4FNG-pdb | HEADER HYDROLASE 19-JUN-12 4FNG
TITLE THE ALPHA-ESTERASE-7 CARBOXYLESTERASE, E3, FROM THE BLOWFLY LUCILIA
TITLE 2 CUPRINA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 ALPHA-ESTERASE-7 CABOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;
SOURCE 3 ORGANISM_COMMON: AUSTRALIAN SHEEP BLOWFLY,GREENBOTTLE FLY;
SOURCE 4 ORGANISM_TAXID: 7375;
SOURCE 5 STRAIN: LS2;
SOURCE 6 GENE: LCAE7;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PETMCSIII
KEYWDS ALPHA/BETA HYDROLASE FOLD, CARBOXYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.J.JACKSON,J-W.LIU,P.D.CARR,F.YOUNIS,G.PANDEY,C.COPPIN,T.MEIRELLES,
AUTHOR 2 D.L.OLLIS,D.S.TAWFIK,M.WEIK,J.G.OAKESHOTT
REVDAT 1 19-JUN-13 4FNG 0
JRNL AUTH C.J.JACKSON,J-W.LIU,P.D.CARR,F.YOUNIS,G.PANDEY,C.COPPIN,
JRNL AUTH 2 T.MEIRELLES,D.L.OLLIS,D.S.TAWFIK,M.WEIK,J.G.OAKESHOTT
JRNL TITL THE STRUCTURE AND FUNCTION OF AN INSECT
JRNL TITL 2 ALPHA-CARBOXYLESERASE(ALPHA-ESTERASE7) ASSOCIATED WITH
JRNL TITL 3 INSECTICIDE RESISTANCE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 40150
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2022
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.6870 - 4.6801 1.00 2887 146 0.1602 0.1741
REMARK 3 2 4.6801 - 3.7230 1.00 2780 141 0.1482 0.1808
REMARK 3 3 3.7230 - 3.2548 1.00 2757 148 0.1650 0.2289
REMARK 3 4 3.2548 - 2.9583 1.00 2745 125 0.1794 0.2596
REMARK 3 5 2.9583 - 2.7468 1.00 2739 153 0.1878 0.2325
REMARK 3 6 2.7468 - 2.5853 1.00 2686 157 0.1801 0.2288
REMARK 3 7 2.5853 - 2.4560 1.00 2684 154 0.1903 0.2816
REMARK 3 8 2.4560 - 2.3493 1.00 2705 152 0.1882 0.2319
REMARK 3 9 2.3493 - 2.2590 1.00 2688 166 0.1881 0.2444
REMARK 3 10 2.2590 - 2.1812 1.00 2701 128 0.1909 0.2513
REMARK 3 11 2.1812 - 2.1130 1.00 2676 136 0.1998 0.2458
REMARK 3 12 2.1130 - 2.0527 1.00 2692 149 0.2116 0.2382
REMARK 3 13 2.0527 - 1.9987 1.00 2683 136 0.2329 0.2908
REMARK 3 14 1.9987 - 1.9500 1.00 2705 131 0.2483 0.3260
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 15.52820
REMARK 3 B22 (A**2) : -5.07770
REMARK 3 B33 (A**2) : -10.45050
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 4671
REMARK 3 ANGLE : 1.086 6320
REMARK 3 CHIRALITY : 0.077 675
REMARK 3 PLANARITY : 0.005 815
REMARK 3 DIHEDRAL : 14.420 1747
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FNG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073118.
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 : 4.5
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) : 0.9393
REMARK 200 MONOCHROMATOR : CHANNEL CUT
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43420
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.80900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.150
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: PDB ENTRY 4FG5 (replaced by 5IKX)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM PEGMME 2K PH 4.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 298K
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 110.87000
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 110.87000
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 24.31000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.25500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.31000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.25500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 110.87000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.31000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.25500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 110.87000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.31000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.25500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: 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: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 642 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 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 ASP A 83 CG OD1 OD2
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 O VAL A 376 NH2 ARG A 385 2.19
REMARK 500 O HOH A 845 O HOH A 876 2.19
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 -1.58 73.03
REMARK 500 SER A 218 -121.74 57.42
REMARK 500 PHE A 421 -60.79 -131.76
REMARK 500 HIS A 435 51.68 -152.74
REMARK 500 THR A 472 -13.35 88.33
REMARK 500 SER A 542 -152.43 -139.40
REMARK 500 HIS A 566 52.49 -144.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FG5(5IKX) RELATED DB: PDB
REMARK 900 SAME PROTEIN AT DIFFERENT PH IN DIFFERENT SPACE GROUP
REMARK 900 RELATED ID: 4FNM RELATED DB: PDB
DBREF 4FNG A 1 570 UNP Q25252 Q25252_LUCCU 1 570
SEQADV 4FNG LEU A 364 UNP Q25252 MET 364 ENGINEERED MUTATION
SEQADV 4FNG PHE A 419 UNP Q25252 ILE 419 ENGINEERED MUTATION
SEQADV 4FNG THR A 472 UNP Q25252 ALA 472 ENGINEERED MUTATION
SEQADV 4FNG THR A 505 UNP Q25252 ILE 505 ENGINEERED MUTATION
SEQADV 4FNG GLU A 530 UNP Q25252 LYS 530 ENGINEERED MUTATION
SEQADV 4FNG 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 ASP 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 GLY 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 *282(H2 O)
HELIX 1 1 SER A 6 LEU A 27 1 22
HELIX 2 2 VAL A 68 ARG A 72 5 5
HELIX 3 3 TYR A 152 LYS A 156 5 5
HELIX 4 4 LEU A 167 LEU A 173 1 7
HELIX 5 5 SER A 177 ASN A 181 5 5
HELIX 6 6 ASN A 185 CYS A 202 1 18
HELIX 7 7 ALA A 203 PHE A 205 5 3
HELIX 8 8 SER A 218 THR A 230 1 13
HELIX 9 9 GLU A 231 ARG A 234 5 4
HELIX 10 10 CYS A 249 ASN A 253 5 5
HELIX 11 11 HIS A 258 ALA A 267 1 10
HELIX 12 12 ASN A 274 ALA A 285 1 12
HELIX 13 13 LYS A 286 GLU A 294 1 9
HELIX 14 14 GLU A 295 VAL A 297 5 3
HELIX 15 15 THR A 299 ASN A 305 1 7
HELIX 16 16 HIS A 328 VAL A 333 1 6
HELIX 17 17 LYS A 334 THR A 335 5 2
HELIX 18 18 ALA A 336 ILE A 341 5 6
HELIX 19 19 TYR A 350 PHE A 354 5 5
HELIX 20 20 PHE A 355 MET A 362 1 8
HELIX 21 21 PRO A 363 THR A 371 5 9
HELIX 22 22 CYS A 372 VAL A 376 5 5
HELIX 23 23 ALA A 387 VAL A 402 1 16
HELIX 24 24 THR A 408 PHE A 421 1 14
HELIX 25 25 PHE A 421 ASN A 434 1 14
HELIX 26 26 PRO A 456 ARG A 461 1 6
HELIX 27 27 THR A 472 PHE A 478 5 7
HELIX 28 28 SER A 491 GLY A 511 1 21
HELIX 29 29 GLU A 552 MET A 562 1 11
HELIX 30 30 HIS A 566 PHE A 570 5 5
SHEET 1 A 3 THR A 28 ALA A 35 0
SHEET 2 A 3 LYS A 41 LEU A 48 -1 O VAL A 42 N ALA A 35
SHEET 3 A 3 VAL A 85 ASP A 87 1 O ARG A 86 N LYS A 41
SHEET 1 B12 THR A 28 ALA A 35 0
SHEET 2 B12 LYS A 41 LEU A 48 -1 O VAL A 42 N ALA A 35
SHEET 3 B12 SER A 54 PRO A 62 -1 O TYR A 55 N ARG A 47
SHEET 4 B12 TYR A 113 THR A 118 -1 O THR A 118 N TYR A 56
SHEET 5 B12 VAL A 159 ILE A 163 -1 O LEU A 160 N TYR A 117
SHEET 6 B12 ARG A 127 ILE A 133 1 N LEU A 130 O VAL A 159
SHEET 7 B12 GLY A 207 GLU A 217 1 O THR A 213 N VAL A 129
SHEET 8 B12 ARG A 239 MET A 243 1 O MET A 243 N GLY A 216
SHEET 9 B12 THR A 343 THR A 348 1 O MET A 344 N LEU A 242
SHEET 10 B12 VAL A 441 PHE A 446 1 O PHE A 446 N ASN A 347
SHEET 11 B12 LYS A 537 ILE A 541 1 O ILE A 541 N ARG A 445
SHEET 12 B12 LEU A 545 ASP A 549 -1 O LYS A 546 N ASN A 540
SHEET 1 C 2 GLN A 97 VAL A 98 0
SHEET 2 C 2 VAL A 105 CYS A 106 -1 O CYS A 106 N GLN A 97
CRYST1 48.620 100.510 221.740 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 0.020568 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009949 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004510 0.00000
TER 4557 PHE A 570
MASTER 297 0 0 30 17 0 0 6 4838 1 0 44
END
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