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HEADER HYDROLASE 13-AUG-14 4UBN
TITLE KINETIC CRYSTALLOGRAPHY OF ALPHA_E7-CARBOXYLESTERSE FROM LUCILLA
TITLE 2 CUPRINA - ABSORBED X-RAY DOSE 1.85 MGY TEMP 150K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3;
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: GREEN BOTTLE 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: 562;
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,P.D.CARR,M.WEIK,T.HUBER,T.MEIRELLES,G.CORREY
REVDAT 1 19-AUG-15 4UBN 0
JRNL AUTH C.J.JACKSON,P.D.CARR,M.WEIK,T.HUBER,T.MEIRELLES,G.CORREY
JRNL TITL MAPPING THE ACCESSIBLE CONFORMATIONAL LANDSCAPE OF AN
JRNL TITL 2 ORGANOPHOSPHATE DETOXIFYING INSECT CARBOXYLESTERASE USING
JRNL TITL 3 KINETIC CRYSTALLOGRAPHY AND CONFORMATIONAL ENSEMBLE ANALYSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1639)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 36905
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1871
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 46.1460 - 4.7481 1.00 2871 168 0.1636 0.2054
REMARK 3 2 4.7481 - 3.7693 1.00 2733 160 0.1617 0.2030
REMARK 3 3 3.7693 - 3.2930 1.00 2764 129 0.1882 0.2418
REMARK 3 4 3.2930 - 2.9920 1.00 2720 152 0.2159 0.2467
REMARK 3 5 2.9920 - 2.7775 1.00 2720 147 0.2291 0.2958
REMARK 3 6 2.7775 - 2.6138 1.00 2685 152 0.2208 0.2717
REMARK 3 7 2.6138 - 2.4829 1.00 2696 141 0.2257 0.3190
REMARK 3 8 2.4829 - 2.3748 1.00 2711 133 0.2283 0.3268
REMARK 3 9 2.3748 - 2.2834 1.00 2713 132 0.2316 0.2941
REMARK 3 10 2.2834 - 2.2046 1.00 2670 156 0.2392 0.3190
REMARK 3 11 2.2046 - 2.1357 1.00 2677 126 0.2527 0.3047
REMARK 3 12 2.1357 - 2.0746 0.99 2646 138 0.2772 0.3582
REMARK 3 13 2.0746 - 2.0200 0.91 2428 137 0.3069 0.3824
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.600
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.007 4688
REMARK 3 ANGLE : 1.047 6341
REMARK 3 CHIRALITY : 0.040 677
REMARK 3 PLANARITY : 0.005 817
REMARK 3 DIHEDRAL : 13.717 1759
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 4UBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203149.
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) : 150
REMARK 200 PH : 4.6
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36959
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 46.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.59700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
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: 4QWM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM PEG2000, 0.1M MES, PH 4.6, 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 111.49550
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 111.49550
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 24.65150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.67550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.65150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.67550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 111.49550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.65150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.67550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 111.49550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.65150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.67550
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 TOTAL BURIED SURFACE AREA: 380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 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 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 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 OG SER A 218 O4 DPF A 601 2.04
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 -2.04 74.12
REMARK 500 ASN A 122 65.99 -119.70
REMARK 500 SER A 218 -119.97 58.42
REMARK 500 PHE A 421 -60.17 -132.23
REMARK 500 HIS A 435 52.53 -142.25
REMARK 500 HIS A 471 128.75 -38.88
REMARK 500 THR A 472 -8.92 83.94
REMARK 500 SER A 542 -143.16 -126.16
REMARK 500 HIS A 566 42.39 -151.58
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 DPF A 601
DBREF 4UBN A 1 570 UNP Q25252 Q25252_LUCCU 1 570
SEQADV 4UBN LEU A 364 UNP Q25252 MET 364 ENGINEERED MUTATION
SEQADV 4UBN PHE A 419 UNP Q25252 ILE 419 ENGINEERED MUTATION
SEQADV 4UBN THR A 472 UNP Q25252 ALA 472 ENGINEERED MUTATION
SEQADV 4UBN THR A 505 UNP Q25252 ILE 505 ENGINEERED MUTATION
SEQADV 4UBN GLU A 530 UNP Q25252 LYS 530 ENGINEERED MUTATION
SEQADV 4UBN 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
HET DPF A 601 8
HETNAM DPF DIETHYL HYDROGEN PHOSPHATE
FORMUL 2 DPF C4 H11 O4 P
FORMUL 3 HOH *203(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 HIS A 144 GLY A 149 1 6
HELIX 4 AA4 TYR A 152 LYS A 156 5 5
HELIX 5 AA5 LEU A 167 LEU A 173 1 7
HELIX 6 AA6 SER A 177 ASN A 181 5 5
HELIX 7 AA7 ASN A 185 CYS A 202 1 18
HELIX 8 AA8 ALA A 203 PHE A 205 5 3
HELIX 9 AA9 SER A 218 THR A 230 1 13
HELIX 10 AB1 GLU A 231 ARG A 234 5 4
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 LEU A 293 1 8
HELIX 14 AB5 GLU A 294 VAL A 297 5 4
HELIX 15 AB6 THR A 299 ASN A 305 1 7
HELIX 16 AB7 HIS A 328 LYS A 334 1 7
HELIX 17 AB8 THR A 335 ILE A 341 5 7
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 ALA A 35 0
SHEET 2 AA1 3 LYS A 41 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 43
SHEET 1 AA212 THR A 28 ALA A 35 0
SHEET 2 AA212 LYS A 41 LEU A 48 -1 O GLY A 44 N VAL A 33
SHEET 3 AA212 SER A 54 PRO A 62 -1 O SER A 57 N VAL A 45
SHEET 4 AA212 TYR A 113 THR A 118 -1 O THR A 118 N TYR A 56
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 TYR A 132 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 ARG A 239 N VAL A 214
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 TYR A 442 N MET A 345
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 ILE A 548 N CYS A 538
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
LINK OG SER A 218 P1 DPF A 601 1555 1555 1.48
SITE 1 AC1 10 GLY A 136 GLY A 137 SER A 218 ALA A 219
SITE 2 AC1 10 TRP A 251 MET A 308 PHE A 354 TYR A 457
SITE 3 AC1 10 HIS A 471 THR A 472
CRYST1 49.303 101.351 222.991 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 0.020283 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009867 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004484 0.00000
TER 4565 PHE A 570
MASTER 272 0 1 30 17 0 3 6 4770 1 9 44
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