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HEADER LYASE 20-SEP-16 5TDX
TITLE RESURRECTED ANCESTRAL HYDROXYNITRILE LYASE FROM FLOWERING PLANTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANCESTRAL HYDROXYNITRILE LYASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 4.1.2.47;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS HNL ANCESTRAL HYDROXYNITRILE LYASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.JONES,R.EVANS,C.M.WILMOT,R.J.KAZLAUSKAS
REVDAT 1 11-OCT-17 5TDX 0
JRNL AUTH B.J.JONES,R.EVANS,C.M.WILMOT,R.J.KAZLAUSKAS
JRNL TITL RESURRECTED ANCESTRAL HYDROXYNITRILE LYASE FROM FLOWERING
JRNL TITL 2 PLANTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 81902
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4319
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) : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5496
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 277
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8396
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.152
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.148
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.113
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.339
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8775 ; 0.027 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8226 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11924 ; 2.346 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19050 ; 1.207 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1072 ; 6.539 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 415 ;40.483 ;25.181
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1512 ;15.665 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;14.161 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1301 ; 0.165 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9887 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1963 ; 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): 4234 ; 1.991 ; 2.498
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4233 ; 1.991 ; 2.498
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5306 ; 2.789 ; 3.729
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): 121.6345 83.5720 20.7366
REMARK 3 T TENSOR
REMARK 3 T11: 0.0736 T22: 0.0471
REMARK 3 T33: 0.0097 T12: 0.0513
REMARK 3 T13: -0.0022 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.9679 L22: 1.0754
REMARK 3 L33: 1.1769 L12: -0.5459
REMARK 3 L13: -0.2465 L23: 0.2649
REMARK 3 S TENSOR
REMARK 3 S11: -0.1002 S12: -0.0970 S13: 0.0396
REMARK 3 S21: 0.1305 S22: 0.0513 S23: 0.0421
REMARK 3 S31: 0.0585 S32: 0.1238 S33: 0.0489
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 260
REMARK 3 ORIGIN FOR THE GROUP (A): 111.1017 86.5046 -12.6700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0404 T22: 0.0408
REMARK 3 T33: 0.0372 T12: 0.0150
REMARK 3 T13: -0.0210 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.6682 L22: 0.3592
REMARK 3 L33: 0.9359 L12: -0.0117
REMARK 3 L13: 0.0989 L23: -0.0503
REMARK 3 S TENSOR
REMARK 3 S11: -0.0895 S12: 0.0170 S13: 0.0777
REMARK 3 S21: 0.0039 S22: 0.0345 S23: 0.0510
REMARK 3 S31: -0.0417 S32: -0.0482 S33: 0.0550
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 266
REMARK 3 ORIGIN FOR THE GROUP (A): 139.0448 57.3076 -7.8936
REMARK 3 T TENSOR
REMARK 3 T11: 0.1012 T22: 0.0987
REMARK 3 T33: 0.0061 T12: 0.0949
REMARK 3 T13: -0.0041 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.7356 L22: 0.7736
REMARK 3 L33: 0.8063 L12: 0.0139
REMARK 3 L13: 0.0289 L23: -0.1273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0367 S12: 0.1149 S13: -0.0639
REMARK 3 S21: -0.0115 S22: -0.0195 S23: 0.0143
REMARK 3 S31: 0.1822 S32: 0.1859 S33: -0.0172
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 261
REMARK 3 ORIGIN FOR THE GROUP (A): 153.3627 89.5048 -4.9648
REMARK 3 T TENSOR
REMARK 3 T11: 0.0923 T22: 0.2289
REMARK 3 T33: 0.1925 T12: -0.1022
REMARK 3 T13: -0.1029 T23: 0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 1.1433 L22: 1.7270
REMARK 3 L33: 1.5623 L12: -0.7600
REMARK 3 L13: 0.4309 L23: -0.4117
REMARK 3 S TENSOR
REMARK 3 S11: -0.1543 S12: 0.1197 S13: 0.3618
REMARK 3 S21: 0.2611 S22: -0.0641 S23: -0.4947
REMARK 3 S31: -0.3248 S32: 0.5030 S33: 0.2184
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5TDX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000223506.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86348
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 29.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.68000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.1
REMARK 200 STARTING MODEL: 1YB6
REMARK 200
REMARK 200 REMARK: OCTOHEDRAL, 220 UM POINT TO POINT
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 MIX OF PROTEIN (IN 5MM BES BUFFER)
REMARK 280 WITH MOTHER LIQUOR (1.1 MOLAR AMMONIUM CITRATE, 50 MM BIS-TRIS
REMARK 280 PROPANE, PH 6.8) CRYSTALS FORMED AFTER 2-3 WEEKS AT 20 DEGREES
REMARK 280 C. CRYSTALS WERE CRYO-PROTECTED IN 5% GLYCEROL IN MOTHER LIQUOR
REMARK 280 FOR 10 SECONDS THEN FLASH FROZEN IN LN2., VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 100.59400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.13250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.13250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 150.89100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.13250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.13250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.29700
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.13250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.13250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 150.89100
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.13250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.13250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 50.29700
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 100.59400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 VAL A 262
REMARK 465 ALA A 263
REMARK 465 GLY A 264
REMARK 465 LEU A 265
REMARK 465 GLU A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 HIS A 272
REMARK 465 MET B 1
REMARK 465 ALA B 261
REMARK 465 VAL B 262
REMARK 465 ALA B 263
REMARK 465 GLY B 264
REMARK 465 LEU B 265
REMARK 465 GLU B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 HIS B 272
REMARK 465 MET C 1
REMARK 465 HIS C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 HIS C 271
REMARK 465 HIS C 272
REMARK 465 MET D 1
REMARK 465 VAL D 262
REMARK 465 ALA D 263
REMARK 465 GLY D 264
REMARK 465 LEU D 265
REMARK 465 GLU D 266
REMARK 465 HIS D 267
REMARK 465 HIS D 268
REMARK 465 HIS D 269
REMARK 465 HIS D 270
REMARK 465 HIS D 271
REMARK 465 HIS D 272
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG1 THR B 137 O ASN B 139 7555 2.19
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 TYR A 20 CZ TYR A 20 CE2 -0.081
REMARK 500 TYR A 136 CB TYR A 136 CG 0.103
REMARK 500 GLU A 167 CD GLU A 167 OE1 0.075
REMARK 500 TRP A 217 CE3 TRP A 217 CZ3 0.116
REMARK 500 GLU A 244 CD GLU A 244 OE2 0.076
REMARK 500 GLU B 164 CD GLU B 164 OE1 0.085
REMARK 500 GLU B 167 CD GLU B 167 OE2 0.096
REMARK 500 GLU B 192 CD GLU B 192 OE1 0.072
REMARK 500 PRO B 211 N PRO B 211 CA -0.112
REMARK 500 GLU B 213 CG GLU B 213 CD 0.094
REMARK 500 GLU B 213 CD GLU B 213 OE2 0.087
REMARK 500 GLU B 220 CD GLU B 220 OE2 0.072
REMARK 500 GLU B 244 CD GLU B 244 OE1 0.074
REMARK 500 TYR C 166 CE1 TYR C 166 CZ -0.079
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 55 CB - CG - OD2 ANGL. DEV. = -9.0 DEGREES
REMARK 500 ILE A 86 CB - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 ARG A 174 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 174 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 229 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ASP A 254 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 46 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP B 91 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ILE B 163 N - CA - CB ANGL. DEV. = 14.7 DEGREES
REMARK 500 GLU B 164 OE1 - CD - OE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP B 205 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP B 258 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP C 37 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG C 174 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 186 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 199 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP C 205 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP C 225 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG C 229 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 229 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 MET D 153 CG - SD - CE ANGL. DEV. = 10.4 DEGREES
REMARK 500 ILE D 163 CB - CA - C ANGL. DEV. = -14.1 DEGREES
REMARK 500 ARG D 199 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 CYS A 13 -8.46 78.73
REMARK 500 HIS A 14 -168.00 -109.44
REMARK 500 PRO A 69 154.80 -48.25
REMARK 500 SER A 80 -119.17 42.28
REMARK 500 ASP A 109 -168.80 -124.75
REMARK 500 LYS A 129 -117.32 54.81
REMARK 500 ASP A 234 -160.69 -161.00
REMARK 500 CYS B 13 -2.90 84.96
REMARK 500 HIS B 14 -167.49 -120.98
REMARK 500 SER B 80 -116.87 47.17
REMARK 500 ASN B 104 57.13 31.00
REMARK 500 ASP B 109 -165.18 -129.59
REMARK 500 LYS B 129 -122.43 53.01
REMARK 500 ASN B 139 -119.13 61.77
REMARK 500 TYR B 222 83.13 -153.12
REMARK 500 ASP B 234 -159.70 -162.40
REMARK 500 LYS B 241 48.16 -140.30
REMARK 500 CYS C 13 -1.20 74.26
REMARK 500 HIS C 14 -164.94 -116.43
REMARK 500 ALA C 40 28.50 48.77
REMARK 500 SER C 80 -117.27 50.87
REMARK 500 ASN C 104 62.93 32.48
REMARK 500 SER C 113 154.72 -48.02
REMARK 500 LYS C 129 -124.75 53.32
REMARK 500 TYR C 222 87.16 -151.19
REMARK 500 CYS D 13 -3.41 73.57
REMARK 500 SER D 80 -122.97 52.47
REMARK 500 ASN D 104 51.80 39.67
REMARK 500 ASP D 109 -164.83 -124.04
REMARK 500 LYS D 129 -119.84 54.82
REMARK 500 SER D 138 -124.65 -145.92
REMARK 500 ASP D 234 -165.33 -166.17
REMARK 500 LYS D 236 68.75 -101.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 300
DBREF 5TDX A 1 272 PDB 5TDX 5TDX 1 272
DBREF 5TDX B 1 272 PDB 5TDX 5TDX 1 272
DBREF 5TDX C 1 272 PDB 5TDX 5TDX 1 272
DBREF 5TDX D 1 272 PDB 5TDX 5TDX 1 272
SEQRES 1 A 272 MET ALA THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 A 272 HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU LEU
SEQRES 3 A 272 GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 A 272 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 A 272 THR PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE MET
SEQRES 6 A 272 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 A 272 GLU SER CYS GLY GLY LEU ASN ILE ALA LEU ALA ALA ASP
SEQRES 8 A 272 LYS TYR PRO GLU LYS ILE SER ALA ALA VAL PHE HIS ASN
SEQRES 9 A 272 ALA LEU MET PRO ASP THR GLU HIS SER PRO SER TYR VAL
SEQRES 10 A 272 VAL ASP LYS PHE MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 A 272 THR GLU PHE SER THR TYR THR SER ASN ASN GLU THR ILE
SEQRES 12 A 272 THR GLY MET LYS LEU GLY PHE LYS LEU MET ARG GLU ASN
SEQRES 13 A 272 LEU TYR THR ASN CYS PRO ILE GLU ASP TYR GLU LEU ALA
SEQRES 14 A 272 LYS MET LEU THR ARG LYS GLY SER PHE PHE GLN ASN ASP
SEQRES 15 A 272 LEU ALA GLN ARG PRO LYS PHE THR GLU GLU GLY TYR GLY
SEQRES 16 A 272 SER ILE LYS ARG VAL TYR VAL TRP THR ASP GLU ASP LYS
SEQRES 17 A 272 ILE PHE PRO PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 A 272 TYR LYS PRO ASP LYS VAL TYR ARG VAL GLN GLY GLY ASP
SEQRES 19 A 272 HIS LYS LEU GLN LEU SER LYS THR ASN GLU LEU ALA GLU
SEQRES 20 A 272 ILE LEU GLN GLU VAL ALA ASP THR TYR ALA ASP LEU LEU
SEQRES 21 A 272 ALA VAL ALA GLY LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 272 MET ALA THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 B 272 HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU LEU
SEQRES 3 B 272 GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 B 272 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 B 272 THR PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE MET
SEQRES 6 B 272 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 B 272 GLU SER CYS GLY GLY LEU ASN ILE ALA LEU ALA ALA ASP
SEQRES 8 B 272 LYS TYR PRO GLU LYS ILE SER ALA ALA VAL PHE HIS ASN
SEQRES 9 B 272 ALA LEU MET PRO ASP THR GLU HIS SER PRO SER TYR VAL
SEQRES 10 B 272 VAL ASP LYS PHE MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 B 272 THR GLU PHE SER THR TYR THR SER ASN ASN GLU THR ILE
SEQRES 12 B 272 THR GLY MET LYS LEU GLY PHE LYS LEU MET ARG GLU ASN
SEQRES 13 B 272 LEU TYR THR ASN CYS PRO ILE GLU ASP TYR GLU LEU ALA
SEQRES 14 B 272 LYS MET LEU THR ARG LYS GLY SER PHE PHE GLN ASN ASP
SEQRES 15 B 272 LEU ALA GLN ARG PRO LYS PHE THR GLU GLU GLY TYR GLY
SEQRES 16 B 272 SER ILE LYS ARG VAL TYR VAL TRP THR ASP GLU ASP LYS
SEQRES 17 B 272 ILE PHE PRO PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 B 272 TYR LYS PRO ASP LYS VAL TYR ARG VAL GLN GLY GLY ASP
SEQRES 19 B 272 HIS LYS LEU GLN LEU SER LYS THR ASN GLU LEU ALA GLU
SEQRES 20 B 272 ILE LEU GLN GLU VAL ALA ASP THR TYR ALA ASP LEU LEU
SEQRES 21 B 272 ALA VAL ALA GLY LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 272 MET ALA THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 C 272 HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU LEU
SEQRES 3 C 272 GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 C 272 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 C 272 THR PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE MET
SEQRES 6 C 272 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 C 272 GLU SER CYS GLY GLY LEU ASN ILE ALA LEU ALA ALA ASP
SEQRES 8 C 272 LYS TYR PRO GLU LYS ILE SER ALA ALA VAL PHE HIS ASN
SEQRES 9 C 272 ALA LEU MET PRO ASP THR GLU HIS SER PRO SER TYR VAL
SEQRES 10 C 272 VAL ASP LYS PHE MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 C 272 THR GLU PHE SER THR TYR THR SER ASN ASN GLU THR ILE
SEQRES 12 C 272 THR GLY MET LYS LEU GLY PHE LYS LEU MET ARG GLU ASN
SEQRES 13 C 272 LEU TYR THR ASN CYS PRO ILE GLU ASP TYR GLU LEU ALA
SEQRES 14 C 272 LYS MET LEU THR ARG LYS GLY SER PHE PHE GLN ASN ASP
SEQRES 15 C 272 LEU ALA GLN ARG PRO LYS PHE THR GLU GLU GLY TYR GLY
SEQRES 16 C 272 SER ILE LYS ARG VAL TYR VAL TRP THR ASP GLU ASP LYS
SEQRES 17 C 272 ILE PHE PRO PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 C 272 TYR LYS PRO ASP LYS VAL TYR ARG VAL GLN GLY GLY ASP
SEQRES 19 C 272 HIS LYS LEU GLN LEU SER LYS THR ASN GLU LEU ALA GLU
SEQRES 20 C 272 ILE LEU GLN GLU VAL ALA ASP THR TYR ALA ASP LEU LEU
SEQRES 21 C 272 ALA VAL ALA GLY LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 272 MET ALA THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 D 272 HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU LEU
SEQRES 3 D 272 GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 D 272 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 D 272 THR PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE MET
SEQRES 6 D 272 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 D 272 GLU SER CYS GLY GLY LEU ASN ILE ALA LEU ALA ALA ASP
SEQRES 8 D 272 LYS TYR PRO GLU LYS ILE SER ALA ALA VAL PHE HIS ASN
SEQRES 9 D 272 ALA LEU MET PRO ASP THR GLU HIS SER PRO SER TYR VAL
SEQRES 10 D 272 VAL ASP LYS PHE MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 D 272 THR GLU PHE SER THR TYR THR SER ASN ASN GLU THR ILE
SEQRES 12 D 272 THR GLY MET LYS LEU GLY PHE LYS LEU MET ARG GLU ASN
SEQRES 13 D 272 LEU TYR THR ASN CYS PRO ILE GLU ASP TYR GLU LEU ALA
SEQRES 14 D 272 LYS MET LEU THR ARG LYS GLY SER PHE PHE GLN ASN ASP
SEQRES 15 D 272 LEU ALA GLN ARG PRO LYS PHE THR GLU GLU GLY TYR GLY
SEQRES 16 D 272 SER ILE LYS ARG VAL TYR VAL TRP THR ASP GLU ASP LYS
SEQRES 17 D 272 ILE PHE PRO PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 D 272 TYR LYS PRO ASP LYS VAL TYR ARG VAL GLN GLY GLY ASP
SEQRES 19 D 272 HIS LYS LEU GLN LEU SER LYS THR ASN GLU LEU ALA GLU
SEQRES 20 D 272 ILE LEU GLN GLU VAL ALA ASP THR TYR ALA ASP LEU LEU
SEQRES 21 D 272 ALA VAL ALA GLY LEU GLU HIS HIS HIS HIS HIS HIS
HET GOL A 300 6
HET GOL B 300 6
HET GOL B 301 6
HET GOL C 300 6
HET GOL C 301 6
HET GOL D 300 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 6(C3 H8 O3)
FORMUL 11 HOH *192(H2 O)
HELIX 1 AA1 GLY A 15 TYR A 20 5 6
HELIX 2 AA2 LYS A 21 ALA A 29 1 9
HELIX 3 AA3 GLN A 47 ILE A 51 5 5
HELIX 4 AA4 THR A 53 SER A 58 1 6
HELIX 5 AA5 SER A 58 LEU A 68 1 11
HELIX 6 AA6 CYS A 81 TYR A 93 1 13
HELIX 7 AA7 SER A 115 PHE A 125 1 11
HELIX 8 AA8 GLY A 149 LEU A 157 1 9
HELIX 9 AA9 PRO A 162 THR A 173 1 12
HELIX 10 AB1 PHE A 179 ARG A 186 1 8
HELIX 11 AB2 GLY A 193 ILE A 197 5 5
HELIX 12 AB3 PRO A 211 TYR A 222 1 12
HELIX 13 AB4 LYS A 236 LYS A 241 1 6
HELIX 14 AB5 LYS A 241 ALA A 257 1 17
HELIX 15 AB6 GLY B 15 TYR B 20 5 6
HELIX 16 AB7 LYS B 21 ALA B 29 1 9
HELIX 17 AB8 GLN B 47 ILE B 51 5 5
HELIX 18 AB9 THR B 53 SER B 58 1 6
HELIX 19 AC1 SER B 58 SER B 67 1 10
HELIX 20 AC2 CYS B 81 TYR B 93 1 13
HELIX 21 AC3 SER B 115 PHE B 125 1 11
HELIX 22 AC4 GLY B 149 LEU B 157 1 9
HELIX 23 AC5 PRO B 162 THR B 173 1 12
HELIX 24 AC6 PHE B 179 ARG B 186 1 8
HELIX 25 AC7 GLY B 193 ILE B 197 5 5
HELIX 26 AC8 PRO B 211 TYR B 222 1 12
HELIX 27 AC9 LYS B 236 LYS B 241 1 6
HELIX 28 AD1 LYS B 241 ALA B 257 1 17
HELIX 29 AD2 GLY C 15 TYR C 20 5 6
HELIX 30 AD3 LYS C 21 ALA C 29 1 9
HELIX 31 AD4 GLN C 47 ILE C 51 5 5
HELIX 32 AD5 THR C 53 SER C 58 1 6
HELIX 33 AD6 SER C 58 LEU C 68 1 11
HELIX 34 AD7 CYS C 81 TYR C 93 1 13
HELIX 35 AD8 SER C 115 PHE C 125 1 11
HELIX 36 AD9 GLY C 149 LEU C 157 1 9
HELIX 37 AE1 PRO C 162 THR C 173 1 12
HELIX 38 AE2 PHE C 179 ARG C 186 1 8
HELIX 39 AE3 GLY C 193 ILE C 197 5 5
HELIX 40 AE4 PRO C 211 TYR C 222 1 12
HELIX 41 AE5 LYS C 236 LYS C 241 1 6
HELIX 42 AE6 LYS C 241 TYR C 256 1 16
HELIX 43 AE7 ASP C 258 ALA C 263 1 6
HELIX 44 AE8 GLY D 15 TYR D 20 5 6
HELIX 45 AE9 LYS D 21 ALA D 29 1 9
HELIX 46 AF1 GLN D 47 ILE D 51 5 5
HELIX 47 AF2 THR D 53 SER D 58 1 6
HELIX 48 AF3 SER D 58 LEU D 68 1 11
HELIX 49 AF4 CYS D 81 TYR D 93 1 13
HELIX 50 AF5 SER D 115 PHE D 125 1 11
HELIX 51 AF6 GLY D 149 LEU D 157 1 9
HELIX 52 AF7 PRO D 162 THR D 173 1 12
HELIX 53 AF8 PHE D 179 ARG D 186 1 8
HELIX 54 AF9 GLY D 193 ILE D 197 5 5
HELIX 55 AG1 PRO D 211 TYR D 222 1 12
HELIX 56 AG2 LYS D 236 LYS D 241 1 6
HELIX 57 AG3 LYS D 241 ALA D 257 1 17
SHEET 1 AA1 6 LYS A 32 ALA A 35 0
SHEET 2 AA1 6 HIS A 5 ILE A 9 1 N PHE A 6 O LYS A 32
SHEET 3 AA1 6 VAL A 74 SER A 80 1 O VAL A 77 N ILE A 9
SHEET 4 AA1 6 ILE A 97 ALA A 105 1 O VAL A 101 N LEU A 76
SHEET 5 AA1 6 ARG A 199 TRP A 203 1 O VAL A 202 N PHE A 102
SHEET 6 AA1 6 LYS A 226 ARG A 229 1 O TYR A 228 N TYR A 201
SHEET 1 AA2 2 GLU A 132 THR A 137 0
SHEET 2 AA2 2 THR A 142 LYS A 147 -1 O ILE A 143 N TYR A 136
SHEET 1 AA3 6 LYS B 32 LEU B 36 0
SHEET 2 AA3 6 HIS B 5 ILE B 9 1 N LEU B 8 O THR B 34
SHEET 3 AA3 6 VAL B 74 SER B 80 1 O VAL B 77 N ILE B 9
SHEET 4 AA3 6 ILE B 97 ALA B 105 1 O VAL B 101 N LEU B 76
SHEET 5 AA3 6 ARG B 199 TRP B 203 1 O VAL B 200 N PHE B 102
SHEET 6 AA3 6 LYS B 226 ARG B 229 1 O LYS B 226 N TYR B 201
SHEET 1 AA4 2 GLU B 132 SER B 138 0
SHEET 2 AA4 2 GLU B 141 LYS B 147 -1 O GLU B 141 N SER B 138
SHEET 1 AA5 6 LYS C 32 LEU C 36 0
SHEET 2 AA5 6 HIS C 5 ILE C 9 1 N LEU C 8 O THR C 34
SHEET 3 AA5 6 VAL C 74 SER C 80 1 O VAL C 77 N ILE C 9
SHEET 4 AA5 6 ILE C 97 ALA C 105 1 O VAL C 101 N LEU C 76
SHEET 5 AA5 6 ARG C 199 TRP C 203 1 O VAL C 202 N PHE C 102
SHEET 6 AA5 6 LYS C 226 ARG C 229 1 O LYS C 226 N TYR C 201
SHEET 1 AA6 2 GLU C 132 SER C 138 0
SHEET 2 AA6 2 GLU C 141 LYS C 147 -1 O GLY C 145 N SER C 134
SHEET 1 AA7 6 LYS D 32 LEU D 36 0
SHEET 2 AA7 6 HIS D 5 ILE D 9 1 N PHE D 6 O THR D 34
SHEET 3 AA7 6 VAL D 74 SER D 80 1 O VAL D 77 N ILE D 9
SHEET 4 AA7 6 ILE D 97 ALA D 105 1 O VAL D 101 N LEU D 76
SHEET 5 AA7 6 ARG D 199 TRP D 203 1 O VAL D 202 N PHE D 102
SHEET 6 AA7 6 LYS D 226 ARG D 229 1 O TYR D 228 N TYR D 201
SHEET 1 AA8 2 GLU D 132 THR D 137 0
SHEET 2 AA8 2 THR D 142 LYS D 147 -1 O ILE D 143 N TYR D 136
SITE 1 AC1 5 THR A 11 SER A 80 LEU A 157 HIS A 235
SITE 2 AC1 5 LYS A 236
SITE 1 AC2 6 THR B 11 ILE B 12 SER B 80 LEU B 157
SITE 2 AC2 6 HIS B 235 LYS B 236
SITE 1 AC3 3 ARG B 229 GLN B 231 LYS C 129
SITE 1 AC4 6 THR C 11 SER C 80 LEU C 157 PHE C 178
SITE 2 AC4 6 HIS C 235 LYS C 236
SITE 1 AC5 3 GLU B 155 ARG C 229 GLN C 231
SITE 1 AC6 7 THR D 11 ILE D 12 HIS D 14 SER D 80
SITE 2 AC6 7 LEU D 157 HIS D 235 LYS D 236
CRYST1 108.265 108.265 201.188 90.00 90.00 90.00 P 43 21 2 32
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 0.009237 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009237 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004970 0.00000
TER 2132 ALA A 261
TER 4245 LEU B 260
TER 6384 GLU C 266
TER 8517 ALA D 261
MASTER 563 0 6 57 32 0 10 6 8624 4 36 84
END |