 7 AA7 ASP A 393 TYR A 397 5 5
HELIX 8 AA8 PRO A 453 ALA A 460 1 8
HELIX 9 AA9 SER A 472 GLN A 477 5 6
HELIX 10 AB1 SER A 481 SER A 491 1 11
HELIX 11 AB2 TRP A 493 ARG A 513 1 21
HELIX 12 AB3 ALA A 527 SER A 540 1 14
HELIX 13 AB4 ASP A 554 SER A 559 1 6
HELIX 14 AB5 ASN A 562 LYS A 571 1 10
HELIX 15 AB6 ALA A 572 GLY A 574 5 3
HELIX 16 AB7 PHE A 585 THR A 589 5 5
HELIX 17 AB8 SER A 590 ALA A 595 1 6
HELIX 18 AB9 SER A 596 LEU A 598 5 3
HELIX 19 AC1 ASP A 608 LEU A 612 1 5
HELIX 20 AC2 ALA A 614 ALA A 624 1 11
HELIX 21 AC3 GLN A 642 ASP A 663 1 22
HELIX 22 AC4 ALA A 668 ASP A 670 5 3
HELIX 23 AC5 LYS A 671 ARG A 685 1 15
HELIX 24 AC6 THR B 39 ARG B 45 1 7
HELIX 25 AC7 ARG B 189 GLY B 203 1 15
HELIX 26 AC8 ARG B 204 GLY B 206 5 3
HELIX 27 AC9 THR B 245 GLU B 254 1 10
HELIX 28 AD1 GLU B 298 GLN B 302 5 5
HELIX 29 AD2 GLY B 323 ASN B 327 5 5
HELIX 30 AD3 ASP B 393 TYR B 397 5 5
HELIX 31 AD4 PRO B 453 ALA B 460 1 8
HELIX 32 AD5 GLU B 473 GLN B 477 5 5
HELIX 33 AD6 SER B 481 SER B 491 1 11
HELIX 34 AD7 TRP B 493 ARG B 513 1 21
HELIX 35 AD8 ALA B 527 SER B 540 1 14
HELIX 36 AD9 ASP B 554 SER B 559 1 6
HELIX 37 AE1 ASN B 562 LYS B 571 1 10
HELIX 38 AE2 ALA B 572 GLY B 574 5 3
HELIX 39 AE3 PHE B 585 THR B 589 5 5
HELIX 40 AE4 SER B 590 ALA B 595 1 6
HELIX 41 AE5 SER B 596 LEU B 598 5 3
HELIX 42 AE6 ASP B 608 LEU B 612 1 5
HELIX 43 AE7 ALA B 614 ALA B 624 1 11
HELIX 44 AE8 GLN B 642 ASP B 663 1 22
HELIX 45 AE9 ALA B 668 ASP B 670 5 3
HELIX 46 AF1 LYS B 671 ARG B 685 1 15
SHEET 1 AA1 3 ASP A 48 ILE A 49 0
SHEET 2 AA1 3 TYR A 69 ASP A 78 -1 O ARG A 75 N ASP A 48
SHEET 3 AA1 3 LEU A 61 LEU A 63 -1 N SER A 62 O ALA A 71
SHEET 1 AA2 4 ASP A 48 ILE A 49 0
SHEET 2 AA2 4 TYR A 69 ASP A 78 -1 O ARG A 75 N ASP A 48
SHEET 3 AA2 4 LEU A 83 ALA A 92 -1 O VAL A 89 N PHE A 72
SHEET 4 AA2 4 ILE A 100 VAL A 104 -1 O VAL A 102 N MET A 88
SHEET 1 AA3 4 ARG A 133 TRP A 134 0
SHEET 2 AA3 4 HIS A 140 ASP A 147 -1 O ALA A 142 N ARG A 133
SHEET 3 AA3 4 ARG A 150 SER A 157 -1 O TRP A 154 N TYR A 143
SHEET 4 AA3 4 ALA A 163 ILE A 167 -1 O VAL A 166 N VAL A 153
SHEET 1 AA4 4 ILE A 173 ASP A 180 0
SHEET 2 AA4 4 THR A 183 GLY A 188 -1 O ILE A 185 N GLN A 177
SHEET 3 AA4 4 VAL A 230 ASP A 235 -1 O LEU A 234 N LEU A 184
SHEET 4 AA4 4 ARG A 241 ALA A 243 -1 O ARG A 242 N VAL A 233
SHEET 1 AA5 9 TRP A 207 VAL A 208 0
SHEET 2 AA5 9 VAL B 628 TYR B 633 -1 O ILE B 632 N TRP A 207
SHEET 3 AA5 9 LEU B 602 ALA B 607 1 N ILE B 604 O ILE B 631
SHEET 4 AA5 9 ALA B 545 THR B 548 1 N THR B 548 O LEU B 603
SHEET 5 AA5 9 ILE B 516 GLY B 525 1 N LEU B 523 O VAL B 547
SHEET 6 AA5 9 LEU B 431 VAL B 436 1 N LEU B 433 O GLY B 522
SHEET 7 AA5 9 ALA B 463 PHE B 467 1 O LEU B 465 N VAL B 436
SHEET 8 AA5 9 GLU B 414 LEU B 421 -1 N ASP B 418 O SER B 466
SHEET 9 AA5 9 LYS B 401 ARG B 408 -1 N LEU B 405 O SER B 417
SHEET 1 AA6 4 ALA A 261 VAL A 263 0
SHEET 2 AA6 4 THR A 266 SER A 271 -1 O PHE A 268 N ALA A 261
SHEET 3 AA6 4 THR A 283 ARG A 288 -1 O VAL A 285 N SER A 269
SHEET 4 AA6 4 VAL A 294 ARG A 295 -1 O VAL A 294 N ALA A 286
SHEET 1 AA7 4 ILE A 304 ASP A 310 0
SHEET 2 AA7 4 VAL A 315 GLU A 322 -1 O LEU A 319 N ARG A 306
SHEET 3 AA7 4 GLU A 328 PRO A 335 -1 O TYR A 332 N PHE A 318
SHEET 4 AA7 4 VAL A 342 ALA A 347 -1 O VAL A 342 N ARG A 333
SHEET 1 AA8 4 LEU A 350 GLN A 357 0
SHEET 2 AA8 4 ARG A 360 SER A 367 -1 O ILE A 362 N GLU A 355
SHEET 3 AA8 4 GLN A 370 ASN A 378 -1 O ARG A 373 N GLN A 365
SHEET 4 AA8 4 MET A 384 TYR A 388 -1 O TYR A 388 N LEU A 374
SHEET 1 AA9 9 LYS A 401 ARG A 408 0
SHEET 2 AA9 9 GLU A 414 LEU A 421 -1 O SER A 417 N LEU A 405
SHEET 3 AA9 9 ALA A 463 PHE A 467 -1 O SER A 466 N ASP A 418
SHEET 4 AA9 9 LEU A 431 VAL A 436 1 N VAL A 436 O PHE A 467
SHEET 5 AA9 9 ILE A 516 GLY A 525 1 O GLY A 522 N LEU A 433
SHEET 6 AA9 9 ALA A 545 THR A 548 1 O ALA A 545 N LEU A 523
SHEET 7 AA9 9 LEU A 602 ALA A 607 1 O GLN A 605 N THR A 548
SHEET 8 AA9 9 VAL A 628 TYR A 633 1 O ILE A 631 N ILE A 604
SHEET 9 AA9 9 TRP B 207 VAL B 208 -1 O TRP B 207 N ILE A 632
SHEET 1 AB1 2 LEU C1008 ASP C1009 0
SHEET 2 AB1 2 GLN C1014 TYR C1015 -1 O GLN C1014 N ASP C1009
SHEET 1 AB2 3 ASP B 48 ILE B 49 0
SHEET 2 AB2 3 TYR B 69 ASP B 78 -1 O ARG B 75 N ASP B 48
SHEET 3 AB2 3 LEU B 61 LEU B 63 -1 N SER B 62 O ALA B 71
SHEET 1 AB3 4 ASP B 48 ILE B 49 0
SHEET 2 AB3 4 TYR B 69 ASP B 78 -1 O ARG B 75 N ASP B 48
SHEET 3 AB3 4 LEU B 83 ALA B 92 -1 O VAL B 89 N PHE B 72
SHEET 4 AB3 4 ILE B 100 VAL B 104 -1 O VAL B 102 N MET B 88
SHEET 1 AB4 4 ARG B 133 TRP B 134 0
SHEET 2 AB4 4 HIS B 140 ASP B 147 -1 O ALA B 142 N ARG B 133
SHEET 3 AB4 4 ARG B 150 SER B 157 -1 O TRP B 154 N TYR B 143
SHEET 4 AB4 4 ALA B 163 ILE B 167 -1 O VAL B 166 N VAL B 153
SHEET 1 AB5 4 ILE B 173 ASP B 180 0
SHEET 2 AB5 4 THR B 183 GLY B 188 -1 O SER B 187 N GLU B 174
SHEET 3 AB5 4 VAL B 230 ASP B 235 -1 O LEU B 234 N LEU B 184
SHEET 4 AB5 4 ARG B 241 ALA B 243 -1 O ARG B 242 N VAL B 233
SHEET 1 AB6 4 ALA B 261 VAL B 263 0
SHEET 2 AB6 4 THR B 266 SER B 271 -1 O PHE B 268 N ALA B 261
SHEET 3 AB6 4 THR B 283 ARG B 288 -1 O VAL B 285 N SER B 269
SHEET 4 AB6 4 VAL B 294 ARG B 295 -1 O VAL B 294 N ALA B 286
SHEET 1 AB7 4 ILE B 304 ASP B 310 0
SHEET 2 AB7 4 VAL B 315 GLU B 322 -1 O TYR B 317 N TRP B 308
SHEET 3 AB7 4 GLU B 328 PRO B 335 -1 O TYR B 332 N PHE B 318
SHEET 4 AB7 4 VAL B 342 ALA B 347 -1 O ILE B 344 N LEU B 331
SHEET 1 AB8 4 LEU B 350 GLN B 357 0
SHEET 2 AB8 4 ARG B 360 SER B 367 -1 O ILE B 362 N GLU B 355
SHEET 3 AB8 4 GLN B 370 ASN B 378 -1 O LEU B 377 N LEU B 361
SHEET 4 AB8 4 MET B 384 TYR B 388 -1 O TYR B 388 N LEU B 374
SHEET 1 AB9 2 LEU D1008 ASP D1009 0
SHEET 2 AB9 2 GLN D1014 TYR D1015 -1 O GLN D1014 N ASP D1009
SSBOND 1 CYS A 296 CYS A 301 1555 1555 2.17
SSBOND 2 CYS A 354 CYS A 363 1555 1555 2.17
SSBOND 3 CYS A 551 CYS A 552 1555 1555 2.12
SSBOND 4 CYS B 296 CYS B 301 1555 1555 2.21
SSBOND 5 CYS B 354 CYS B 363 1555 1555 2.22
SSBOND 6 CYS B 551 CYS B 552 1555 1555 2.17
LINK N GLY C1001 CG ASP C1009 1555 1555 1.25
LINK N GLY D1001 CG ASP D1009 1555 1555 1.27
CISPEP 1 GLU A 225 PRO A 226 0 8.46
CISPEP 2 GLN A 437 TYR A 438 0 -5.77
CISPEP 3 CYS A 551 CYS A 552 0 8.44
CISPEP 4 GLU B 225 PRO B 226 0 -0.33
CISPEP 5 GLN B 437 TYR B 438 0 -4.68
CISPEP 6 CYS B 551 CYS B 552 0 6.86
CRYST1 151.253 202.854 110.399 90.00 90.00 90.00 C 2 2 2 16
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 0.006611 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004930 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009058 0.00000
TER 5162 GLN A 686
TER 5288 ASP C1017
TER 10460 GLN B 686
TER 10595 GLN D1018
MASTER 561 0 0 46 76 0 0 611465 4 16 114
END |