| 5c8v-pdb | HEADER HYDROLASE 26-JUN-15 5C8V
TITLE LUCILIA CUPRINA ALPHA ESTERASE 7: GLY137ASP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;
SOURCE 3 ORGANISM_COMMON: GREEN BOTTLE FLY;
SOURCE 4 ORGANISM_TAXID: 7375;
SOURCE 5 GENE: LCAE7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACETYLCHOLINESTERASE, ANIMALS, AUSTRALIA, CARBOXYLESTERASE, CATALYTIC
KEYWDS 2 DOMAIN, DIPTERA, DRUG RESISTANCE, GENES, INSECT, INSECTICIDES,
KEYWDS 3 PHOSPHORYLATION, PROTEIN STRUCTURE, SHEEP, SHEEP DISEASES, SUBSTRATE
KEYWDS 4 SPECIFICITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.J.CORREY,P.D.MABBITT,C.J.JACKSON
REVDAT 1 09-MAR-16 5C8V 0
JRNL AUTH P.D.MABBITT,G.J.CORREY,T.MEIRELLES,N.J.FRASER,M.L.COOTE,
JRNL AUTH 2 C.J.JACKSON
JRNL TITL CONFORMATIONAL DISORGANIZATION WITHIN THE ACTIVE SITE OF A
JRNL TITL 2 RECENTLY EVOLVED ORGANOPHOSPHATE HYDROLASE LIMITS ITS
JRNL TITL 3 CATALYTIC EFFICIENCY.
JRNL REF BIOCHEMISTRY 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 26881849
JRNL DOI 10.1021/ACS.BIOCHEM.5B01322
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 35283
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1867
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2644
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 133
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4561
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 208
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.03000
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): 0.209
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.187
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.929
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4706 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4420 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6373 ; 1.666 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10210 ; 0.877 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 571 ; 6.521 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 223 ;38.369 ;24.305
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 829 ;14.071 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;17.518 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 679 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5315 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1094 ; 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): 2278 ; 1.943 ; 2.537
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2277 ; 1.944 ; 2.537
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2851 ; 2.889 ; 3.797
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2852 ; 2.889 ; 3.797
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2428 ; 2.532 ; 2.830
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2428 ; 2.532 ; 2.830
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3522 ; 3.930 ; 4.125
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5508 ; 5.193 ;20.333
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5447 ; 5.162 ;20.293
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5C8V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0-5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE, AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44051
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 56.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.90600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4FNG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM-ACETATE (PH 4.6) AND 20%
REMARK 280 PEG 2K MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.73800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.73800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 24.83700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.29150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.83700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.29150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 112.73800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.83700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.29150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 112.73800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.83700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.29150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 807 LIES ON A SPECIAL POSITION.
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 ASN A 2
REMARK 465 PHE A 3
REMARK 465 ASN A 4
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 O ALA A 83 ND2 ASN A 523 5545 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 486 NE - CZ - NH1 ANGL. DEV. = 3.4 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 PHE A 73 -1.43 71.53
REMARK 500 ASN A 120 112.02 -162.16
REMARK 500 ASP A 137 28.55 47.72
REMARK 500 SER A 218 -119.75 59.87
REMARK 500 TYR A 350 64.34 -150.48
REMARK 500 PHE A 421 -58.77 -133.72
REMARK 500 SER A 462 54.79 39.32
REMARK 500 THR A 472 -12.30 83.94
REMARK 500 MET A 521 56.05 -112.43
REMARK 500 SER A 542 -142.71 -132.73
REMARK 500 HIS A 566 53.47 -143.22
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5C8V A 1 570 UNP Q25252 Q25252_LUCCU 1 570
SEQADV 5C8V ALA A 83 UNP Q25252 ASP 83 ENGINEERED MUTATION
SEQADV 5C8V ASP A 137 UNP Q25252 GLY 137 ENGINEERED MUTATION
SEQADV 5C8V LEU A 364 UNP Q25252 MET 364 ENGINEERED MUTATION
SEQADV 5C8V PHE A 419 UNP Q25252 ILE 419 ENGINEERED MUTATION
SEQADV 5C8V THR A 472 UNP Q25252 ALA 472 ENGINEERED MUTATION
SEQADV 5C8V THR A 505 UNP Q25252 ILE 505 ENGINEERED MUTATION
SEQADV 5C8V GLU A 530 UNP Q25252 LYS 530 ENGINEERED MUTATION
SEQADV 5C8V GLY A 554 UNP Q25252 ASP 554 ENGINEERED MUTATION
SEQRES 1 A 570 MET ASN PHE ASN VAL SER LEU MET GLU LYS LEU LYS TRP
SEQRES 2 A 570 LYS ILE LYS CYS ILE GLU ASN LYS PHE LEU ASN TYR ARG
SEQRES 3 A 570 LEU THR THR ASN GLU THR VAL VAL ALA GLU THR GLU TYR
SEQRES 4 A 570 GLY LYS VAL LYS GLY VAL LYS ARG LEU THR VAL TYR ASP
SEQRES 5 A 570 ASP SER TYR TYR SER PHE GLU GLY ILE PRO TYR ALA GLN
SEQRES 6 A 570 PRO PRO VAL GLY GLU LEU ARG PHE LYS ALA PRO GLN ARG
SEQRES 7 A 570 PRO THR PRO TRP ALA GLY VAL ARG ASP CYS CYS ASN HIS
SEQRES 8 A 570 LYS ASP LYS SER VAL GLN VAL ASP PHE ILE THR GLY LYS
SEQRES 9 A 570 VAL CYS GLY SER GLU ASP CYS LEU TYR LEU SER VAL TYR
SEQRES 10 A 570 THR ASN ASN LEU ASN PRO GLU THR LYS ARG PRO VAL LEU
SEQRES 11 A 570 VAL TYR ILE HIS GLY GLY ASP PHE ILE ILE GLY GLU ASN
SEQRES 12 A 570 HIS ARG ASP MET TYR GLY PRO ASP TYR PHE ILE LYS LYS
SEQRES 13 A 570 ASP VAL VAL LEU ILE ASN ILE GLN TYR ARG LEU GLY ALA
SEQRES 14 A 570 LEU GLY PHE LEU SER LEU ASN SER GLU ASP LEU ASN VAL
SEQRES 15 A 570 PRO GLY ASN ALA GLY LEU LYS ASP GLN VAL MET ALA LEU
SEQRES 16 A 570 ARG TRP ILE LYS ASN ASN CYS ALA ASN PHE GLY GLY ASN
SEQRES 17 A 570 PRO ASP ASN ILE THR VAL PHE GLY GLU SER ALA GLY ALA
SEQRES 18 A 570 ALA SER THR HIS TYR MET MET LEU THR GLU GLN THR ARG
SEQRES 19 A 570 GLY LEU PHE HIS ARG GLY ILE LEU MET SER GLY ASN ALA
SEQRES 20 A 570 ILE CYS PRO TRP ALA ASN THR GLN CYS GLN HIS ARG ALA
SEQRES 21 A 570 PHE THR LEU ALA LYS LEU ALA GLY TYR LYS GLY GLU ASP
SEQRES 22 A 570 ASN ASP LYS ASP VAL LEU GLU PHE LEU MET LYS ALA LYS
SEQRES 23 A 570 PRO GLN ASP LEU ILE LYS LEU GLU GLU LYS VAL LEU THR
SEQRES 24 A 570 LEU GLU GLU ARG THR ASN LYS VAL MET PHE PRO PHE GLY
SEQRES 25 A 570 PRO THR VAL GLU PRO TYR GLN THR ALA ASP CYS VAL LEU
SEQRES 26 A 570 PRO LYS HIS PRO ARG GLU MET VAL LYS THR ALA TRP GLY
SEQRES 27 A 570 ASN SER ILE PRO THR MET MET GLY ASN THR SER TYR GLU
SEQRES 28 A 570 GLY LEU PHE PHE THR SER ILE LEU LYS GLN MET PRO LEU
SEQRES 29 A 570 LEU VAL LYS GLU LEU GLU THR CYS VAL ASN PHE VAL PRO
SEQRES 30 A 570 SER GLU LEU ALA ASP ALA GLU ARG THR ALA PRO GLU THR
SEQRES 31 A 570 LEU GLU MET GLY ALA LYS ILE LYS LYS ALA HIS VAL THR
SEQRES 32 A 570 GLY GLU THR PRO THR ALA ASP ASN PHE MET ASP LEU CYS
SEQRES 33 A 570 SER HIS PHE TYR PHE TRP PHE PRO MET HIS ARG LEU LEU
SEQRES 34 A 570 GLN LEU ARG PHE ASN HIS THR SER GLY THR PRO VAL TYR
SEQRES 35 A 570 LEU TYR ARG PHE ASP PHE ASP SER GLU ASP LEU ILE ASN
SEQRES 36 A 570 PRO TYR ARG ILE MET ARG SER GLY ARG GLY VAL LYS GLY
SEQRES 37 A 570 VAL SER HIS THR ASP GLU LEU THR TYR PHE PHE TRP ASN
SEQRES 38 A 570 GLN LEU ALA LYS ARG MET PRO LYS GLU SER ARG GLU TYR
SEQRES 39 A 570 LYS THR ILE GLU ARG MET THR GLY ILE TRP THR GLN PHE
SEQRES 40 A 570 ALA THR THR GLY ASN PRO TYR SER ASN GLU ILE GLU GLY
SEQRES 41 A 570 MET GLU ASN VAL SER TRP ASP PRO ILE GLU LYS SER ASP
SEQRES 42 A 570 GLU VAL TYR LYS CYS LEU ASN ILE SER ASP GLU LEU LYS
SEQRES 43 A 570 MET ILE ASP VAL PRO GLU MET GLY LYS ILE LYS GLN TRP
SEQRES 44 A 570 GLU SER MET PHE GLU LYS HIS ARG ASP LEU PHE
FORMUL 2 HOH *208(H2 O)
HELIX 1 AA1 SER A 6 LEU A 27 1 22
HELIX 2 AA2 VAL A 68 ARG A 72 5 5
HELIX 3 AA3 TYR A 152 LYS A 156 5 5
HELIX 4 AA4 LEU A 167 LEU A 173 1 7
HELIX 5 AA5 SER A 177 ASN A 181 5 5
HELIX 6 AA6 ASN A 185 CYS A 202 1 18
HELIX 7 AA7 ALA A 203 PHE A 205 5 3
HELIX 8 AA8 SER A 218 THR A 230 1 13
HELIX 9 AA9 GLU A 231 ARG A 234 5 4
HELIX 10 AB1 CYS A 249 ASN A 253 5 5
HELIX 11 AB2 HIS A 258 ALA A 267 1 10
HELIX 12 AB3 ASN A 274 ALA A 285 1 12
HELIX 13 AB4 LYS A 286 GLU A 294 1 9
HELIX 14 AB5 GLU A 295 VAL A 297 5 3
HELIX 15 AB6 THR A 299 ASN A 305 1 7
HELIX 16 AB7 HIS A 328 THR A 335 1 8
HELIX 17 AB8 ALA A 336 ILE A 341 5 6
HELIX 18 AB9 TYR A 350 PHE A 354 5 5
HELIX 19 AC1 PHE A 355 MET A 362 1 8
HELIX 20 AC2 PRO A 363 THR A 371 5 9
HELIX 21 AC3 CYS A 372 VAL A 376 5 5
HELIX 22 AC4 ALA A 387 VAL A 402 1 16
HELIX 23 AC5 THR A 408 PHE A 421 1 14
HELIX 24 AC6 PHE A 421 ASN A 434 1 14
HELIX 25 AC7 PRO A 456 ARG A 461 1 6
HELIX 26 AC8 THR A 472 PHE A 478 5 7
HELIX 27 AC9 SER A 491 GLY A 511 1 21
HELIX 28 AD1 GLU A 552 SER A 561 1 10
HELIX 29 AD2 MET A 562 GLU A 564 5 3
HELIX 30 AD3 HIS A 566 PHE A 570 5 5
SHEET 1 AA1 3 THR A 28 THR A 37 0
SHEET 2 AA1 3 GLY A 40 LEU A 48 -1 O GLY A 44 N VAL A 33
SHEET 3 AA1 3 VAL A 85 ASP A 87 1 O ARG A 86 N LYS A 41
SHEET 1 AA212 THR A 28 THR A 37 0
SHEET 2 AA212 GLY A 40 LEU A 48 -1 O GLY A 44 N VAL A 33
SHEET 3 AA212 SER A 54 PRO A 62 -1 O TYR A 55 N ARG A 47
SHEET 4 AA212 TYR A 113 THR A 118 -1 O VAL A 116 N PHE A 58
SHEET 5 AA212 VAL A 159 ILE A 163 -1 O LEU A 160 N TYR A 117
SHEET 6 AA212 ARG A 127 ILE A 133 1 N LEU A 130 O ILE A 161
SHEET 7 AA212 GLY A 207 GLU A 217 1 O ASN A 208 N ARG A 127
SHEET 8 AA212 ARG A 239 MET A 243 1 O MET A 243 N GLY A 216
SHEET 9 AA212 THR A 343 THR A 348 1 O MET A 344 N LEU A 242
SHEET 10 AA212 VAL A 441 PHE A 446 1 O PHE A 446 N ASN A 347
SHEET 11 AA212 LYS A 537 ILE A 541 1 O ILE A 541 N ARG A 445
SHEET 12 AA212 LEU A 545 ASP A 549 -1 O LYS A 546 N ASN A 540
SHEET 1 AA3 2 GLN A 97 VAL A 98 0
SHEET 2 AA3 2 VAL A 105 CYS A 106 -1 O CYS A 106 N GLN A 97
CRYST1 49.674 102.583 225.476 90.00 90.00 90.00 C 2 2 21 8
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 0.020131 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009748 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004435 0.00000
TER 4588 PHE A 570
MASTER 336 0 0 30 17 0 0 6 4769 1 0 44
END
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