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HEADER HYDROLASE 05-JAN-16 5HDF
TITLE HYDROLASE SEMET-STNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE;
COMPND 3 CHAIN: B, A, C, D;
COMPND 4 ENGINEERED: 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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.QIAN
REVDAT 1 11-JAN-17 5HDF 0
JRNL AUTH T.QIAN
JRNL TITL CRYSTAL STRUCTURE OF A HYDROLASE STNA AT 2.2 ANGSTROMS
JRNL TITL 2 RESOLUTION FROM STREPTOMYCES FLOCCULUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.71 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) : 2.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 35537
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1870
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) : 2.71
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.78
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2460
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 115
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9594
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 52
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.31000
REMARK 3 B22 (A**2) : 4.49000
REMARK 3 B33 (A**2) : -2.42000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.22000
REMARK 3 B23 (A**2) : 0.00000
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): 0.316
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.227
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.985
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9837 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8998 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13431 ; 1.250 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20694 ; 1.220 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1264 ; 6.795 ; 5.008
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 444 ;33.375 ;23.806
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1355 ;13.337 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;18.548 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1488 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11407 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2251 ; 0.006 ; 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): 5064 ; 2.219 ; 3.501
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5063 ; 2.215 ; 3.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6323 ; 3.527 ; 5.247
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6324 ; 3.527 ; 5.248
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4773 ; 3.561 ; 3.829
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4774 ; 3.561 ; 3.831
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7109 ; 5.423 ; 5.588
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10628 ; 7.263 ;28.108
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10629 ; 7.263 ;28.115
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 B 61 374 A 61 374 36112 0.09 0.05
REMARK 3 2 B 61 375 C 61 375 36058 0.09 0.05
REMARK 3 3 B 61 375 D 61 375 35838 0.09 0.05
REMARK 3 4 A 61 374 C 61 374 35578 0.10 0.05
REMARK 3 5 A 61 374 D 61 374 35354 0.10 0.05
REMARK 3 6 C 61 376 D 61 376 36128 0.09 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 : 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 5HDF 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_1000216858.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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) : 0.9819
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 : 37623
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.710
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.080
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% 2-PROPANOL, 0.1 M SODIUM CITRATE
REMARK 280 PH 5.0,12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -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 89.21000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.98500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 89.21000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.98500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 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 MSE 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 HIS B 381
REMARK 465 HIS B 382
REMARK 465 HIS B 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 MSE 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 LEU A 376
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 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 MSE 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 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 MSE 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 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 LEU D 73 CB CG CD1 CD2
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 OD2 ASP D 340 NH2 ARG D 370 2.11
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 SER B 185 CA SER B 185 CB 0.097
REMARK 500 SER A 185 CA SER A 185 CB 0.098
REMARK 500 GLY D 76 N GLY D 76 CA 0.097
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 ASP A 202 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 MSE C 262 CA - CB - CG ANGL. DEV. = -11.5 DEGREES
REMARK 500 MSE D 262 CG - SE - CE ANGL. DEV. = 13.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN B 105 -159.84 -136.28
REMARK 500 SER B 185 -130.86 58.37
REMARK 500 TYR B 316 -139.13 -120.12
REMARK 500 ASN B 356 31.17 -94.04
REMARK 500 VAL B 372 -39.53 -131.10
REMARK 500 ASN A 105 -159.38 -136.69
REMARK 500 SER A 185 -131.01 59.75
REMARK 500 TYR A 316 -138.25 -117.44
REMARK 500 ASN A 356 35.29 -96.93
REMARK 500 VAL A 372 -41.64 -130.72
REMARK 500 ASN C 105 -157.32 -135.26
REMARK 500 SER C 185 -130.07 57.61
REMARK 500 TYR C 316 -138.70 -120.12
REMARK 500 VAL C 372 -39.31 -132.03
REMARK 500 ASN D 105 -159.49 -137.99
REMARK 500 SER D 185 -131.35 56.50
REMARK 500 TYR D 316 -137.38 -122.71
REMARK 500 ASN D 356 35.21 -95.20
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 SER B 61 ALA B 62 -147.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HDP RELATED DB: PDB
DBREF 5HDF B 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
DBREF 5HDF A 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
DBREF 5HDF C 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
DBREF 5HDF D 2 375 UNP L7PIJ2 L7PIJ2_9ACTN 2 375
SEQADV 5HDF VAL B 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF LEU B 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF GLU B 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS B 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS B 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS B 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS B 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS B 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS B 383 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF VAL A 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF LEU A 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF GLU A 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS A 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS A 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS A 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS A 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS A 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS A 383 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF VAL C 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF LEU C 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF GLU C 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS C 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS C 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS C 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS C 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS C 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS C 383 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF VAL D 1 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF LEU D 376 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF GLU D 377 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS D 378 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS D 379 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS D 380 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS D 381 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS D 382 UNP L7PIJ2 EXPRESSION TAG
SEQADV 5HDF HIS D 383 UNP L7PIJ2 EXPRESSION TAG
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 MSE 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 MSE TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 B 383 PRO ASP THR VAL VAL THR MSE 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 MSE 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 MSE 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 SER 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 MSE 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 MSE PHE ALA LEU GLY ASP ARG ASP PRO LEU MSE 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 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 MSE 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 MSE TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 A 383 PRO ASP THR VAL VAL THR MSE 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 MSE 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 MSE 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 SER 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 MSE 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 MSE PHE ALA LEU GLY ASP ARG ASP PRO LEU MSE 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 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 MSE 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 MSE TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 C 383 PRO ASP THR VAL VAL THR MSE 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 MSE 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 MSE 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 SER 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 MSE 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 MSE PHE ALA LEU GLY ASP ARG ASP PRO LEU MSE 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 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 MSE 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 MSE TRP GLY GLU LEU CYS ARG PRO ALA GLY SER SER
SEQRES 8 D 383 PRO ASP THR VAL VAL THR MSE 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 MSE 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 MSE 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 SER 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 MSE 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 MSE PHE ALA LEU GLY ASP ARG ASP PRO LEU MSE 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
MODRES 5HDF MSE B 80 MET MODIFIED RESIDUE
MODRES 5HDF MSE B 98 MET MODIFIED RESIDUE
MODRES 5HDF MSE B 123 MET MODIFIED RESIDUE
MODRES 5HDF MSE B 159 MET MODIFIED RESIDUE
MODRES 5HDF MSE B 262 MET MODIFIED RESIDUE
MODRES 5HDF MSE B 301 MET MODIFIED RESIDUE
MODRES 5HDF MSE B 311 MET MODIFIED RESIDUE
MODRES 5HDF MSE A 80 MET MODIFIED RESIDUE
MODRES 5HDF MSE A 98 MET MODIFIED RESIDUE
MODRES 5HDF MSE A 123 MET MODIFIED RESIDUE
MODRES 5HDF MSE A 159 MET MODIFIED RESIDUE
MODRES 5HDF MSE A 262 MET MODIFIED RESIDUE
MODRES 5HDF MSE A 301 MET MODIFIED RESIDUE
MODRES 5HDF MSE A 311 MET MODIFIED RESIDUE
MODRES 5HDF MSE C 80 MET MODIFIED RESIDUE
MODRES 5HDF MSE C 98 MET MODIFIED RESIDUE
MODRES 5HDF MSE C 123 MET MODIFIED RESIDUE
MODRES 5HDF MSE C 159 MET MODIFIED RESIDUE
MODRES 5HDF MSE C 262 MET MODIFIED RESIDUE
MODRES 5HDF MSE C 301 MET MODIFIED RESIDUE
MODRES 5HDF MSE C 311 MET MODIFIED RESIDUE
MODRES 5HDF MSE D 80 MET MODIFIED RESIDUE
MODRES 5HDF MSE D 98 MET MODIFIED RESIDUE
MODRES 5HDF MSE D 123 MET MODIFIED RESIDUE
MODRES 5HDF MSE D 159 MET MODIFIED RESIDUE
MODRES 5HDF MSE D 262 MET MODIFIED RESIDUE
MODRES 5HDF MSE D 301 MET MODIFIED RESIDUE
MODRES 5HDF MSE D 311 MET MODIFIED RESIDUE
HET MSE B 80 8
HET MSE B 98 8
HET MSE B 123 8
HET MSE B 159 8
HET MSE B 262 8
HET MSE B 301 8
HET MSE B 311 8
HET MSE A 80 8
HET MSE A 98 8
HET MSE A 123 8
HET MSE A 159 8
HET MSE A 262 8
HET MSE A 301 8
HET MSE A 311 8
HET MSE C 80 8
HET MSE C 98 8
HET MSE C 123 8
HET MSE C 159 8
HET MSE C 262 8
HET MSE C 301 8
HET MSE C 311 8
HET MSE D 80 8
HET MSE D 98 8
HET MSE D 123 8
HET MSE D 159 8
HET MSE D 262 8
HET MSE D 301 8
HET MSE D 311 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 28(C5 H11 N O2 SE)
FORMUL 5 HOH *52(H2 O)
HELIX 1 AA1 ASN B 105 TRP B 109 5 5
HELIX 2 AA2 GLN B 114 SER B 119 1 6
HELIX 3 AA3 SER B 119 ALA B 127 1 9
HELIX 4 AA4 PRO B 146 LEU B 150 5 5
HELIX 5 AA5 ASN B 151 GLY B 169 1 19
HELIX 6 AA6 SER B 185 HIS B 199 1 15
HELIX 7 AA7 ASN B 214 ASN B 224 1 11
HELIX 8 AA8 SER B 227 ASP B 231 5 5
HELIX 9 AA9 SER B 251 PHE B 256 1 6
HELIX 10 AB1 ASP B 263 THR B 273 1 11
HELIX 11 AB2 THR B 280 ILE B 288 5 9
HELIX 12 AB3 ASP B 289 ALA B 295 1 7
HELIX 13 AB4 SER B 321 ALA B 330 1 10
HELIX 14 AB5 PRO B 331 TRP B 333 5 3
HELIX 15 AB6 GLY B 350 VAL B 354 5 5
HELIX 16 AB7 ASN B 356 VAL B 372 1 17
HELIX 17 AB8 ASN A 105 TRP A 109 5 5
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 SER A 185 HIS A 199 1 15
HELIX 23 AC5 ASN A 214 ASN A 224 1 11
HELIX 24 AC6 SER A 227 ASP A 231 5 5
HELIX 25 AC7 SER A 251 PHE A 256 1 6
HELIX 26 AC8 ASP A 263 THR A 273 1 11
HELIX 27 AC9 THR A 280 ILE A 288 5 9
HELIX 28 AD1 ASP A 289 ALA A 295 1 7
HELIX 29 AD2 SER A 321 ALA A 330 1 10
HELIX 30 AD3 PRO A 331 TRP A 333 5 3
HELIX 31 AD4 GLY A 350 VAL A 354 5 5
HELIX 32 AD5 ASN A 356 VAL A 372 1 17
HELIX 33 AD6 ASN C 105 TRP C 109 5 5
HELIX 34 AD7 GLN C 114 SER C 119 1 6
HELIX 35 AD8 SER C 119 ALA C 127 1 9
HELIX 36 AD9 PRO C 146 LEU C 150 5 5
HELIX 37 AE1 ASN C 151 GLY C 169 1 19
HELIX 38 AE2 SER C 185 HIS C 199 1 15
HELIX 39 AE3 ASN C 214 ASN C 224 1 11
HELIX 40 AE4 SER C 227 ASP C 231 5 5
HELIX 41 AE5 SER C 251 PHE C 256 1 6
HELIX 42 AE6 ASP C 263 THR C 273 1 11
HELIX 43 AE7 THR C 280 ILE C 288 5 9
HELIX 44 AE8 ASP C 289 ALA C 295 1 7
HELIX 45 AE9 SER C 321 ALA C 330 1 10
HELIX 46 AF1 PRO C 331 TRP C 333 5 3
HELIX 47 AF2 GLY C 350 VAL C 354 5 5
HELIX 48 AF3 ASN C 356 VAL C 372 1 17
HELIX 49 AF4 ASN D 105 TRP D 109 5 5
HELIX 50 AF5 GLN D 114 SER D 119 1 6
HELIX 51 AF6 SER D 119 ALA D 127 1 9
HELIX 52 AF7 PRO D 146 LEU D 150 5 5
HELIX 53 AF8 ASN D 151 GLY D 169 1 19
HELIX 54 AF9 SER D 185 HIS D 199 1 15
HELIX 55 AG1 ASN D 214 ASN D 224 1 11
HELIX 56 AG2 SER D 227 ASP D 231 5 5
HELIX 57 AG3 SER D 251 PHE D 256 1 6
HELIX 58 AG4 ASP D 263 THR D 273 1 11
HELIX 59 AG5 THR D 280 ILE D 288 5 9
HELIX 60 AG6 ASP D 289 ALA D 295 1 7
HELIX 61 AG7 SER D 321 ALA D 330 1 10
HELIX 62 AG8 PRO D 331 TRP D 333 5 3
HELIX 63 AG9 GLY D 350 VAL D 354 5 5
HELIX 64 AH1 ASN D 356 VAL D 372 1 17
SHEET 1 AA1 8 ILE B 63 LEU B 73 0
SHEET 2 AA1 8 GLY B 76 ARG B 86 -1 O GLY B 78 N VAL B 71
SHEET 3 AA1 8 ALA B 130 VAL B 134 -1 O VAL B 133 N GLU B 83
SHEET 4 AA1 8 THR B 94 VAL B 99 1 N VAL B 96 O PHE B 132
SHEET 5 AA1 8 LYS B 178 TYR B 184 1 O ALA B 182 N THR B 97
SHEET 6 AA1 8 ALA B 203 THR B 207 1 O LEU B 205 N GLY B 183
SHEET 7 AA1 8 VAL B 300 GLY B 305 1 O MSE B 301 N ILE B 206
SHEET 8 AA1 8 PHE B 339 VAL B 344 1 O VAL B 344 N LEU B 304
SHEET 1 AA2 3 GLY B 225 LEU B 226 0
SHEET 2 AA2 3 TYR B 244 THR B 247 -1 O THR B 246 N LEU B 226
SHEET 3 AA2 3 ASN B 277 VAL B 278 -1 O ASN B 277 N ALA B 245
SHEET 1 AA3 8 ALA A 62 LEU A 73 0
SHEET 2 AA3 8 GLY A 76 PRO A 87 -1 O GLY A 78 N VAL A 71
SHEET 3 AA3 8 ALA A 130 VAL A 134 -1 O THR A 131 N CYS A 85
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 MSE A 301 N ILE A 206
SHEET 8 AA3 8 PHE A 339 VAL A 344 1 O VAL A 344 N LEU A 304
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 C 62 LEU C 73 0
SHEET 2 AA5 8 GLY C 76 PRO C 87 -1 O GLY C 78 N VAL C 71
SHEET 3 AA5 8 ALA C 130 VAL C 134 -1 O VAL C 133 N GLU C 83
SHEET 4 AA5 8 THR C 94 VAL C 99 1 N VAL C 96 O PHE C 132
SHEET 5 AA5 8 LYS C 178 TYR C 184 1 O ALA C 182 N THR C 97
SHEET 6 AA5 8 ALA C 203 THR C 207 1 O LEU C 205 N GLY C 183
SHEET 7 AA5 8 VAL C 300 GLY C 305 1 O MSE C 301 N ILE C 206
SHEET 8 AA5 8 PHE C 339 VAL C 344 1 O VAL C 344 N LEU C 304
SHEET 1 AA6 3 GLY C 225 LEU C 226 0
SHEET 2 AA6 3 TYR C 244 THR C 247 -1 O THR C 246 N LEU C 226
SHEET 3 AA6 3 ASN C 277 VAL C 278 -1 O ASN C 277 N ALA C 245
SHEET 1 AA7 8 ALA D 62 VAL D 71 0
SHEET 2 AA7 8 GLY D 78 PRO D 87 -1 O GLY D 78 N VAL D 71
SHEET 3 AA7 8 ALA D 130 VAL D 134 -1 O VAL D 133 N GLU D 83
SHEET 4 AA7 8 THR D 94 VAL D 99 1 N VAL D 96 O ALA D 130
SHEET 5 AA7 8 LYS D 178 TYR D 184 1 O ALA D 182 N THR D 97
SHEET 6 AA7 8 ALA D 203 THR D 207 1 O LEU D 205 N GLY D 183
SHEET 7 AA7 8 VAL D 300 GLY D 305 1 O MSE D 301 N ILE D 206
SHEET 8 AA7 8 PHE D 339 VAL D 344 1 O VAL D 344 N LEU D 304
SHEET 1 AA8 3 GLY D 225 LEU D 226 0
SHEET 2 AA8 3 TYR D 244 THR D 247 -1 O THR D 246 N LEU D 226
SHEET 3 AA8 3 ASN D 277 VAL D 278 -1 O ASN D 277 N ALA D 245
SSBOND 1 CYS B 64 CYS B 85 1555 1555 2.10
SSBOND 2 CYS B 312 CYS B 319 1555 1555 2.07
SSBOND 3 CYS A 64 CYS A 85 1555 1555 2.12
SSBOND 4 CYS A 312 CYS A 319 1555 1555 2.07
SSBOND 5 CYS C 64 CYS C 85 1555 1555 2.11
SSBOND 6 CYS C 312 CYS C 319 1555 1555 2.06
SSBOND 7 CYS D 64 CYS D 85 1555 1555 2.09
SSBOND 8 CYS D 312 CYS D 319 1555 1555 2.07
LINK C LYS B 79 N MSE B 80 1555 1555 1.32
LINK C MSE B 80 N TRP B 81 1555 1555 1.32
LINK C THR B 97 N MSE B 98 1555 1555 1.33
LINK C MSE B 98 N VAL B 99 1555 1555 1.31
LINK C LYS B 122 N MSE B 123 1555 1555 1.31
LINK C MSE B 123 N LEU B 124 1555 1555 1.33
LINK C GLN B 158 N MSE B 159 1555 1555 1.32
LINK C MSE B 159 N HIS B 160 1555 1555 1.33
LINK C PRO B 261 N MSE B 262 1555 1555 1.34
LINK C MSE B 262 N ASP B 263 1555 1555 1.29
LINK C VAL B 300 N MSE B 301 1555 1555 1.31
LINK C MSE B 301 N PHE B 302 1555 1555 1.31
LINK C LEU B 310 N MSE B 311 1555 1555 1.33
LINK C MSE B 311 N CYS B 312 1555 1555 1.32
LINK C LYS A 79 N MSE A 80 1555 1555 1.32
LINK C MSE A 80 N TRP A 81 1555 1555 1.32
LINK C THR A 97 N MSE A 98 1555 1555 1.32
LINK C MSE A 98 N VAL A 99 1555 1555 1.31
LINK C LYS A 122 N MSE A 123 1555 1555 1.31
LINK C MSE A 123 N LEU A 124 1555 1555 1.33
LINK C GLN A 158 N MSE A 159 1555 1555 1.34
LINK C MSE A 159 N HIS A 160 1555 1555 1.32
LINK C PRO A 261 N MSE A 262 1555 1555 1.34
LINK C MSE A 262 N ASP A 263 1555 1555 1.31
LINK C VAL A 300 N MSE A 301 1555 1555 1.31
LINK C MSE A 301 N PHE A 302 1555 1555 1.32
LINK C LEU A 310 N MSE A 311 1555 1555 1.32
LINK C MSE A 311 N CYS A 312 1555 1555 1.33
LINK C LYS C 79 N MSE C 80 1555 1555 1.32
LINK C MSE C 80 N TRP C 81 1555 1555 1.32
LINK C THR C 97 N MSE C 98 1555 1555 1.32
LINK C MSE C 98 N VAL C 99 1555 1555 1.32
LINK C LYS C 122 N MSE C 123 1555 1555 1.32
LINK C MSE C 123 N LEU C 124 1555 1555 1.33
LINK C GLN C 158 N MSE C 159 1555 1555 1.32
LINK C MSE C 159 N HIS C 160 1555 1555 1.32
LINK C PRO C 261 N MSE C 262 1555 1555 1.35
LINK C MSE C 262 N ASP C 263 1555 1555 1.32
LINK C VAL C 300 N MSE C 301 1555 1555 1.31
LINK C MSE C 301 N PHE C 302 1555 1555 1.32
LINK C LEU C 310 N MSE C 311 1555 1555 1.33
LINK C MSE C 311 N CYS C 312 1555 1555 1.32
LINK C LYS D 79 N MSE D 80 1555 1555 1.32
LINK C MSE D 80 N TRP D 81 1555 1555 1.32
LINK C THR D 97 N MSE D 98 1555 1555 1.33
LINK C MSE D 98 N VAL D 99 1555 1555 1.32
LINK C LYS D 122 N MSE D 123 1555 1555 1.31
LINK C MSE D 123 N LEU D 124 1555 1555 1.32
LINK C GLN D 158 N MSE D 159 1555 1555 1.33
LINK C MSE D 159 N HIS D 160 1555 1555 1.32
LINK C PRO D 261 N MSE D 262 1555 1555 1.34
LINK C MSE D 262 N ASP D 263 1555 1555 1.31
LINK C VAL D 300 N MSE D 301 1555 1555 1.32
LINK C MSE D 301 N PHE D 302 1555 1555 1.32
LINK C LEU D 310 N MSE D 311 1555 1555 1.34
LINK C MSE D 311 N CYS D 312 1555 1555 1.32
CISPEP 1 LYS D 75 GLY D 76 0 -26.76
CISPEP 2 GLY D 76 THR D 77 0 -7.36
CRYST1 178.420 81.970 118.693 90.00 126.75 90.00 C 1 2 1 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 0.005605 0.000000 0.004186 0.00000
SCALE2 0.000000 0.012200 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010515 0.00000
TER 2432 HIS B 380
TER 4817 GLY A 375
TER 7210 LEU C 376
TER 9598 LEU D 376
MASTER 645 0 28 64 44 0 0 6 9646 4 296 120
END |