| content |
HEADER HYDROLASE 03-AUG-18 6EB3
TITLE STRUCTURAL AND ENZYMATIC CHARACTERIZATION OF AN ESTERASE FROM A
TITLE 2 METAGENOMIC LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EST1;
COMPND 3 CHAIN: A, B, C, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318
KEYWDS APHA-BETA HYDROLASE, ESTERASE, METAGENOMIC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.GUZZO,C.F.CARVALHO,R.D.TEIXEIRA,C.S.FARAH
REVDAT 1 07-AUG-19 6EB3 0
JRNL AUTH C.R.GUZZO,N.K.MACIEL,A.S.BARBOSA,C.S.FARAH
JRNL TITL FUNCTIONAL AND STRUCTURAL CHARACTERISATION OF AN ESTERASE
JRNL TITL 2 FROM AMAZONIAN DARK SOIL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 44300
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2268
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3227
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 167
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8189
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 391
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.05000
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): 0.454
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.249
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.186
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.418
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8593 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8194 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11666 ; 1.549 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19006 ; 0.983 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1085 ; 5.721 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 358 ;36.191 ;23.631
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1423 ;15.867 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 53 ;19.278 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1319 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9470 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1683 ; 0.001 ; 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): 4287 ; 1.604 ; 3.510
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4286 ; 1.603 ; 3.510
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5355 ; 2.621 ; 5.256
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5356 ; 2.621 ; 5.256
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4306 ; 1.984 ; 3.871
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4303 ; 1.978 ; 3.866
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6294 ; 3.287 ; 5.667
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9197 ; 5.002 ;41.603
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9142 ; 4.972 ;41.499
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 A 1 268 B 1 268 16248 0.10 0.05
REMARK 3 2 A 1 268 C 1 268 16396 0.09 0.05
REMARK 3 3 A 1 268 D 1 268 16300 0.10 0.05
REMARK 3 4 B 1 268 C 1 268 16372 0.09 0.05
REMARK 3 5 B 1 268 D 1 268 16842 0.09 0.05
REMARK 3 6 C 1 268 D 1 268 16384 0.08 0.05
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 1 A 268
REMARK 3 ORIGIN FOR THE GROUP (A): 54.2395 58.8029 82.5095
REMARK 3 T TENSOR
REMARK 3 T11: 0.0365 T22: 0.1076
REMARK 3 T33: 0.0416 T12: -0.0021
REMARK 3 T13: 0.0140 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 0.8109 L22: 0.1952
REMARK 3 L33: 2.2240 L12: 0.0848
REMARK 3 L13: -0.4747 L23: -0.4994
REMARK 3 S TENSOR
REMARK 3 S11: -0.0840 S12: 0.0874 S13: 0.0631
REMARK 3 S21: 0.0060 S22: 0.1563 S23: -0.0365
REMARK 3 S31: -0.1254 S32: -0.3563 S33: -0.0723
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 1 B 268
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8350 70.8010 136.6948
REMARK 3 T TENSOR
REMARK 3 T11: 0.0321 T22: 0.0434
REMARK 3 T33: 0.0798 T12: 0.0096
REMARK 3 T13: 0.0061 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 0.0342 L22: 0.9139
REMARK 3 L33: 1.7135 L12: -0.1099
REMARK 3 L13: -0.0078 L23: -0.8428
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: -0.0271 S13: -0.0404
REMARK 3 S21: 0.0774 S22: 0.1236 S23: 0.1938
REMARK 3 S31: -0.1464 S32: 0.0260 S33: -0.1431
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 1 C 268
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1081 90.9564 99.4285
REMARK 3 T TENSOR
REMARK 3 T11: 0.0263 T22: 0.0090
REMARK 3 T33: 0.0708 T12: -0.0125
REMARK 3 T13: 0.0080 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.6570 L22: 0.0744
REMARK 3 L33: 0.8378 L12: 0.1599
REMARK 3 L13: 0.2236 L23: 0.1317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0482 S12: 0.0094 S13: 0.0896
REMARK 3 S21: -0.0085 S22: 0.0196 S23: 0.0225
REMARK 3 S31: 0.0397 S32: -0.0011 S33: -0.0679
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 1 D 268
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1863 53.7451 101.2803
REMARK 3 T TENSOR
REMARK 3 T11: 0.0354 T22: 0.0160
REMARK 3 T33: 0.0524 T12: -0.0031
REMARK 3 T13: -0.0069 T23: -0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.5280 L22: 0.4104
REMARK 3 L33: 0.3627 L12: -0.0131
REMARK 3 L13: 0.0813 L23: -0.0396
REMARK 3 S TENSOR
REMARK 3 S11: -0.0522 S12: 0.0100 S13: 0.0178
REMARK 3 S21: 0.0141 S22: 0.0465 S23: 0.0333
REMARK 3 S31: 0.0308 S32: 0.0075 S33: 0.0057
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 6EB3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1000235953.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50655
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2XUA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 BIS-TRIS, PH 6.5, 0.1 M NACL, 1.3
REMARK 280 M (NH4)2SO4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 35.82500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.97000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.97500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.97000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.82500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.97500
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 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: 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: 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: 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: 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 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 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 GLU A 138
REMARK 465 GLY A 139
REMARK 465 ARG A 140
REMARK 465 GLU C 138
REMARK 465 GLY C 139
REMARK 465 ARG C 140
REMARK 465 ALA C 141
REMARK 465 GLY C 142
REMARK 465 LEU C 143
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 LYS A 135 CG CD CE NZ
REMARK 470 LEU A 137 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 55 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 PRO A 128 C - N - CA ANGL. DEV. = -9.3 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 252 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 252 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG C 175 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 175 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG C 252 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG D 55 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG D 55 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG D 252 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG D 252 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG D 265 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG D 265 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 94 -125.33 59.66
REMARK 500 CYS A 118 57.17 30.12
REMARK 500 LEU A 134 53.02 -64.70
REMARK 500 ALA A 136 46.75 -88.68
REMARK 500 SER A 242 53.06 -101.90
REMARK 500 SER B 94 -124.37 60.06
REMARK 500 CYS B 118 57.32 29.93
REMARK 500 SER B 242 54.43 -103.99
REMARK 500 SER C 94 -125.36 59.56
REMARK 500 CYS C 118 57.71 29.80
REMARK 500 SER D 94 -125.30 61.46
REMARK 500 CYS D 118 56.95 30.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 ABU C 301
REMARK 610 ABU D 301
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J3J A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J3G B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ABU C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ABU D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 304
DBREF 6EB3 A 1 268 PDB 6EB3 6EB3 1 268
DBREF 6EB3 B 1 268 PDB 6EB3 6EB3 1 268
DBREF 6EB3 C 1 268 PDB 6EB3 6EB3 1 268
DBREF 6EB3 D 1 268 PDB 6EB3 6EB3 1 268
SEQRES 1 A 268 MET LEU TYR ALA GLN VAL ASN GLY ILE ASN LEU HIS TYR
SEQRES 2 A 268 GLU ILE GLU GLY GLN GLY GLN PRO LEU LEU LEU ILE MET
SEQRES 3 A 268 GLY LEU GLY ALA PRO ALA ALA ALA TRP ASP PRO ILE PHE
SEQRES 4 A 268 VAL GLN THR LEU THR LYS THR HIS GLN VAL ILE ILE TYR
SEQRES 5 A 268 ASP ASN ARG GLY THR GLY LEU SER ASP LYS PRO ASP MET
SEQRES 6 A 268 PRO TYR SER ILE ALA MET PHE ALA SER ASP ALA VAL GLY
SEQRES 7 A 268 LEU LEU ASP ALA LEU ASN ILE PRO ARG ALA HIS VAL PHE
SEQRES 8 A 268 GLY VAL SER MET GLY GLY MET ILE ALA GLN GLU LEU ALA
SEQRES 9 A 268 ILE HIS TYR PRO GLN ARG VAL ALA SER LEU ILE LEU GLY
SEQRES 10 A 268 CYS THR THR PRO GLY GLY LYS HIS ALA VAL PRO ALA PRO
SEQRES 11 A 268 PRO GLU SER LEU LYS ALA LEU GLU GLY ARG ALA GLY LEU
SEQRES 12 A 268 THR PRO GLU GLU ALA ILE ARG GLU GLY TRP LYS LEU SER
SEQRES 13 A 268 PHE SER GLU GLU PHE ILE HIS THR HIS LYS ALA GLU LEU
SEQRES 14 A 268 GLU ALA HIS ILE PRO ARG LEU LEU ALA GLN LEU THR PRO
SEQRES 15 A 268 ARG PHE ALA TYR GLU ARG HIS PHE GLN ALA THR MET THR
SEQRES 16 A 268 LEU ARG VAL PHE LYS GLN LEU LYS GLU ILE GLN ALA PRO
SEQRES 17 A 268 THR LEU VAL ALA THR GLY ARG ASP ASP MET LEU ILE PRO
SEQRES 18 A 268 ALA VAL ASN SER GLU ILE LEU ALA ARG GLU ILE PRO GLY
SEQRES 19 A 268 ALA GLU LEU ALA ILE PHE GLU SER ALA GLY HIS GLY PHE
SEQRES 20 A 268 VAL THR SER ALA ARG GLU PRO PHE LEU LYS VAL LEU LYS
SEQRES 21 A 268 GLU PHE LEU ALA ARG GLN SER VAL
SEQRES 1 B 268 MET LEU TYR ALA GLN VAL ASN GLY ILE ASN LEU HIS TYR
SEQRES 2 B 268 GLU ILE GLU GLY GLN GLY GLN PRO LEU LEU LEU ILE MET
SEQRES 3 B 268 GLY LEU GLY ALA PRO ALA ALA ALA TRP ASP PRO ILE PHE
SEQRES 4 B 268 VAL GLN THR LEU THR LYS THR HIS GLN VAL ILE ILE TYR
SEQRES 5 B 268 ASP ASN ARG GLY THR GLY LEU SER ASP LYS PRO ASP MET
SEQRES 6 B 268 PRO TYR SER ILE ALA MET PHE ALA SER ASP ALA VAL GLY
SEQRES 7 B 268 LEU LEU ASP ALA LEU ASN ILE PRO ARG ALA HIS VAL PHE
SEQRES 8 B 268 GLY VAL SER MET GLY GLY MET ILE ALA GLN GLU LEU ALA
SEQRES 9 B 268 ILE HIS TYR PRO GLN ARG VAL ALA SER LEU ILE LEU GLY
SEQRES 10 B 268 CYS THR THR PRO GLY GLY LYS HIS ALA VAL PRO ALA PRO
SEQRES 11 B 268 PRO GLU SER LEU LYS ALA LEU GLU GLY ARG ALA GLY LEU
SEQRES 12 B 268 THR PRO GLU GLU ALA ILE ARG GLU GLY TRP LYS LEU SER
SEQRES 13 B 268 PHE SER GLU GLU PHE ILE HIS THR HIS LYS ALA GLU LEU
SEQRES 14 B 268 GLU ALA HIS ILE PRO ARG LEU LEU ALA GLN LEU THR PRO
SEQRES 15 B 268 ARG PHE ALA TYR GLU ARG HIS PHE GLN ALA THR MET THR
SEQRES 16 B 268 LEU ARG VAL PHE LYS GLN LEU LYS GLU ILE GLN ALA PRO
SEQRES 17 B 268 THR LEU VAL ALA THR GLY ARG ASP ASP MET LEU ILE PRO
SEQRES 18 B 268 ALA VAL ASN SER GLU ILE LEU ALA ARG GLU ILE PRO GLY
SEQRES 19 B 268 ALA GLU LEU ALA ILE PHE GLU SER ALA GLY HIS GLY PHE
SEQRES 20 B 268 VAL THR SER ALA ARG GLU PRO PHE LEU LYS VAL LEU LYS
SEQRES 21 B 268 GLU PHE LEU ALA ARG GLN SER VAL
SEQRES 1 C 268 MET LEU TYR ALA GLN VAL ASN GLY ILE ASN LEU HIS TYR
SEQRES 2 C 268 GLU ILE GLU GLY GLN GLY GLN PRO LEU LEU LEU ILE MET
SEQRES 3 C 268 GLY LEU GLY ALA PRO ALA ALA ALA TRP ASP PRO ILE PHE
SEQRES 4 C 268 VAL GLN THR LEU THR LYS THR HIS GLN VAL ILE ILE TYR
SEQRES 5 C 268 ASP ASN ARG GLY THR GLY LEU SER ASP LYS PRO ASP MET
SEQRES 6 C 268 PRO TYR SER ILE ALA MET PHE ALA SER ASP ALA VAL GLY
SEQRES 7 C 268 LEU LEU ASP ALA LEU ASN ILE PRO ARG ALA HIS VAL PHE
SEQRES 8 C 268 GLY VAL SER MET GLY GLY MET ILE ALA GLN GLU LEU ALA
SEQRES 9 C 268 ILE HIS TYR PRO GLN ARG VAL ALA SER LEU ILE LEU GLY
SEQRES 10 C 268 CYS THR THR PRO GLY GLY LYS HIS ALA VAL PRO ALA PRO
SEQRES 11 C 268 PRO GLU SER LEU LYS ALA LEU GLU GLY ARG ALA GLY LEU
SEQRES 12 C 268 THR PRO GLU GLU ALA ILE ARG GLU GLY TRP LYS LEU SER
SEQRES 13 C 268 PHE SER GLU GLU PHE ILE HIS THR HIS LYS ALA GLU LEU
SEQRES 14 C 268 GLU ALA HIS ILE PRO ARG LEU LEU ALA GLN LEU THR PRO
SEQRES 15 C 268 ARG PHE ALA TYR GLU ARG HIS PHE GLN ALA THR MET THR
SEQRES 16 C 268 LEU ARG VAL PHE LYS GLN LEU LYS GLU ILE GLN ALA PRO
SEQRES 17 C 268 THR LEU VAL ALA THR GLY ARG ASP ASP MET LEU ILE PRO
SEQRES 18 C 268 ALA VAL ASN SER GLU ILE LEU ALA ARG GLU ILE PRO GLY
SEQRES 19 C 268 ALA GLU LEU ALA ILE PHE GLU SER ALA GLY HIS GLY PHE
SEQRES 20 C 268 VAL THR SER ALA ARG GLU PRO PHE LEU LYS VAL LEU LYS
SEQRES 21 C 268 GLU PHE LEU ALA ARG GLN SER VAL
SEQRES 1 D 268 MET LEU TYR ALA GLN VAL ASN GLY ILE ASN LEU HIS TYR
SEQRES 2 D 268 GLU ILE GLU GLY GLN GLY GLN PRO LEU LEU LEU ILE MET
SEQRES 3 D 268 GLY LEU GLY ALA PRO ALA ALA ALA TRP ASP PRO ILE PHE
SEQRES 4 D 268 VAL GLN THR LEU THR LYS THR HIS GLN VAL ILE ILE TYR
SEQRES 5 D 268 ASP ASN ARG GLY THR GLY LEU SER ASP LYS PRO ASP MET
SEQRES 6 D 268 PRO TYR SER ILE ALA MET PHE ALA SER ASP ALA VAL GLY
SEQRES 7 D 268 LEU LEU ASP ALA LEU ASN ILE PRO ARG ALA HIS VAL PHE
SEQRES 8 D 268 GLY VAL SER MET GLY GLY MET ILE ALA GLN GLU LEU ALA
SEQRES 9 D 268 ILE HIS TYR PRO GLN ARG VAL ALA SER LEU ILE LEU GLY
SEQRES 10 D 268 CYS THR THR PRO GLY GLY LYS HIS ALA VAL PRO ALA PRO
SEQRES 11 D 268 PRO GLU SER LEU LYS ALA LEU GLU GLY ARG ALA GLY LEU
SEQRES 12 D 268 THR PRO GLU GLU ALA ILE ARG GLU GLY TRP LYS LEU SER
SEQRES 13 D 268 PHE SER GLU GLU PHE ILE HIS THR HIS LYS ALA GLU LEU
SEQRES 14 D 268 GLU ALA HIS ILE PRO ARG LEU LEU ALA GLN LEU THR PRO
SEQRES 15 D 268 ARG PHE ALA TYR GLU ARG HIS PHE GLN ALA THR MET THR
SEQRES 16 D 268 LEU ARG VAL PHE LYS GLN LEU LYS GLU ILE GLN ALA PRO
SEQRES 17 D 268 THR LEU VAL ALA THR GLY ARG ASP ASP MET LEU ILE PRO
SEQRES 18 D 268 ALA VAL ASN SER GLU ILE LEU ALA ARG GLU ILE PRO GLY
SEQRES 19 D 268 ALA GLU LEU ALA ILE PHE GLU SER ALA GLY HIS GLY PHE
SEQRES 20 D 268 VAL THR SER ALA ARG GLU PRO PHE LEU LYS VAL LEU LYS
SEQRES 21 D 268 GLU PHE LEU ALA ARG GLN SER VAL
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET J3J A 304 11
HET EDO B 301 4
HET J3G B 302 16
HET PO4 B 303 5
HET ABU C 301 6
HET SO4 C 302 5
HET SO4 C 303 5
HET EDO C 304 4
HET EDO C 305 4
HET ABU D 301 6
HET SO4 D 302 5
HET SO4 D 303 5
HET GOL D 304 6
HETNAM GOL GLYCEROL
HETNAM J3J 1,3-DIHYDROXYPROPAN-2-YL BUTANOATE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM J3G 2-HYDROXYPROPANE-1,3-DIYL DIBUTANOATE
HETNAM PO4 PHOSPHATE ION
HETNAM ABU GAMMA-AMINO-BUTANOIC ACID
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN ABU GAMMA(AMINO)-BUTYRIC ACID
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 8 J3J C7 H14 O4
FORMUL 9 EDO 3(C2 H6 O2)
FORMUL 10 J3G C11 H20 O5
FORMUL 11 PO4 O4 P 3-
FORMUL 12 ABU 2(C4 H9 N O2)
FORMUL 13 SO4 4(O4 S 2-)
FORMUL 21 HOH *391(H2 O)
HELIX 1 AA1 PRO A 31 TRP A 35 5 5
HELIX 2 AA2 ASP A 36 LYS A 45 1 10
HELIX 3 AA3 SER A 68 LEU A 83 1 16
HELIX 4 AA4 SER A 94 TYR A 107 1 14
HELIX 5 AA5 THR A 144 PHE A 157 1 14
HELIX 6 AA6 SER A 158 HIS A 165 1 8
HELIX 7 AA7 HIS A 165 HIS A 172 1 8
HELIX 8 AA8 HIS A 172 ALA A 178 1 7
HELIX 9 AA9 PRO A 182 THR A 193 1 12
HELIX 10 AB1 MET A 194 LEU A 196 5 3
HELIX 11 AB2 VAL A 198 ILE A 205 5 8
HELIX 12 AB3 ALA A 222 ILE A 232 1 11
HELIX 13 AB4 GLY A 246 ALA A 251 1 6
HELIX 14 AB5 ALA A 251 ARG A 265 1 15
HELIX 15 AB6 PRO B 31 TRP B 35 5 5
HELIX 16 AB7 ASP B 36 LYS B 45 1 10
HELIX 17 AB8 SER B 68 LEU B 83 1 16
HELIX 18 AB9 SER B 94 TYR B 107 1 14
HELIX 19 AC1 PRO B 130 ARG B 140 1 11
HELIX 20 AC2 ALA B 141 LEU B 143 5 3
HELIX 21 AC3 THR B 144 PHE B 157 1 14
HELIX 22 AC4 SER B 158 HIS B 165 1 8
HELIX 23 AC5 HIS B 165 HIS B 172 1 8
HELIX 24 AC6 HIS B 172 ALA B 178 1 7
HELIX 25 AC7 PRO B 182 THR B 193 1 12
HELIX 26 AC8 MET B 194 LEU B 196 5 3
HELIX 27 AC9 VAL B 198 ILE B 205 5 8
HELIX 28 AD1 ALA B 222 ILE B 232 1 11
HELIX 29 AD2 GLY B 246 ALA B 251 1 6
HELIX 30 AD3 ALA B 251 ARG B 265 1 15
HELIX 31 AD4 PRO C 31 TRP C 35 5 5
HELIX 32 AD5 ASP C 36 LYS C 45 1 10
HELIX 33 AD6 SER C 68 LEU C 83 1 16
HELIX 34 AD7 SER C 94 TYR C 107 1 14
HELIX 35 AD8 PRO C 130 ALA C 136 1 7
HELIX 36 AD9 PRO C 145 PHE C 157 1 13
HELIX 37 AE1 SER C 158 HIS C 165 1 8
HELIX 38 AE2 HIS C 165 HIS C 172 1 8
HELIX 39 AE3 HIS C 172 ALA C 178 1 7
HELIX 40 AE4 PRO C 182 THR C 193 1 12
HELIX 41 AE5 VAL C 198 ILE C 205 5 8
HELIX 42 AE6 ALA C 222 ILE C 232 1 11
HELIX 43 AE7 GLY C 246 ALA C 251 1 6
HELIX 44 AE8 ALA C 251 ARG C 265 1 15
HELIX 45 AE9 PRO D 31 TRP D 35 5 5
HELIX 46 AF1 ASP D 36 LYS D 45 1 10
HELIX 47 AF2 SER D 68 LEU D 83 1 16
HELIX 48 AF3 SER D 94 TYR D 107 1 14
HELIX 49 AF4 PRO D 130 ARG D 140 1 11
HELIX 50 AF5 ALA D 141 LEU D 143 5 3
HELIX 51 AF6 THR D 144 PHE D 157 1 14
HELIX 52 AF7 SER D 158 HIS D 165 1 8
HELIX 53 AF8 HIS D 165 HIS D 172 1 8
HELIX 54 AF9 HIS D 172 ALA D 178 1 7
HELIX 55 AG1 PRO D 182 THR D 193 1 12
HELIX 56 AG2 VAL D 198 ILE D 205 5 8
HELIX 57 AG3 ALA D 222 ILE D 232 1 11
HELIX 58 AG4 GLY D 246 ALA D 251 1 6
HELIX 59 AG5 ALA D 251 ARG D 265 1 15
SHEET 1 AA1 8 TYR A 3 VAL A 6 0
SHEET 2 AA1 8 ILE A 9 GLU A 16 -1 O ILE A 9 N VAL A 6
SHEET 3 AA1 8 HIS A 47 TYR A 52 -1 O VAL A 49 N GLU A 16
SHEET 4 AA1 8 GLN A 20 ILE A 25 1 N LEU A 22 O ILE A 50
SHEET 5 AA1 8 ALA A 88 VAL A 93 1 O HIS A 89 N LEU A 23
SHEET 6 AA1 8 VAL A 111 GLY A 117 1 O GLY A 117 N GLY A 92
SHEET 7 AA1 8 THR A 209 GLY A 214 1 O ALA A 212 N LEU A 116
SHEET 8 AA1 8 GLU A 236 PHE A 240 1 O GLU A 236 N VAL A 211
SHEET 1 AA2 8 LEU B 2 VAL B 6 0
SHEET 2 AA2 8 ILE B 9 GLU B 16 -1 O ILE B 9 N VAL B 6
SHEET 3 AA2 8 HIS B 47 TYR B 52 -1 O VAL B 49 N GLU B 16
SHEET 4 AA2 8 GLN B 20 ILE B 25 1 N LEU B 22 O ILE B 50
SHEET 5 AA2 8 ALA B 88 VAL B 93 1 O HIS B 89 N LEU B 23
SHEET 6 AA2 8 VAL B 111 GLY B 117 1 O GLY B 117 N GLY B 92
SHEET 7 AA2 8 THR B 209 GLY B 214 1 O ALA B 212 N LEU B 116
SHEET 8 AA2 8 GLU B 236 PHE B 240 1 O GLU B 236 N VAL B 211
SHEET 1 AA3 8 LEU C 2 VAL C 6 0
SHEET 2 AA3 8 ILE C 9 GLU C 16 -1 O ILE C 9 N VAL C 6
SHEET 3 AA3 8 HIS C 47 TYR C 52 -1 O VAL C 49 N GLU C 16
SHEET 4 AA3 8 GLN C 20 ILE C 25 1 N LEU C 22 O ILE C 50
SHEET 5 AA3 8 ALA C 88 VAL C 93 1 O HIS C 89 N LEU C 23
SHEET 6 AA3 8 VAL C 111 GLY C 117 1 O GLY C 117 N GLY C 92
SHEET 7 AA3 8 THR C 209 GLY C 214 1 O ALA C 212 N LEU C 116
SHEET 8 AA3 8 GLU C 236 PHE C 240 1 O GLU C 236 N VAL C 211
SHEET 1 AA4 8 TYR D 3 VAL D 6 0
SHEET 2 AA4 8 ILE D 9 GLU D 16 -1 O ILE D 9 N VAL D 6
SHEET 3 AA4 8 HIS D 47 TYR D 52 -1 O VAL D 49 N GLU D 16
SHEET 4 AA4 8 GLN D 20 ILE D 25 1 N LEU D 22 O ILE D 50
SHEET 5 AA4 8 ALA D 88 VAL D 93 1 O HIS D 89 N LEU D 23
SHEET 6 AA4 8 VAL D 111 GLY D 117 1 O GLY D 117 N GLY D 92
SHEET 7 AA4 8 THR D 209 GLY D 214 1 O ALA D 212 N LEU D 116
SHEET 8 AA4 8 GLU D 236 PHE D 240 1 O GLU D 236 N VAL D 211
SITE 1 AC1 7 LEU A 28 SER A 94 MET A 95 LEU A 134
SITE 2 AC1 7 LEU A 219 ILE A 220 HOH A 449
SITE 1 AC2 4 GLU A 14 GLU A 16 HOH A 421 HOH D 445
SITE 1 AC3 5 SER A 133 MET A 218 HOH A 443 ILE C 239
SITE 2 AC3 5 VAL C 258
SITE 1 AC4 5 ILE A 15 GLY A 17 GLN A 48 HOH A 402
SITE 2 AC4 5 HOH A 425
SITE 1 AC5 1 HIS B 125
SITE 1 AC6 10 SER B 68 ILE B 69 ALA B 70 GLU B 102
SITE 2 AC6 10 HIS B 106 THR B 195 ARG B 197 GLN B 201
SITE 3 AC6 10 HOH B 410 HOH B 483
SITE 1 AC7 2 GLN B 48 ILE D 15
SITE 1 AC8 3 LEU C 28 SER C 94 MET C 95
SITE 1 AC9 2 ARG C 265 GLN C 266
SITE 1 AD1 3 TYR C 107 EDO C 304 HOH C 417
SITE 1 AD2 2 HIS C 106 SO4 C 303
SITE 1 AD3 2 HIS C 172 THR C 249
SITE 1 AD4 5 GLY D 27 LEU D 28 SER D 94 MET D 95
SITE 2 AD4 5 HIS D 245
SITE 1 AD5 3 GLY D 123 LYS D 124 ARG D 197
SITE 1 AD6 3 LYS D 62 HOH D 457 HOH D 461
SITE 1 AD7 6 GLY D 122 PRO D 128 ALA D 129 THR D 193
SITE 2 AD7 6 HOH D 410 HOH D 427
CRYST1 71.650 105.950 145.940 90.00 90.00 90.00 P 21 21 21 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 0.013957 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009438 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006852 0.00000
TER 2061 VAL A 268
TER 4174 VAL B 268
TER 6221 VAL C 268
TER 8304 VAL D 268
MASTER 505 0 16 59 32 0 23 6 8680 4 100 84
END |