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HEADER HYDROLASE 05-JAN-16 5HDP
TITLE HYDROLASE STNA MUTANT - S185A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE;
COMPND 3 CHAIN: D, A, B, C, E, F, G;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES FLOCCULUS;
SOURCE 3 ORGANISM_TAXID: 67300;
SOURCE 4 GENE: STNA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD(DE3)PLYSS AG;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HYDROLASE, COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.QIAN
REVDAT 1 11-JAN-17 5HDP 0
JRNL AUTH T.QIAN
JRNL TITL CRYSTAL STRUCTURE OF STNA MUTANT IN COMPLEX AT 2.9 ANGSTROMS
JRNL TITL 2 RESOLUTION FROM STREPTOMYCES FLOCCULUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 52120
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) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2792
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3544
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16720
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 252
REMARK 3 SOLVENT ATOMS : 27
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.90000
REMARK 3 B22 (A**2) : 0.45000
REMARK 3 B33 (A**2) : -0.45000
REMARK 3 B12 (A**2) : -1.33000
REMARK 3 B13 (A**2) : 1.35000
REMARK 3 B23 (A**2) : -1.01000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.510
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.450
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.518
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.871
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.823
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17413 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 15861 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23814 ; 1.370 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 36411 ; 0.969 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2203 ; 6.471 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 770 ;32.988 ;23.818
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2506 ;13.994 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 112 ;16.198 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2602 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20153 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3988 ; 0.002 ; 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): 8833 ; 2.540 ; 5.075
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8832 ; 2.540 ; 5.075
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11029 ; 4.159 ; 7.609
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 11030 ; 4.159 ; 7.609
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8580 ; 2.648 ; 5.277
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 8581 ; 2.647 ; 5.277
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 12786 ; 4.370 ; 7.812
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 19627 ; 6.938 ;40.804
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 19627 ; 6.938 ;40.804
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 : 1.20
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 5HDP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216857.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-15
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9818
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57747
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.48700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.540
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5HDF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM CITRATE DIBASIC, 0.1 M
REMARK 280 SODIUM CITRATE PH 5.0, 20% 2-PROPANOL, 15% PEG 3350, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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 VAL D 1
REMARK 465 THR D 2
REMARK 465 ALA D 3
REMARK 465 LEU D 4
REMARK 465 SER D 5
REMARK 465 ARG D 6
REMARK 465 LEU D 7
REMARK 465 GLY D 8
REMARK 465 GLU D 9
REMARK 465 PRO D 10
REMARK 465 PRO D 11
REMARK 465 SER D 12
REMARK 465 GLY D 13
REMARK 465 HIS D 14
REMARK 465 ASP D 15
REMARK 465 GLY D 16
REMARK 465 ASN D 17
REMARK 465 SER D 18
REMARK 465 GLU D 19
REMARK 465 VAL D 20
REMARK 465 ARG D 21
REMARK 465 ARG D 22
REMARK 465 ILE D 23
REMARK 465 ALA D 24
REMARK 465 MET D 25
REMARK 465 LYS D 26
REMARK 465 ARG D 27
REMARK 465 ALA D 28
REMARK 465 THR D 29
REMARK 465 VAL D 30
REMARK 465 PRO D 31
REMARK 465 VAL D 32
REMARK 465 LEU D 33
REMARK 465 ARG D 34
REMARK 465 ARG D 35
REMARK 465 VAL D 36
REMARK 465 ALA D 37
REMARK 465 ALA D 38
REMARK 465 VAL D 39
REMARK 465 CYS D 40
REMARK 465 ALA D 41
REMARK 465 ALA D 42
REMARK 465 ALA D 43
REMARK 465 LEU D 44
REMARK 465 LEU D 45
REMARK 465 VAL D 46
REMARK 465 THR D 47
REMARK 465 VAL D 48
REMARK 465 GLY D 49
REMARK 465 THR D 50
REMARK 465 GLY D 51
REMARK 465 GLY D 52
REMARK 465 PRO D 53
REMARK 465 ALA D 54
REMARK 465 SER D 55
REMARK 465 ALA D 56
REMARK 465 THR D 57
REMARK 465 GLY D 58
REMARK 465 THR D 59
REMARK 465 ARG D 60
REMARK 465 GLU D 377
REMARK 465 HIS D 378
REMARK 465 HIS D 379
REMARK 465 HIS D 380
REMARK 465 HIS D 381
REMARK 465 HIS D 382
REMARK 465 HIS D 383
REMARK 465 VAL A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 ARG A 6
REMARK 465 LEU A 7
REMARK 465 GLY A 8
REMARK 465 GLU A 9
REMARK 465 PRO A 10
REMARK 465 PRO A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 HIS A 14
REMARK 465 ASP A 15
REMARK 465 GLY A 16
REMARK 465 ASN A 17
REMARK 465 SER A 18
REMARK 465 GLU A 19
REMARK 465 VAL A 20
REMARK 465 ARG A 21
REMARK 465 ARG A 22
REMARK 465 ILE A 23
REMARK 465 ALA A 24
REMARK 465 MET A 25
REMARK 465 LYS A 26
REMARK 465 ARG A 27
REMARK 465 ALA A 28
REMARK 465 THR A 29
REMARK 465 VAL A 30
REMARK 465 PRO A 31
REMARK 465 VAL A 32
REMARK 465 LEU A 33
REMARK 465 ARG A 34
REMARK 465 ARG A 35
REMARK 465 VAL A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 VAL A 39
REMARK 465 CYS A 40
REMARK 465 ALA A 41
REMARK 465 ALA A 42
REMARK 465 ALA A 43
REMARK 465 LEU A 44
REMARK 465 LEU A 45
REMARK 465 VAL A 46
REMARK 465 THR A 47
REMARK 465 VAL A 48
REMARK 465 GLY A 49
REMARK 465 THR A 50
REMARK 465 GLY A 51
REMARK 465 GLY A 52
REMARK 465 PRO A 53
REMARK 465 ALA A 54
REMARK 465 SER A 55
REMARK 465 ALA A 56
REMARK 465 THR A 57
REMARK 465 GLY A 58
REMARK 465 THR A 59
REMARK 465 ARG A 60
REMARK 465 GLU A 377
REMARK 465 HIS A 378
REMARK 465 HIS A 379
REMARK 465 HIS A 380
REMARK 465 HIS A 381
REMARK 465 HIS A 382
REMARK 465 HIS A 383
REMARK 465 VAL B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 LEU B 4
REMARK 465 SER B 5
REMARK 465 ARG B 6
REMARK 465 LEU B 7
REMARK 465 GLY B 8
REMARK 465 GLU B 9
REMARK 465 PRO B 10
REMARK 465 PRO B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 HIS B 14
REMARK 465 ASP B 15
REMARK 465 GLY B 16
REMARK 465 ASN B 17
REMARK 465 SER B 18
REMARK 465 GLU B 19
REMARK 465 VAL B 20
REMARK 465 ARG B 21
REMARK 465 ARG B 22
REMARK 465 ILE B 23
REMARK 465 ALA B 24
REMARK 465 MET B 25
REMARK 465 LYS B 26
REMARK 465 ARG B 27
REMARK 465 ALA B 28
REMARK 465 THR B 29
REMARK 465 VAL B 30
REMARK 465 PRO B 31
REMARK 465 VAL B 32
REMARK 465 LEU B 33
REMARK 465 ARG B 34
REMARK 465 ARG B 35
REMARK 465 VAL B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 VAL B 39
REMARK 465 CYS B 40
REMARK 465 ALA B 41
REMARK 465 ALA B 42
REMARK 465 ALA B 43
REMARK 465 LEU B 44
REMARK 465 LEU B 45
REMARK 465 VAL B 46
REMARK 465 THR B 47
REMARK 465 VAL B 48
REMARK 465 GLY B 49
REMARK 465 THR B 50
REMARK 465 GLY B 51
REMARK 465 GLY B 52
REMARK 465 PRO B 53
REMARK 465 ALA B 54
REMARK 465 SER B 55
REMARK 465 ALA B 56
REMARK 465 THR B 57
REMARK 465 GLY B 58
REMARK 465 THR B 59
REMARK 465 ARG B 60
REMARK 465 GLU B 377
REMARK 465 HIS B 378
REMARK 465 HIS B 379
REMARK 465 HIS B 380
REMARK 465 HIS B 381
REMARK 465 HIS B 382
REMARK 465 HIS B 383
REMARK 465 VAL C 1
REMARK 465 THR C 2
REMARK 465 ALA C 3
REMARK 465 LEU C 4
REMARK 465 SER C 5
REMARK 465 ARG C 6
REMARK 465 LEU C 7
REMARK 465 GLY C 8
REMARK 465 GLU C 9
REMARK 465 PRO C 10
REMARK 465 PRO C 11
REMARK 465 SER C 12
REMARK 465 GLY C 13
REMARK 465 HIS C 14
REMARK 465 ASP C 15
REMARK 465 GLY C 16
REMARK 465 ASN C 17
REMARK 465 SER C 18
REMARK 465 GLU C 19
REMARK 465 VAL C 20
REMARK 465 ARG C 21
REMARK 465 ARG C 22
REMARK 465 ILE C 23
REMARK 465 ALA C 24
REMARK 465 MET C 25
REMARK 465 LYS C 26
REMARK 465 ARG C 27
REMARK 465 ALA C 28
REMARK 465 THR C 29
REMARK 465 VAL C 30
REMARK 465 PRO C 31
REMARK 465 VAL C 32
REMARK 465 LEU C 33
REMARK 465 ARG C 34
REMARK 465 ARG C 35
REMARK 465 VAL C 36
REMARK 465 ALA C 37
REMARK 465 ALA C 38
REMARK 465 VAL C 39
REMARK 465 CYS C 40
REMARK 465 ALA C 41
REMARK 465 ALA C 42
REMARK 465 ALA C 43
REMARK 465 LEU C 44
REMARK 465 LEU C 45
REMARK 465 VAL C 46
REMARK 465 THR C 47
REMARK 465 VAL C 48
REMARK 465 GLY C 49
REMARK 465 THR C 50
REMARK 465 GLY C 51
REMARK 465 GLY C 52
REMARK 465 PRO C 53
REMARK 465 ALA C 54
REMARK 465 SER C 55
REMARK 465 ALA C 56
REMARK 465 THR C 57
REMARK 465 GLY C 58
REMARK 465 THR C 59
REMARK 465 ARG C 60
REMARK 465 GLU C 377
REMARK 465 HIS C 378
REMARK 465 HIS C 379
REMARK 465 HIS C 380
REMARK 465 HIS C 381
REMARK 465 HIS C 382
REMARK 465 HIS C 383
REMARK 465 VAL E 1
REMARK 465 THR E 2
REMARK 465 ALA E 3
REMARK 465 LEU E 4
REMARK 465 SER E 5
REMARK 465 ARG E 6
REMARK 465 LEU E 7
REMARK 465 GLY E 8
REMARK 465 GLU E 9
REMARK 465 PRO E 10
REMARK 465 PRO E 11
REMARK 465 SER E 12
REMARK 465 GLY E 13
REMARK 465 HIS E 14
REMARK 465 ASP E 15
REMARK 465 GLY E 16
REMARK 465 ASN E 17
REMARK 465 SER E 18
REMARK 465 GLU E 19
REMARK 465 VAL E 20
REMARK 465 ARG E 21
REMARK 465 ARG E 22
REMARK 465 ILE E 23
REMARK 465 ALA E 24
REMARK 465 MET E 25
REMARK 465 LYS E 26
REMARK 465 ARG E 27
REMARK 465 ALA E 28
REMARK 465 THR E 29
REMARK 465 VAL E 30
REMARK 465 PRO E 31
REMARK 465 VAL E 32
REMARK 465 LEU E 33
REMARK 465 ARG E 34
REMARK 465 ARG E 35
REMARK 465 VAL E 36
REMARK 465 ALA E 37
REMARK 465 ALA E 38
REMARK 465 VAL E 39
REMARK 465 CYS E 40
REMARK 465 ALA E 41
REMARK 465 ALA E 42
REMARK 465 ALA E 43
REMARK 465 LEU E 44
REMARK 465 LEU E 45
REMARK 465 VAL E 46
REMARK 465 THR E 47
REMARK 465 VAL E 48
REMARK 465 GLY E 49
REMARK 465 THR E 50
REMARK 465 GLY E 51
REMARK 465 GLY E 52
REMARK 465 PRO E 53
REMARK 465 ALA E 54
REMARK 465 SER E 55
REMARK 465 ALA E 56
REMARK 465 THR E 57
REMARK 465 GLY E 58
REMARK 465 THR E 59
REMARK 465 ARG E 60
REMARK 465 GLU E 377
REMARK 465 HIS E 378
REMARK 465 HIS E 379
REMARK 465 HIS E 380
REMARK 465 HIS E 381
REMARK 465 HIS E 382
REMARK 465 HIS E 383
REMARK 465 VAL F 1
REMARK 465 THR F 2
REMARK 465 ALA F 3
REMARK 465 LEU F 4
REMARK 465 SER F 5
REMARK 465 ARG F 6
REMARK 465 LEU F 7
REMARK 465 GLY F 8
REMARK 465 GLU F 9
REMARK 465 PRO F 10
REMARK 465 PRO F 11
REMARK 465 SER F 12
REMARK 465 GLY F 13
REMARK 465 HIS F 14
REMARK 465 ASP F 15
REMARK 465 GLY F 16
REMARK 465 ASN F 17
REMARK 465 SER F 18
REMARK 465 GLU F 19
REMARK 465 VAL F 20
REMARK 465 ARG F 21
REMARK 465 ARG F 22
REMARK 465 ILE F 23
REMARK 465 ALA F 24
REMARK 465 MET F 25
REMARK 465 LYS F 26
REMARK 465 ARG F 27
REMARK 465 ALA F 28
REMARK 465 THR F 29
REMARK 465 VAL F 30
REMARK 465 PRO F 31
REMARK 465 VAL F 32
REMARK 465 LEU F 33
REMARK 465 ARG F 34
REMARK 465 ARG F 35
REMARK 465 VAL F 36
REMARK 465 ALA F 37
REMARK 465 ALA F 38
REMARK 465 VAL F 39
REMARK 465 CYS F 40
REMARK 465 ALA F 41
REMARK 465 ALA F 42
REMARK 465 ALA F 43
REMARK 465 LEU F 44
REMARK 465 LEU F 45
REMARK 465 VAL F 46
REMARK 465 THR F 47
REMARK 465 VAL F 48
REMARK 465 GLY F 49
REMARK 465 THR F 50
REMARK 465 GLY F 51
REMARK 465 GLY F 52
REMARK 465 PRO F 53
REMARK 465 ALA F 54
REMARK 465 SER F 55
REMARK 465 ALA F 56
REMARK 465 THR F 57
REMARK 465 GLY F 58
REMARK 465 THR F 59
REMARK 465 ARG F 60
REMARK 465 SER F 61
REMARK 465 ALA F 62
REMARK 465 GLU F 377
REMARK 465 HIS F 378
REMARK 465 HIS F 379
REMARK 465 HIS F 380
REMARK 465 HIS F 381
REMARK 465 HIS F 382
REMARK 465 HIS F 383
REMARK 465 VAL G 1
REMARK 465 THR G 2
REMARK 465 ALA G 3
REMARK 465 LEU G 4
REMARK 465 SER G 5
REMARK 465 ARG G 6
REMARK 465 LEU G 7
REMARK 465 GLY G 8
REMARK 465 GLU G 9
REMARK 465 PRO G 10
REMARK 465 PRO G 11
REMARK 465 SER G 12
REMARK 465 GLY G 13
REMARK 465 HIS G 14
REMARK 465 ASP G 15
REMARK 465 GLY G 16
REMARK 465 ASN G 17
REMARK 465 SER G 18
REMARK 465 GLU G 19
REMARK 465 VAL G 20
REMARK 465 ARG G 21
REMARK 465 ARG G 22
REMARK 465 ILE G 23
REMARK 465 ALA G 24
REMARK 465 MET G 25
REMARK 465 LYS G 26
REMARK 465 ARG G 27
REMARK 465 ALA G 28
REMARK 465 THR G 29
REMARK 465 VAL G 30
REMARK 465 PRO G 31
REMARK 465 VAL G 32
REMARK 465 LEU G 33
REMARK 465 ARG G 34
REMARK 465 ARG G 35
REMARK 465 VAL G 36
REMARK 465 ALA G 37
REMARK 465 ALA G 38
REMARK 465 VAL G 39
REMARK 465 CYS G 40
REMARK 465 ALA G 41
REMARK 465 ALA G 42
REMARK 465 ALA G 43
REMARK 465 LEU G 44
REMARK 465 LEU G 45
REMARK 465 VAL G 46
REMARK 465 THR G 47
REMARK 465 VAL G 48
REMARK 465 GLY G 49
REMARK 465 THR G 50
REMARK 465 GLY G 51
REMARK 465 GLY G 52
REMARK 465 PRO G 53
REMARK 465 ALA G 54
REMARK 465 SER G 55
REMARK 465 ALA G 56
REMARK 465 THR G 57
REMARK 465 GLY G 58
REMARK 465 THR G 59
REMARK 465 ARG G 60
REMARK 465 GLU G 377
REMARK 465 HIS G 378
REMARK 465 HIS G 379
REMARK 465 HIS G 380
REMARK 465 HIS G 381
REMARK 465 HIS G 382
REMARK 465 HIS G 383
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 SER D 61 OG
REMARK 470 SER A 61 OG
REMARK 470 SER B 61 OG
REMARK 470 SER C 61 OG
REMARK 470 SER E 61 OG
REMARK 470 SER G 61 OG
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 F 370 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU D 73 81.72 -155.59
REMARK 500 THR D 103 -9.43 83.16
REMARK 500 ALA D 185 -127.23 64.50
REMARK 500 PRO D 228 -9.08 -59.62
REMARK 500 TYR D 316 -136.87 -126.85
REMARK 500 VAL D 372 -44.16 -131.49
REMARK 500 LEU A 73 84.19 -157.30
REMARK 500 ASN A 105 -158.42 -133.24
REMARK 500 ARG A 136 152.88 -49.95
REMARK 500 ALA A 185 -122.23 65.45
REMARK 500 PRO A 249 130.70 -38.82
REMARK 500 TYR A 316 -132.24 -112.92
REMARK 500 PRO A 331 3.02 -57.60
REMARK 500 ASN A 356 35.94 -99.78
REMARK 500 LEU B 73 89.91 -150.02
REMARK 500 THR B 103 -6.84 83.95
REMARK 500 ASN B 105 -157.26 -133.77
REMARK 500 ARG B 136 155.65 -42.89
REMARK 500 ALA B 185 -127.68 59.93
REMARK 500 TYR B 316 -141.59 -119.35
REMARK 500 ASN C 105 -156.46 -136.09
REMARK 500 GLN C 114 57.14 39.60
REMARK 500 LYS C 117 -65.49 -91.75
REMARK 500 ALA C 185 -122.32 67.40
REMARK 500 TYR C 316 -137.56 -101.82
REMARK 500 TRP C 333 48.38 -140.60
REMARK 500 ASN C 356 41.89 -95.75
REMARK 500 VAL C 372 -49.40 -135.19
REMARK 500 ALA E 185 -118.10 52.29
REMARK 500 TYR E 316 -129.24 -113.47
REMARK 500 ASN E 356 45.86 -94.45
REMARK 500 VAL E 372 -39.71 -133.18
REMARK 500 LEU F 73 85.42 -151.57
REMARK 500 ASN F 105 -158.28 -139.89
REMARK 500 ARG F 136 151.37 -49.54
REMARK 500 ALA F 185 -120.04 60.62
REMARK 500 ARG F 307 58.46 -108.12
REMARK 500 TYR F 316 -134.14 -123.74
REMARK 500 ASN F 356 40.46 -93.10
REMARK 500 VAL F 372 -47.25 -133.61
REMARK 500 ALA G 185 -121.30 64.72
REMARK 500 TYR G 316 -125.53 -127.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 505 DISTANCE = 7.70 ANGSTROMS
REMARK 525 HOH A 502 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 509 DISTANCE = 7.14 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue STM D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue STM A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue STM B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue STM C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue STM E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue STM F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue STM G 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HDF RELATED DB: PDB
DBREF 5HDP D 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
DBREF 5HDP A 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
DBREF 5HDP B 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
DBREF 5HDP C 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
DBREF 5HDP E 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
DBREF 5HDP F 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
DBREF 5HDP G 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
SEQADV 5HDP VAL D 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP ALA D 185 UNP L7PIJ2 SER 185 ENGINEERED MUTATION
SEQADV 5HDP LEU D 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP GLU D 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS D 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS D 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS D 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS D 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS D 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS D 383 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP VAL A 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP ALA A 185 UNP L7PIJ2 SER 185 ENGINEERED MUTATION
SEQADV 5HDP LEU A 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP GLU A 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS A 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS A 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS A 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS A 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS A 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS A 383 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP VAL B 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP ALA B 185 UNP L7PIJ2 SER 185 ENGINEERED MUTATION
SEQADV 5HDP LEU B 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP GLU B 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS B 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS B 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS B 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS B 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS B 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS B 383 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP VAL C 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP ALA C 185 UNP L7PIJ2 SER 185 ENGINEERED MUTATION
SEQADV 5HDP LEU C 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP GLU C 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS C 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS C 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS C 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS C 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS C 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS C 383 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP VAL E 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP ALA E 185 UNP L7PIJ2 SER 185 ENGINEERED MUTATION
SEQADV 5HDP LEU E 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP GLU E 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS E 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS E 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS E 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS E 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS E 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS E 383 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP VAL F 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP ALA F 185 UNP L7PIJ2 SER 185 ENGINEERED MUTATION
SEQADV 5HDP LEU F 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP GLU F 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS F 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS F 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS F 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS F 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS F 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS F 383 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP VAL G 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP ALA G 185 UNP L7PIJ2 SER 185 ENGINEERED MUTATION
SEQADV 5HDP LEU G 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP GLU G 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS G 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS G 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS G 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS G 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS G 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDP HIS G 383 UNP L7PIJ2 EXPRESSION TAG
SEQRES 1 D 383 VAL THR ALA LEU SER ARG LEU GLY GLU PRO PRO SER GLY
SEQRES 2 D 383 HIS ASP GLY ASN SER GLU VAL ARG ARG ILE ALA MET LYS
SEQRES 3 D 383 ARG ALA THR VAL PRO VAL LEU ARG ARG VAL ALA ALA VAL
SEQRES 4 D 383 CYS ALA ALA ALA LEU LEU VAL THR VAL GLY THR GLY GLY
SEQRES 5 D 383 PRO ALA SER ALA THR GLY THR ARG SER ALA ILE CYS ARG
SEQRES 6 D 383 ALA THR THR VAL GLU VAL THR LEU GLY LYS GLY THR GLY
SEQRES 7 D 383 LYS MET TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 D 383 PRO ASP THR VAL VAL THR MET VAL HIS GLY ALA THR TYR
SEQRES 9 D 383 ASN HIS ASN TYR TRP ASP PHE PRO TYR GLN PRO ASP LYS
SEQRES 10 D 383 TYR SER PHE ARG LYS MET LEU ASN GLY ALA GLY TYR ALA
SEQRES 11 D 383 THR PHE VAL VAL ASP ARG LEU GLY THR GLY ASN SER THR
SEQRES 12 D 383 VAL PRO PRO SER SER GLU LEU ASN LEU THR VAL GLU ALA
SEQRES 13 D 383 ARG GLN MET HIS GLU VAL VAL GLN GLY LEU ARG THR GLY
SEQRES 14 D 383 ARG ILE GLY GLY THR GLY PHE GLY LYS VAL VAL LEU ALA
SEQRES 15 D 383 GLY TYR ALA LEU GLY SER ALA VAL THR SER ILE GLU ALA
SEQRES 16 D 383 SER THR PHE HIS ASP VAL ASP ALA VAL LEU ILE THR ALA
SEQRES 17 D 383 LEU GLY HIS TYR ASN ASN PRO ALA GLY THR GLN ALA ILE
SEQRES 18 D 383 ILE ASP ASN GLY LEU SER PRO ASN ASP ASP PRO VAL LEU
SEQRES 19 D 383 LYS ASP ARG HIS HIS TYR ASP ASP GLY TYR ALA THR THR
SEQRES 20 D 383 LYS PRO GLY SER ARG LYS HIS VAL PHE TYR ALA ASP ARG
SEQRES 21 D 383 PRO MET ASP PRO GLY VAL LEU ALA THR ASP GLU LEU THR
SEQRES 22 D 383 LYS ASP ALA ASN VAL PHE THR GLU ALA ALA ASP PRO LEU
SEQRES 23 D 383 VAL ILE ASP PRO ALA VAL SER ARG ALA ILE ASP VAL PRO
SEQRES 24 D 383 VAL MET PHE ALA LEU GLY ASP ARG ASP PRO LEU MET CYS
SEQRES 25 D 383 GLY ASP GLY TYR GLU ASP CYS SER SER GLN ALA ALA LEU
SEQRES 26 D 383 ARG ALA GLN GLU ALA PRO PHE TRP THR SER ALA PRO SER
SEQRES 27 D 383 PHE ASP VAL ILE LEU VAL GLU ASP ALA GLY HIS GLY LEU
SEQRES 28 D 383 ASN LEU VAL PRO ASN THR ARG VAL TYR GLN ASP ALA SER
SEQRES 29 D 383 ARG ASP TRP LEU ASP ARG VAL VAL GLY HIS GLY LEU GLU
SEQRES 30 D 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 A 383 VAL THR ALA LEU SER ARG LEU GLY GLU PRO PRO SER GLY
SEQRES 2 A 383 HIS ASP GLY ASN SER GLU VAL ARG ARG ILE ALA MET LYS
SEQRES 3 A 383 ARG ALA THR VAL PRO VAL LEU ARG ARG VAL ALA ALA VAL
SEQRES 4 A 383 CYS ALA ALA ALA LEU LEU VAL THR VAL GLY THR GLY GLY
SEQRES 5 A 383 PRO ALA SER ALA THR GLY THR ARG SER ALA ILE CYS ARG
SEQRES 6 A 383 ALA THR THR VAL GLU VAL THR LEU GLY LYS GLY THR GLY
SEQRES 7 A 383 LYS MET TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 A 383 PRO ASP THR VAL VAL THR MET VAL HIS GLY ALA THR TYR
SEQRES 9 A 383 ASN HIS ASN TYR TRP ASP PHE PRO TYR GLN PRO ASP LYS
SEQRES 10 A 383 TYR SER PHE ARG LYS MET LEU ASN GLY ALA GLY TYR ALA
SEQRES 11 A 383 THR PHE VAL VAL ASP ARG LEU GLY THR GLY ASN SER THR
SEQRES 12 A 383 VAL PRO PRO SER SER GLU LEU ASN LEU THR VAL GLU ALA
SEQRES 13 A 383 ARG GLN MET HIS GLU VAL VAL GLN GLY LEU ARG THR GLY
SEQRES 14 A 383 ARG ILE GLY GLY THR GLY PHE GLY LYS VAL VAL LEU ALA
SEQRES 15 A 383 GLY TYR ALA LEU GLY SER ALA VAL THR SER ILE GLU ALA
SEQRES 16 A 383 SER THR PHE HIS ASP VAL ASP ALA VAL LEU ILE THR ALA
SEQRES 17 A 383 LEU GLY HIS TYR ASN ASN PRO ALA GLY THR GLN ALA ILE
SEQRES 18 A 383 ILE ASP ASN GLY LEU SER PRO ASN ASP ASP PRO VAL LEU
SEQRES 19 A 383 LYS ASP ARG HIS HIS TYR ASP ASP GLY TYR ALA THR THR
SEQRES 20 A 383 LYS PRO GLY SER ARG LYS HIS VAL PHE TYR ALA ASP ARG
SEQRES 21 A 383 PRO MET ASP PRO GLY VAL LEU ALA THR ASP GLU LEU THR
SEQRES 22 A 383 LYS ASP ALA ASN VAL PHE THR GLU ALA ALA ASP PRO LEU
SEQRES 23 A 383 VAL ILE ASP PRO ALA VAL SER ARG ALA ILE ASP VAL PRO
SEQRES 24 A 383 VAL MET PHE ALA LEU GLY ASP ARG ASP PRO LEU MET CYS
SEQRES 25 A 383 GLY ASP GLY TYR GLU ASP CYS SER SER GLN ALA ALA LEU
SEQRES 26 A 383 ARG ALA GLN GLU ALA PRO PHE TRP THR SER ALA PRO SER
SEQRES 27 A 383 PHE ASP VAL ILE LEU VAL GLU ASP ALA GLY HIS GLY LEU
SEQRES 28 A 383 ASN LEU VAL PRO ASN THR ARG VAL TYR GLN ASP ALA SER
SEQRES 29 A 383 ARG ASP TRP LEU ASP ARG VAL VAL GLY HIS GLY LEU GLU
SEQRES 30 A 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 383 VAL THR ALA LEU SER ARG LEU GLY GLU PRO PRO SER GLY
SEQRES 2 B 383 HIS ASP GLY ASN SER GLU VAL ARG ARG ILE ALA MET LYS
SEQRES 3 B 383 ARG ALA THR VAL PRO VAL LEU ARG ARG VAL ALA ALA VAL
SEQRES 4 B 383 CYS ALA ALA ALA LEU LEU VAL THR VAL GLY THR GLY GLY
SEQRES 5 B 383 PRO ALA SER ALA THR GLY THR ARG SER ALA ILE CYS ARG
SEQRES 6 B 383 ALA THR THR VAL GLU VAL THR LEU GLY LYS GLY THR GLY
SEQRES 7 B 383 LYS MET TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 B 383 PRO ASP THR VAL VAL THR MET VAL HIS GLY ALA THR TYR
SEQRES 9 B 383 ASN HIS ASN TYR TRP ASP PHE PRO TYR GLN PRO ASP LYS
SEQRES 10 B 383 TYR SER PHE ARG LYS MET LEU ASN GLY ALA GLY TYR ALA
SEQRES 11 B 383 THR PHE VAL VAL ASP ARG LEU GLY THR GLY ASN SER THR
SEQRES 12 B 383 VAL PRO PRO SER SER GLU LEU ASN LEU THR VAL GLU ALA
SEQRES 13 B 383 ARG GLN MET HIS GLU VAL VAL GLN GLY LEU ARG THR GLY
SEQRES 14 B 383 ARG ILE GLY GLY THR GLY PHE GLY LYS VAL VAL LEU ALA
SEQRES 15 B 383 GLY TYR ALA LEU GLY SER ALA VAL THR SER ILE GLU ALA
SEQRES 16 B 383 SER THR PHE HIS ASP VAL ASP ALA VAL LEU ILE THR ALA
SEQRES 17 B 383 LEU GLY HIS TYR ASN ASN PRO ALA GLY THR GLN ALA ILE
SEQRES 18 B 383 ILE ASP ASN GLY LEU SER PRO ASN ASP ASP PRO VAL LEU
SEQRES 19 B 383 LYS ASP ARG HIS HIS TYR ASP ASP GLY TYR ALA THR THR
SEQRES 20 B 383 LYS PRO GLY SER ARG LYS HIS VAL PHE TYR ALA ASP ARG
SEQRES 21 B 383 PRO MET ASP PRO GLY VAL LEU ALA THR ASP GLU LEU THR
SEQRES 22 B 383 LYS ASP ALA ASN VAL PHE THR GLU ALA ALA ASP PRO LEU
SEQRES 23 B 383 VAL ILE ASP PRO ALA VAL SER ARG ALA ILE ASP VAL PRO
SEQRES 24 B 383 VAL MET PHE ALA LEU GLY ASP ARG ASP PRO LEU MET CYS
SEQRES 25 B 383 GLY ASP GLY TYR GLU ASP CYS SER SER GLN ALA ALA LEU
SEQRES 26 B 383 ARG ALA GLN GLU ALA PRO PHE TRP THR SER ALA PRO SER
SEQRES 27 B 383 PHE ASP VAL ILE LEU VAL GLU ASP ALA GLY HIS GLY LEU
SEQRES 28 B 383 ASN LEU VAL PRO ASN THR ARG VAL TYR GLN ASP ALA SER
SEQRES 29 B 383 ARG ASP TRP LEU ASP ARG VAL VAL GLY HIS GLY LEU GLU
SEQRES 30 B 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 383 VAL THR ALA LEU SER ARG LEU GLY GLU PRO PRO SER GLY
SEQRES 2 C 383 HIS ASP GLY ASN SER GLU VAL ARG ARG ILE ALA MET LYS
SEQRES 3 C 383 ARG ALA THR VAL PRO VAL LEU ARG ARG VAL ALA ALA VAL
SEQRES 4 C 383 CYS ALA ALA ALA LEU LEU VAL THR VAL GLY THR GLY GLY
SEQRES 5 C 383 PRO ALA SER ALA THR GLY THR ARG SER ALA ILE CYS ARG
SEQRES 6 C 383 ALA THR THR VAL GLU VAL THR LEU GLY LYS GLY THR GLY
SEQRES 7 C 383 LYS MET TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 C 383 PRO ASP THR VAL VAL THR MET VAL HIS GLY ALA THR TYR
SEQRES 9 C 383 ASN HIS ASN TYR TRP ASP PHE PRO TYR GLN PRO ASP LYS
SEQRES 10 C 383 TYR SER PHE ARG LYS MET LEU ASN GLY ALA GLY TYR ALA
SEQRES 11 C 383 THR PHE VAL VAL ASP ARG LEU GLY THR GLY ASN SER THR
SEQRES 12 C 383 VAL PRO PRO SER SER GLU LEU ASN LEU THR VAL GLU ALA
SEQRES 13 C 383 ARG GLN MET HIS GLU VAL VAL GLN GLY LEU ARG THR GLY
SEQRES 14 C 383 ARG ILE GLY GLY THR GLY PHE GLY LYS VAL VAL LEU ALA
SEQRES 15 C 383 GLY TYR ALA LEU GLY SER ALA VAL THR SER ILE GLU ALA
SEQRES 16 C 383 SER THR PHE HIS ASP VAL ASP ALA VAL LEU ILE THR ALA
SEQRES 17 C 383 LEU GLY HIS TYR ASN ASN PRO ALA GLY THR GLN ALA ILE
SEQRES 18 C 383 ILE ASP ASN GLY LEU SER PRO ASN ASP ASP PRO VAL LEU
SEQRES 19 C 383 LYS ASP ARG HIS HIS TYR ASP ASP GLY TYR ALA THR THR
SEQRES 20 C 383 LYS PRO GLY SER ARG LYS HIS VAL PHE TYR ALA ASP ARG
SEQRES 21 C 383 PRO MET ASP PRO GLY VAL LEU ALA THR ASP GLU LEU THR
SEQRES 22 C 383 LYS ASP ALA ASN VAL PHE THR GLU ALA ALA ASP PRO LEU
SEQRES 23 C 383 VAL ILE ASP PRO ALA VAL SER ARG ALA ILE ASP VAL PRO
SEQRES 24 C 383 VAL MET PHE ALA LEU GLY ASP ARG ASP PRO LEU MET CYS
SEQRES 25 C 383 GLY ASP GLY TYR GLU ASP CYS SER SER GLN ALA ALA LEU
SEQRES 26 C 383 ARG ALA GLN GLU ALA PRO PHE TRP THR SER ALA PRO SER
SEQRES 27 C 383 PHE ASP VAL ILE LEU VAL GLU ASP ALA GLY HIS GLY LEU
SEQRES 28 C 383 ASN LEU VAL PRO ASN THR ARG VAL TYR GLN ASP ALA SER
SEQRES 29 C 383 ARG ASP TRP LEU ASP ARG VAL VAL GLY HIS GLY LEU GLU
SEQRES 30 C 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 E 383 VAL THR ALA LEU SER ARG LEU GLY GLU PRO PRO SER GLY
SEQRES 2 E 383 HIS ASP GLY ASN SER GLU VAL ARG ARG ILE ALA MET LYS
SEQRES 3 E 383 ARG ALA THR VAL PRO VAL LEU ARG ARG VAL ALA ALA VAL
SEQRES 4 E 383 CYS ALA ALA ALA LEU LEU VAL THR VAL GLY THR GLY GLY
SEQRES 5 E 383 PRO ALA SER ALA THR GLY THR ARG SER ALA ILE CYS ARG
SEQRES 6 E 383 ALA THR THR VAL GLU VAL THR LEU GLY LYS GLY THR GLY
SEQRES 7 E 383 LYS MET TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 E 383 PRO ASP THR VAL VAL THR MET VAL HIS GLY ALA THR TYR
SEQRES 9 E 383 ASN HIS ASN TYR TRP ASP PHE PRO TYR GLN PRO ASP LYS
SEQRES 10 E 383 TYR SER PHE ARG LYS MET LEU ASN GLY ALA GLY TYR ALA
SEQRES 11 E 383 THR PHE VAL VAL ASP ARG LEU GLY THR GLY ASN SER THR
SEQRES 12 E 383 VAL PRO PRO SER SER GLU LEU ASN LEU THR VAL GLU ALA
SEQRES 13 E 383 ARG GLN MET HIS GLU VAL VAL GLN GLY LEU ARG THR GLY
SEQRES 14 E 383 ARG ILE GLY GLY THR GLY PHE GLY LYS VAL VAL LEU ALA
SEQRES 15 E 383 GLY TYR ALA LEU GLY SER ALA VAL THR SER ILE GLU ALA
SEQRES 16 E 383 SER THR PHE HIS ASP VAL ASP ALA VAL LEU ILE THR ALA
SEQRES 17 E 383 LEU GLY HIS TYR ASN ASN PRO ALA GLY THR GLN ALA ILE
SEQRES 18 E 383 ILE ASP ASN GLY LEU SER PRO ASN ASP ASP PRO VAL LEU
SEQRES 19 E 383 LYS ASP ARG HIS HIS TYR ASP ASP GLY TYR ALA THR THR
SEQRES 20 E 383 LYS PRO GLY SER ARG LYS HIS VAL PHE TYR ALA ASP ARG
SEQRES 21 E 383 PRO MET ASP PRO GLY VAL LEU ALA THR ASP GLU LEU THR
SEQRES 22 E 383 LYS ASP ALA ASN VAL PHE THR GLU ALA ALA ASP PRO LEU
SEQRES 23 E 383 VAL ILE ASP PRO ALA VAL SER ARG ALA ILE ASP VAL PRO
SEQRES 24 E 383 VAL MET PHE ALA LEU GLY ASP ARG ASP PRO LEU MET CYS
SEQRES 25 E 383 GLY ASP GLY TYR GLU ASP CYS SER SER GLN ALA ALA LEU
SEQRES 26 E 383 ARG ALA GLN GLU ALA PRO PHE TRP THR SER ALA PRO SER
SEQRES 27 E 383 PHE ASP VAL ILE LEU VAL GLU ASP ALA GLY HIS GLY LEU
SEQRES 28 E 383 ASN LEU VAL PRO ASN THR ARG VAL TYR GLN ASP ALA SER
SEQRES 29 E 383 ARG ASP TRP LEU ASP ARG VAL VAL GLY HIS GLY LEU GLU
SEQRES 30 E 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 F 383 VAL THR ALA LEU SER ARG LEU GLY GLU PRO PRO SER GLY
SEQRES 2 F 383 HIS ASP GLY ASN SER GLU VAL ARG ARG ILE ALA MET LYS
SEQRES 3 F 383 ARG ALA THR VAL PRO VAL LEU ARG ARG VAL ALA ALA VAL
SEQRES 4 F 383 CYS ALA ALA ALA LEU LEU VAL THR VAL GLY THR GLY GLY
SEQRES 5 F 383 PRO ALA SER ALA THR GLY THR ARG SER ALA ILE CYS ARG
SEQRES 6 F 383 ALA THR THR VAL GLU VAL THR LEU GLY LYS GLY THR GLY
SEQRES 7 F 383 LYS MET TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 F 383 PRO ASP THR VAL VAL THR MET VAL HIS GLY ALA THR TYR
SEQRES 9 F 383 ASN HIS ASN TYR TRP ASP PHE PRO TYR GLN PRO ASP LYS
SEQRES 10 F 383 TYR SER PHE ARG LYS MET LEU ASN GLY ALA GLY TYR ALA
SEQRES 11 F 383 THR PHE VAL VAL ASP ARG LEU GLY THR GLY ASN SER THR
SEQRES 12 F 383 VAL PRO PRO SER SER GLU LEU ASN LEU THR VAL GLU ALA
SEQRES 13 F 383 ARG GLN MET HIS GLU VAL VAL GLN GLY LEU ARG THR GLY
SEQRES 14 F 383 ARG ILE GLY GLY THR GLY PHE GLY LYS VAL VAL LEU ALA
SEQRES 15 F 383 GLY TYR ALA LEU GLY SER ALA VAL THR SER ILE GLU ALA
SEQRES 16 F 383 SER THR PHE HIS ASP VAL ASP ALA VAL LEU ILE THR ALA
SEQRES 17 F 383 LEU GLY HIS TYR ASN ASN PRO ALA GLY THR GLN ALA ILE
SEQRES 18 F 383 ILE ASP ASN GLY LEU SER PRO ASN ASP ASP PRO VAL LEU
SEQRES 19 F 383 LYS ASP ARG HIS HIS TYR ASP ASP GLY TYR ALA THR THR
SEQRES 20 F 383 LYS PRO GLY SER ARG LYS HIS VAL PHE TYR ALA ASP ARG
SEQRES 21 F 383 PRO MET ASP PRO GLY VAL LEU ALA THR ASP GLU LEU THR
SEQRES 22 F 383 LYS ASP ALA ASN VAL PHE THR GLU ALA ALA ASP PRO LEU
SEQRES 23 F 383 VAL ILE ASP PRO ALA VAL SER ARG ALA ILE ASP VAL PRO
SEQRES 24 F 383 VAL MET PHE ALA LEU GLY ASP ARG ASP PRO LEU MET CYS
SEQRES 25 F 383 GLY ASP GLY TYR GLU ASP CYS SER SER GLN ALA ALA LEU
SEQRES 26 F 383 ARG ALA GLN GLU ALA PRO PHE TRP THR SER ALA PRO SER
SEQRES 27 F 383 PHE ASP VAL ILE LEU VAL GLU ASP ALA GLY HIS GLY LEU
SEQRES 28 F 383 ASN LEU VAL PRO ASN THR ARG VAL TYR GLN ASP ALA SER
SEQRES 29 F 383 ARG ASP TRP LEU ASP ARG VAL VAL GLY HIS GLY LEU GLU
SEQRES 30 F 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 G 383 VAL THR ALA LEU SER ARG LEU GLY GLU PRO PRO SER GLY
SEQRES 2 G 383 HIS ASP GLY ASN SER GLU VAL ARG ARG ILE ALA MET LYS
SEQRES 3 G 383 ARG ALA THR VAL PRO VAL LEU ARG ARG VAL ALA ALA VAL
SEQRES 4 G 383 CYS ALA ALA ALA LEU LEU VAL THR VAL GLY THR GLY GLY
SEQRES 5 G 383 PRO ALA SER ALA THR GLY THR ARG SER ALA ILE CYS ARG
SEQRES 6 G 383 ALA THR THR VAL GLU VAL THR LEU GLY LYS GLY THR GLY
SEQRES 7 G 383 LYS MET TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 G 383 PRO ASP THR VAL VAL THR MET VAL HIS GLY ALA THR TYR
SEQRES 9 G 383 ASN HIS ASN TYR TRP ASP PHE PRO TYR GLN PRO ASP LYS
SEQRES 10 G 383 TYR SER PHE ARG LYS MET LEU ASN GLY ALA GLY TYR ALA
SEQRES 11 G 383 THR PHE VAL VAL ASP ARG LEU GLY THR GLY ASN SER THR
SEQRES 12 G 383 VAL PRO PRO SER SER GLU LEU ASN LEU THR VAL GLU ALA
SEQRES 13 G 383 ARG GLN MET HIS GLU VAL VAL GLN GLY LEU ARG THR GLY
SEQRES 14 G 383 ARG ILE GLY GLY THR GLY PHE GLY LYS VAL VAL LEU ALA
SEQRES 15 G 383 GLY TYR ALA LEU GLY SER ALA VAL THR SER ILE GLU ALA
SEQRES 16 G 383 SER THR PHE HIS ASP VAL ASP ALA VAL LEU ILE THR ALA
SEQRES 17 G 383 LEU GLY HIS TYR ASN ASN PRO ALA GLY THR GLN ALA ILE
SEQRES 18 G 383 ILE ASP ASN GLY LEU SER PRO ASN ASP ASP PRO VAL LEU
SEQRES 19 G 383 LYS ASP ARG HIS HIS TYR ASP ASP GLY TYR ALA THR THR
SEQRES 20 G 383 LYS PRO GLY SER ARG LYS HIS VAL PHE TYR ALA ASP ARG
SEQRES 21 G 383 PRO MET ASP PRO GLY VAL LEU ALA THR ASP GLU LEU THR
SEQRES 22 G 383 LYS ASP ALA ASN VAL PHE THR GLU ALA ALA ASP PRO LEU
SEQRES 23 G 383 VAL ILE ASP PRO ALA VAL SER ARG ALA ILE ASP VAL PRO
SEQRES 24 G 383 VAL MET PHE ALA LEU GLY ASP ARG ASP PRO LEU MET CYS
SEQRES 25 G 383 GLY ASP GLY TYR GLU ASP CYS SER SER GLN ALA ALA LEU
SEQRES 26 G 383 ARG ALA GLN GLU ALA PRO PHE TRP THR SER ALA PRO SER
SEQRES 27 G 383 PHE ASP VAL ILE LEU VAL GLU ASP ALA GLY HIS GLY LEU
SEQRES 28 G 383 ASN LEU VAL PRO ASN THR ARG VAL TYR GLN ASP ALA SER
SEQRES 29 G 383 ARG ASP TRP LEU ASP ARG VAL VAL GLY HIS GLY LEU GLU
SEQRES 30 G 383 HIS HIS HIS HIS HIS HIS
HET STM D 401 36
HET STM A 401 36
HET STM B 401 36
HET STM C 401 36
HET STM E 401 36
HET STM F 401 36
HET STM G 401 36
HETNAM STM METHYL 5-AMINO-6-(7-AMINO-6-METHOXY-5,8-DIOXO-5,8-
HETNAM 2 STM DIHYDROQUINOLIN-2-YL)-4-(2-HYDROXY-3-METHOXYPHENYL)-3-
HETNAM 3 STM METHYLPYRIDINE-2-CARBOXYLATE
FORMUL 8 STM 7(C25 H22 N4 O7)
FORMUL 15 HOH *27(H2 O)
HELIX 1 AA1 ASN D 105 TRP D 109 5 5
HELIX 2 AA2 GLN D 114 SER D 119 1 6
HELIX 3 AA3 SER D 119 ALA D 127 1 9
HELIX 4 AA4 PRO D 146 LEU D 150 5 5
HELIX 5 AA5 ASN D 151 GLY D 169 1 19
HELIX 6 AA6 ALA D 185 HIS D 199 1 15
HELIX 7 AA7 ASN D 214 ASN D 224 1 11
HELIX 8 AA8 SER D 251 PHE D 256 1 6
HELIX 9 AA9 ASP D 263 THR D 273 1 11
HELIX 10 AB1 PHE D 279 ASP D 284 1 6
HELIX 11 AB2 PRO D 285 ILE D 288 5 4
HELIX 12 AB3 ASP D 289 ALA D 295 1 7
HELIX 13 AB4 SER D 321 ALA D 330 1 10
HELIX 14 AB5 PRO D 331 TRP D 333 5 3
HELIX 15 AB6 GLY D 350 VAL D 354 5 5
HELIX 16 AB7 ASN D 356 VAL D 372 1 17
HELIX 17 AB8 ASN A 105 ASP A 110 5 6
HELIX 18 AB9 GLN A 114 SER A 119 1 6
HELIX 19 AC1 SER A 119 ALA A 127 1 9
HELIX 20 AC2 PRO A 146 LEU A 150 5 5
HELIX 21 AC3 ASN A 151 GLY A 169 1 19
HELIX 22 AC4 ALA A 185 HIS A 199 1 15
HELIX 23 AC5 ASN A 214 ASN A 224 1 11
HELIX 24 AC6 SER A 251 PHE A 256 1 6
HELIX 25 AC7 ASP A 263 THR A 273 1 11
HELIX 26 AC8 THR A 280 ILE A 288 5 9
HELIX 27 AC9 ASP A 289 ALA A 295 1 7
HELIX 28 AD1 SER A 321 ALA A 330 1 10
HELIX 29 AD2 PRO A 331 TRP A 333 5 3
HELIX 30 AD3 GLY A 350 VAL A 354 5 5
HELIX 31 AD4 ASN A 356 VAL A 372 1 17
HELIX 32 AD5 ASN B 105 TRP B 109 5 5
HELIX 33 AD6 GLN B 114 SER B 119 1 6
HELIX 34 AD7 SER B 119 ALA B 127 1 9
HELIX 35 AD8 PRO B 146 LEU B 150 5 5
HELIX 36 AD9 ASN B 151 GLY B 169 1 19
HELIX 37 AE1 ALA B 185 HIS B 199 1 15
HELIX 38 AE2 ASN B 214 ASN B 224 1 11
HELIX 39 AE3 SER B 251 PHE B 256 1 6
HELIX 40 AE4 ASP B 263 THR B 273 1 11
HELIX 41 AE5 THR B 280 ALA B 282 5 3
HELIX 42 AE6 ASP B 284 ILE B 288 5 5
HELIX 43 AE7 ASP B 289 ARG B 294 1 6
HELIX 44 AE8 SER B 321 ALA B 330 1 10
HELIX 45 AE9 PRO B 331 TRP B 333 5 3
HELIX 46 AF1 GLY B 350 VAL B 354 5 5
HELIX 47 AF2 ASN B 356 VAL B 372 1 17
HELIX 48 AF3 ASN C 105 TRP C 109 5 5
HELIX 49 AF4 GLN C 114 SER C 119 1 6
HELIX 50 AF5 SER C 119 ALA C 127 1 9
HELIX 51 AF6 PRO C 146 LEU C 150 5 5
HELIX 52 AF7 ASN C 151 THR C 168 1 18
HELIX 53 AF8 ALA C 185 PHE C 198 1 14
HELIX 54 AF9 ASN C 214 ASN C 224 1 11
HELIX 55 AG1 SER C 251 PHE C 256 1 6
HELIX 56 AG2 ASP C 263 THR C 273 1 11
HELIX 57 AG3 THR C 280 ASP C 284 5 5
HELIX 58 AG4 ASP C 289 ALA C 295 1 7
HELIX 59 AG5 SER C 321 ALA C 330 1 10
HELIX 60 AG6 PRO C 331 TRP C 333 5 3
HELIX 61 AG7 GLY C 350 VAL C 354 5 5
HELIX 62 AG8 ASN C 356 VAL C 372 1 17
HELIX 63 AG9 ASN E 105 TRP E 109 5 5
HELIX 64 AH1 GLN E 114 SER E 119 1 6
HELIX 65 AH2 SER E 119 ALA E 127 1 9
HELIX 66 AH3 PRO E 146 LEU E 150 5 5
HELIX 67 AH4 ASN E 151 GLY E 169 1 19
HELIX 68 AH5 ALA E 185 HIS E 199 1 15
HELIX 69 AH6 ASN E 214 ASN E 224 1 11
HELIX 70 AH7 SER E 251 PHE E 256 1 6
HELIX 71 AH8 ASP E 263 THR E 273 1 11
HELIX 72 AH9 THR E 280 ALA E 282 5 3
HELIX 73 AI1 ASP E 289 ALA E 295 1 7
HELIX 74 AI2 SER E 321 ALA E 330 1 10
HELIX 75 AI3 PRO E 331 TRP E 333 5 3
HELIX 76 AI4 ASN E 356 VAL E 372 1 17
HELIX 77 AI5 GLN F 114 SER F 119 1 6
HELIX 78 AI6 SER F 119 ALA F 127 1 9
HELIX 79 AI7 PRO F 146 LEU F 150 5 5
HELIX 80 AI8 ASN F 151 GLY F 169 1 19
HELIX 81 AI9 ALA F 185 HIS F 199 1 15
HELIX 82 AJ1 ASN F 214 ASN F 224 1 11
HELIX 83 AJ2 SER F 251 PHE F 256 1 6
HELIX 84 AJ3 ASP F 263 THR F 273 1 11
HELIX 85 AJ4 THR F 280 ILE F 288 5 9
HELIX 86 AJ5 ASP F 289 ALA F 295 1 7
HELIX 87 AJ6 SER F 321 ALA F 330 1 10
HELIX 88 AJ7 PRO F 331 THR F 334 5 4
HELIX 89 AJ8 GLY F 350 VAL F 354 5 5
HELIX 90 AJ9 ASN F 356 VAL F 372 1 17
HELIX 91 AK1 ASN G 105 TRP G 109 5 5
HELIX 92 AK2 GLN G 114 SER G 119 1 6
HELIX 93 AK3 SER G 119 ALA G 127 1 9
HELIX 94 AK4 PRO G 146 LEU G 150 5 5
HELIX 95 AK5 ASN G 151 GLY G 169 1 19
HELIX 96 AK6 ALA G 185 HIS G 199 1 15
HELIX 97 AK7 ASN G 214 ASN G 224 1 11
HELIX 98 AK8 SER G 251 PHE G 256 1 6
HELIX 99 AK9 ASP G 263 THR G 273 1 11
HELIX 100 AL1 THR G 280 ASP G 284 5 5
HELIX 101 AL2 ASP G 289 ILE G 296 1 8
HELIX 102 AL3 SER G 321 ALA G 330 1 10
HELIX 103 AL4 PRO G 331 TRP G 333 5 3
HELIX 104 AL5 GLY G 350 VAL G 354 5 5
HELIX 105 AL6 ASN G 356 VAL G 372 1 17
SHEET 1 AA1 8 ALA D 62 VAL D 71 0
SHEET 2 AA1 8 GLY D 78 PRO D 87 -1 O GLY D 78 N VAL D 71
SHEET 3 AA1 8 ALA D 130 ASP D 135 -1 O ASP D 135 N TRP D 81
SHEET 4 AA1 8 THR D 94 VAL D 99 1 N VAL D 96 O PHE D 132
SHEET 5 AA1 8 LYS D 178 TYR D 184 1 O VAL D 180 N THR D 97
SHEET 6 AA1 8 ALA D 203 THR D 207 1 O LEU D 205 N LEU D 181
SHEET 7 AA1 8 VAL D 300 GLY D 305 1 O MET D 301 N ILE D 206
SHEET 8 AA1 8 PHE D 339 VAL D 344 1 O VAL D 344 N LEU D 304
SHEET 1 AA2 3 GLY D 225 LEU D 226 0
SHEET 2 AA2 3 TYR D 244 THR D 247 -1 O THR D 246 N LEU D 226
SHEET 3 AA2 3 ASN D 277 VAL D 278 -1 O ASN D 277 N ALA D 245
SHEET 1 AA3 8 ALA A 62 VAL A 71 0
SHEET 2 AA3 8 GLY A 78 PRO A 87 -1 O LEU A 84 N ARG A 65
SHEET 3 AA3 8 ALA A 130 VAL A 134 -1 O VAL A 133 N GLU A 83
SHEET 4 AA3 8 THR A 94 VAL A 99 1 N VAL A 96 O PHE A 132
SHEET 5 AA3 8 LYS A 178 TYR A 184 1 O ALA A 182 N THR A 97
SHEET 6 AA3 8 ALA A 203 THR A 207 1 O LEU A 205 N GLY A 183
SHEET 7 AA3 8 VAL A 300 GLY A 305 1 O ALA A 303 N ILE A 206
SHEET 8 AA3 8 PHE A 339 VAL A 344 1 O ASP A 340 N PHE A 302
SHEET 1 AA4 3 GLY A 225 LEU A 226 0
SHEET 2 AA4 3 TYR A 244 THR A 247 -1 O THR A 246 N LEU A 226
SHEET 3 AA4 3 ASN A 277 VAL A 278 -1 O ASN A 277 N ALA A 245
SHEET 1 AA5 8 ALA B 62 VAL B 71 0
SHEET 2 AA5 8 GLY B 78 PRO B 87 -1 O ARG B 86 N ILE B 63
SHEET 3 AA5 8 ALA B 130 VAL B 134 -1 O VAL B 133 N GLU B 83
SHEET 4 AA5 8 THR B 94 VAL B 99 1 N THR B 94 O ALA B 130
SHEET 5 AA5 8 LYS B 178 TYR B 184 1 O ALA B 182 N THR B 97
SHEET 6 AA5 8 ALA B 203 THR B 207 1 O LEU B 205 N GLY B 183
SHEET 7 AA5 8 VAL B 300 GLY B 305 1 O ALA B 303 N ILE B 206
SHEET 8 AA5 8 PHE B 339 VAL B 344 1 O VAL B 344 N LEU B 304
SHEET 1 AA6 3 GLY B 225 LEU B 226 0
SHEET 2 AA6 3 TYR B 244 THR B 247 -1 O THR B 246 N LEU B 226
SHEET 3 AA6 3 ASN B 277 VAL B 278 -1 O ASN B 277 N ALA B 245
SHEET 1 AA7 8 ALA C 62 VAL C 71 0
SHEET 2 AA7 8 GLY C 78 PRO C 87 -1 O GLY C 78 N VAL C 71
SHEET 3 AA7 8 ALA C 130 VAL C 134 -1 O VAL C 133 N GLU C 83
SHEET 4 AA7 8 THR C 94 VAL C 99 1 N THR C 94 O ALA C 130
SHEET 5 AA7 8 LYS C 178 TYR C 184 1 O ALA C 182 N THR C 97
SHEET 6 AA7 8 ALA C 203 THR C 207 1 O LEU C 205 N GLY C 183
SHEET 7 AA7 8 VAL C 300 GLY C 305 1 O ALA C 303 N ILE C 206
SHEET 8 AA7 8 PHE C 339 VAL C 344 1 O VAL C 344 N LEU C 304
SHEET 1 AA8 3 GLY C 225 LEU C 226 0
SHEET 2 AA8 3 TYR C 244 THR C 247 -1 O THR C 246 N LEU C 226
SHEET 3 AA8 3 ASN C 277 VAL C 278 -1 O ASN C 277 N ALA C 245
SHEET 1 AA9 8 ALA E 62 VAL E 71 0
SHEET 2 AA9 8 GLY E 78 PRO E 87 -1 O GLY E 78 N VAL E 71
SHEET 3 AA9 8 ALA E 130 VAL E 134 -1 O VAL E 133 N GLU E 83
SHEET 4 AA9 8 THR E 94 VAL E 99 1 N VAL E 96 O PHE E 132
SHEET 5 AA9 8 LYS E 178 TYR E 184 1 O ALA E 182 N VAL E 99
SHEET 6 AA9 8 ALA E 203 THR E 207 1 O LEU E 205 N GLY E 183
SHEET 7 AA9 8 VAL E 300 GLY E 305 1 O ALA E 303 N ILE E 206
SHEET 8 AA9 8 PHE E 339 VAL E 344 1 O ASP E 340 N PHE E 302
SHEET 1 AB1 3 GLY E 225 LEU E 226 0
SHEET 2 AB1 3 TYR E 244 THR E 247 -1 O THR E 246 N LEU E 226
SHEET 3 AB1 3 ASN E 277 VAL E 278 -1 O ASN E 277 N ALA E 245
SHEET 1 AB2 8 CYS F 64 VAL F 71 0
SHEET 2 AB2 8 GLY F 78 CYS F 85 -1 O GLY F 82 N THR F 67
SHEET 3 AB2 8 ALA F 130 VAL F 134 -1 O THR F 131 N CYS F 85
SHEET 4 AB2 8 THR F 94 VAL F 99 1 N VAL F 96 O ALA F 130
SHEET 5 AB2 8 LYS F 178 TYR F 184 1 O ALA F 182 N THR F 97
SHEET 6 AB2 8 ALA F 203 THR F 207 1 O LEU F 205 N GLY F 183
SHEET 7 AB2 8 VAL F 300 GLY F 305 1 O MET F 301 N ILE F 206
SHEET 8 AB2 8 PHE F 339 VAL F 344 1 O VAL F 344 N LEU F 304
SHEET 1 AB3 3 GLY F 225 LEU F 226 0
SHEET 2 AB3 3 TYR F 244 THR F 247 -1 O THR F 246 N LEU F 226
SHEET 3 AB3 3 ASN F 277 VAL F 278 -1 O ASN F 277 N ALA F 245
SHEET 1 AB4 8 ALA G 62 VAL G 71 0
SHEET 2 AB4 8 GLY G 78 PRO G 87 -1 O LEU G 84 N ARG G 65
SHEET 3 AB4 8 ALA G 130 VAL G 134 -1 O VAL G 133 N GLU G 83
SHEET 4 AB4 8 THR G 94 VAL G 99 1 N VAL G 96 O ALA G 130
SHEET 5 AB4 8 LYS G 178 TYR G 184 1 O ALA G 182 N THR G 97
SHEET 6 AB4 8 ALA G 203 THR G 207 1 O LEU G 205 N GLY G 183
SHEET 7 AB4 8 VAL G 300 GLY G 305 1 O MET G 301 N ILE G 206
SHEET 8 AB4 8 PHE G 339 VAL G 344 1 O ASP G 340 N PHE G 302
SHEET 1 AB5 3 GLY G 225 LEU G 226 0
SHEET 2 AB5 3 TYR G 244 THR G 247 -1 O THR G 246 N LEU G 226
SHEET 3 AB5 3 ASN G 277 VAL G 278 -1 O ASN G 277 N ALA G 245
SSBOND 1 CYS D 64 CYS D 85 1555 1555 2.05
SSBOND 2 CYS D 312 CYS D 319 1555 1555 2.03
SSBOND 3 CYS A 64 CYS A 85 1555 1555 2.04
SSBOND 4 CYS A 312 CYS A 319 1555 1555 2.04
SSBOND 5 CYS B 64 CYS B 85 1555 1555 2.04
SSBOND 6 CYS B 312 CYS B 319 1555 1555 2.04
SSBOND 7 CYS C 64 CYS C 85 1555 1555 2.04
SSBOND 8 CYS C 312 CYS C 319 1555 1555 2.06
SSBOND 9 CYS E 64 CYS E 85 1555 1555 2.04
SSBOND 10 CYS E 312 CYS E 319 1555 1555 2.03
SSBOND 11 CYS F 64 CYS F 85 1555 1555 2.05
SSBOND 12 CYS F 312 CYS F 319 1555 1555 2.04
SSBOND 13 CYS G 64 CYS G 85 1555 1555 2.05
SSBOND 14 CYS G 312 CYS G 319 1555 1555 2.03
CISPEP 1 GLY D 76 THR D 77 0 -11.40
CISPEP 2 GLY A 76 THR A 77 0 -10.37
CISPEP 3 GLY A 375 LEU A 376 0 6.88
CISPEP 4 GLY B 76 THR B 77 0 -0.77
CISPEP 5 GLY B 375 LEU B 376 0 -4.90
CISPEP 6 GLY C 76 THR C 77 0 3.69
CISPEP 7 GLY C 375 LEU C 376 0 -8.92
CISPEP 8 GLY E 76 THR E 77 0 -9.33
CISPEP 9 GLY E 375 LEU E 376 0 16.38
CISPEP 10 GLY F 76 THR F 77 0 -2.54
CISPEP 11 GLY G 76 THR G 77 0 -6.56
SITE 1 AC1 14 ALA D 102 TYR D 104 ALA D 185 LEU D 186
SITE 2 AC1 14 ILE D 221 ILE D 222 GLY D 225 ALA D 245
SITE 3 AC1 14 ASN D 277 PHE D 279 ALA D 282 VAL D 287
SITE 4 AC1 14 ILE D 288 HIS D 349
SITE 1 AC2 16 ALA A 102 TYR A 104 ALA A 185 LEU A 186
SITE 2 AC2 16 ASN A 213 ILE A 221 ILE A 222 GLY A 225
SITE 3 AC2 16 ALA A 245 ASN A 277 PHE A 279 ALA A 282
SITE 4 AC2 16 VAL A 287 MET A 311 HIS A 349 HOH A 501
SITE 1 AC3 16 GLY B 101 ALA B 102 TYR B 104 ALA B 185
SITE 2 AC3 16 LEU B 186 THR B 218 ILE B 221 ILE B 222
SITE 3 AC3 16 ALA B 245 PHE B 256 ASN B 277 PHE B 279
SITE 4 AC3 16 ALA B 282 VAL B 287 MET B 311 HIS B 349
SITE 1 AC4 14 ALA C 102 TYR C 104 ALA C 185 LEU C 186
SITE 2 AC4 14 ILE C 221 ILE C 222 ALA C 245 PHE C 256
SITE 3 AC4 14 ASN C 277 PHE C 279 ALA C 282 VAL C 287
SITE 4 AC4 14 MET C 311 HIS C 349
SITE 1 AC5 11 ALA E 102 TYR E 104 ALA E 185 LEU E 186
SITE 2 AC5 11 ILE E 221 ALA E 245 PHE E 279 ALA E 282
SITE 3 AC5 11 VAL E 287 HIS E 349 HOH E 501
SITE 1 AC6 15 ALA F 102 TYR F 104 ALA F 185 LEU F 186
SITE 2 AC6 15 ASN F 213 ILE F 221 ALA F 245 PHE F 256
SITE 3 AC6 15 ASN F 277 PHE F 279 ALA F 282 VAL F 287
SITE 4 AC6 15 ILE F 288 MET F 311 HIS F 349
SITE 1 AC7 14 ALA G 102 ALA G 185 LEU G 186 ASN G 213
SITE 2 AC7 14 THR G 218 ILE G 221 ILE G 222 GLY G 225
SITE 3 AC7 14 ALA G 245 PHE G 256 PHE G 279 ALA G 282
SITE 4 AC7 14 VAL G 287 HIS G 349
CRYST1 83.256 92.847 104.037 115.06 106.09 97.69 P 1 7
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 0.012011 0.001621 0.004854 0.00000
SCALE2 0.000000 0.010868 0.006007 0.00000
SCALE3 0.000000 0.000000 0.011430 0.00000
TER 2391 LEU D 376
TER 4782 LEU A 376
TER 7173 LEU B 376
TER 9564 LEU C 376
TER 11955 LEU E 376
TER 14336 LEU F 376
TER 16727 LEU G 376
MASTER 893 0 7 105 77 0 27 616999 7 280 210
END |