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HEADER HYDROLASE 28-JUL-25 9W30
TITLE CRYSTAL STRUCTURE OF FERULOYL ESTERASE FROM CLOSTRIDIUM ACETOBUTYLICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA SUPERFAMILY HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: FERULOYL ESTERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACETOBUTYLICUM;
SOURCE 3 ORGANISM_TAXID: 272562;
SOURCE 4 STRAIN: ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC
SOURCE 5 13948 / NRRL B-527 / VKM B-1787 / 2291 / W;
SOURCE 6 GENE: CA_C3665;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS FERULOYL ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.XUE,Y.FENG,S.LI
REVDAT 1 05-AUG-26 9W30 0
JRNL AUTH S.LI,Y.FENG,S.XUE
JRNL TITL UNVEILING ENZYMATIC PLASTICITY OF FERULOYL ESTERASE FROM
JRNL TITL 2 CLOSTRIDIUM ACETOBUTYLICUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 36075
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1851
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 48.9700 - 5.7700 0.96 2590 128 0.1815 0.2584
REMARK 3 2 5.7600 - 4.5800 0.99 2671 140 0.1769 0.2125
REMARK 3 3 4.5800 - 4.0000 1.00 2691 130 0.1635 0.1861
REMARK 3 4 4.0000 - 3.6400 1.00 2662 107 0.1908 0.2844
REMARK 3 5 3.6300 - 3.3700 0.99 2657 161 0.2061 0.2852
REMARK 3 6 3.3700 - 3.1800 0.99 2609 153 0.2333 0.2623
REMARK 3 7 3.1800 - 3.0200 0.99 2639 155 0.2358 0.2701
REMARK 3 8 3.0200 - 2.8900 0.99 2597 153 0.2310 0.2939
REMARK 3 9 2.8900 - 2.7700 0.99 2661 131 0.2321 0.2835
REMARK 3 10 2.7700 - 2.6800 0.99 2653 157 0.2307 0.2592
REMARK 3 11 2.6800 - 2.5900 0.99 2601 169 0.2445 0.2966
REMARK 3 12 2.5900 - 2.5200 0.99 2601 132 0.2445 0.2918
REMARK 3 13 2.5200 - 2.4500 0.97 2592 135 0.2625 0.2864
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.268
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.077
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.73
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 : 0.002 8273
REMARK 3 ANGLE : 0.483 11142
REMARK 3 CHIRALITY : 0.040 1254
REMARK 3 PLANARITY : 0.003 1415
REMARK 3 DIHEDRAL : 4.792 1095
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 9W30 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 01-AUG-25.
REMARK 100 THE DEPOSITION ID IS D_1300062097.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JAN-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 VERSION 723
REMARK 200 DATA SCALING SOFTWARE : HKL-3000 VERSION 723
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36468
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 48.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.12880
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 9.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41070
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.810
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.20.1_4487
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS TRIS, PEG3350, MGCL2, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 106.55800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.27900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 159.83700
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 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 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 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 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 LYS A 258
REMARK 465 PHE A 259
REMARK 465 LYS B 258
REMARK 465 PHE B 259
REMARK 465 LYS C 258
REMARK 465 PHE C 259
REMARK 465 VAL D 257
REMARK 465 LYS D 258
REMARK 465 PHE D 259
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 OD1 ASP B 125 O HOH B 301 1.96
REMARK 500 OE1 GLU D 158 O HOH D 301 1.97
REMARK 500 OD1 ASP B 246 O HOH B 302 2.02
REMARK 500 OE1 GLU D 26 O HOH D 302 2.06
REMARK 500 O LYS D 182 O HOH D 303 2.07
REMARK 500 OE1 GLN D 195 O HOH D 304 2.16
REMARK 500 OE1 GLN A 195 O HOH A 301 2.18
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 LYS A 10 -132.63 54.80
REMARK 500 HIS A 45 43.33 37.74
REMARK 500 SER A 113 -123.76 58.01
REMARK 500 ASN A 141 51.68 -96.81
REMARK 500 TYR A 151 -93.20 -124.51
REMARK 500 ASP A 154 38.10 -84.86
REMARK 500 ASN A 232 -167.12 -79.89
REMARK 500 LYS B 10 -132.52 57.99
REMARK 500 HIS B 45 41.14 39.47
REMARK 500 SER B 113 -122.04 58.37
REMARK 500 ASN B 141 49.08 -94.80
REMARK 500 TYR B 151 -85.66 -131.01
REMARK 500 ASP B 154 34.34 -89.35
REMARK 500 TYR B 156 -78.11 -57.85
REMARK 500 LYS B 194 -162.30 -110.62
REMARK 500 GLU B 236 44.74 -81.87
REMARK 500 LYS C 10 -127.30 57.30
REMARK 500 GLU C 23 101.94 -57.94
REMARK 500 HIS C 45 41.98 39.16
REMARK 500 SER C 113 -119.18 58.42
REMARK 500 ASN C 141 52.66 -96.36
REMARK 500 TYR C 151 -95.47 -130.26
REMARK 500 ASP C 154 44.87 -82.12
REMARK 500 LYS C 194 -162.49 -115.02
REMARK 500 LEU C 256 13.12 -142.59
REMARK 500 LYS D 10 -132.66 53.80
REMARK 500 HIS D 45 43.14 37.73
REMARK 500 ARG D 106 41.71 -140.51
REMARK 500 SER D 113 -120.81 59.03
REMARK 500 ASN D 141 52.98 -97.65
REMARK 500 TYR D 151 -92.38 -123.67
REMARK 500 LYS D 194 -165.60 -112.10
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9W30 A 1 259 UNP Q97D17 Q97D17_CLOAB 7 265
DBREF 9W30 B 1 259 UNP Q97D17 Q97D17_CLOAB 7 265
DBREF 9W30 C 1 259 UNP Q97D17 Q97D17_CLOAB 7 265
DBREF 9W30 D 1 259 UNP Q97D17 Q97D17_CLOAB 7 265
SEQADV 9W30 LYS A 25 UNP Q97D17 ARG 31 CONFLICT
SEQADV 9W30 ILE A 160 UNP Q97D17 MET 166 CONFLICT
SEQADV 9W30 THR A 164 UNP Q97D17 ILE 170 CONFLICT
SEQADV 9W30 GLU A 175 UNP Q97D17 LYS 181 CONFLICT
SEQADV 9W30 LYS B 25 UNP Q97D17 ARG 31 CONFLICT
SEQADV 9W30 ILE B 160 UNP Q97D17 MET 166 CONFLICT
SEQADV 9W30 THR B 164 UNP Q97D17 ILE 170 CONFLICT
SEQADV 9W30 GLU B 175 UNP Q97D17 LYS 181 CONFLICT
SEQADV 9W30 LYS C 25 UNP Q97D17 ARG 31 CONFLICT
SEQADV 9W30 ILE C 160 UNP Q97D17 MET 166 CONFLICT
SEQADV 9W30 THR C 164 UNP Q97D17 ILE 170 CONFLICT
SEQADV 9W30 GLU C 175 UNP Q97D17 LYS 181 CONFLICT
SEQADV 9W30 LYS D 25 UNP Q97D17 ARG 31 CONFLICT
SEQADV 9W30 ILE D 160 UNP Q97D17 MET 166 CONFLICT
SEQADV 9W30 THR D 164 UNP Q97D17 ILE 170 CONFLICT
SEQADV 9W30 GLU D 175 UNP Q97D17 LYS 181 CONFLICT
SEQRES 1 A 259 MET GLN LYS SER VAL GLU ILE LYS SER LYS SER LEU THR
SEQRES 2 A 259 LEU ARG GLY VAL LEU HIS MET PRO LEU GLU ALA LYS GLU
SEQRES 3 A 259 LYS LEU PRO ILE VAL VAL ILE TYR HIS GLY PHE CYS GLY
SEQRES 4 A 259 ASN LYS MET GLY PRO HIS PHE ILE PHE VAL LYS LEU ALA
SEQRES 5 A 259 ARG GLU LEU GLU LYS LEU GLY ILE ALA THR ILE ARG PHE
SEQRES 6 A 259 ASP PHE ALA GLY THR GLY GLU SER ASP GLY GLU PHE VAL
SEQRES 7 A 259 ASP MET THR PHE SER ASN GLU VAL TYR ASP ALA ASN VAL
SEQRES 8 A 259 ILE LEU ASP TYR VAL LYS THR LEU GLU PHE VAL ASP LYS
SEQRES 9 A 259 ASP ARG ILE SER ILE LEU GLY PHE SER MET GLY GLY ALA
SEQRES 10 A 259 ILE ALA SER VAL ILE ALA GLY ASP ARG LYS ASP GLU ILE
SEQRES 11 A 259 ASN THR LEU CYS LEU TRP ALA PRO ALA GLY ASN MET GLU
SEQRES 12 A 259 GLN ILE ILE LEU SER ASP THR TYR ILE GLY ASP LYS TYR
SEQRES 13 A 259 ASP GLU ILE ILE GLU LYS GLY THR TYR ASP VAL GLU GLY
SEQRES 14 A 259 LEU LEU LEU GLY LYS GLU PHE LEU GLU ASP ILE LYS LYS
SEQRES 15 A 259 VAL ASN ILE PHE ASP ARG ALA SER ALA TYR ASN LYS GLN
SEQRES 16 A 259 SER LEU ILE ILE HIS GLY THR SER ASP GLU ILE VAL PRO
SEQRES 17 A 259 LEU SER THR SER GLU ARG TYR LEU GLU MET TYR GLY GLU
SEQRES 18 A 259 ASN THR SER LEU GLU LEU VAL GLU GLY ALA ASN HIS ILE
SEQRES 19 A 259 PHE GLU LYS ASN SER TRP GLU ASN ARG VAL ILE ASP LEU
SEQRES 20 A 259 THR LYS LYS TYR PHE SER GLY LYS LEU VAL LYS PHE
SEQRES 1 B 259 MET GLN LYS SER VAL GLU ILE LYS SER LYS SER LEU THR
SEQRES 2 B 259 LEU ARG GLY VAL LEU HIS MET PRO LEU GLU ALA LYS GLU
SEQRES 3 B 259 LYS LEU PRO ILE VAL VAL ILE TYR HIS GLY PHE CYS GLY
SEQRES 4 B 259 ASN LYS MET GLY PRO HIS PHE ILE PHE VAL LYS LEU ALA
SEQRES 5 B 259 ARG GLU LEU GLU LYS LEU GLY ILE ALA THR ILE ARG PHE
SEQRES 6 B 259 ASP PHE ALA GLY THR GLY GLU SER ASP GLY GLU PHE VAL
SEQRES 7 B 259 ASP MET THR PHE SER ASN GLU VAL TYR ASP ALA ASN VAL
SEQRES 8 B 259 ILE LEU ASP TYR VAL LYS THR LEU GLU PHE VAL ASP LYS
SEQRES 9 B 259 ASP ARG ILE SER ILE LEU GLY PHE SER MET GLY GLY ALA
SEQRES 10 B 259 ILE ALA SER VAL ILE ALA GLY ASP ARG LYS ASP GLU ILE
SEQRES 11 B 259 ASN THR LEU CYS LEU TRP ALA PRO ALA GLY ASN MET GLU
SEQRES 12 B 259 GLN ILE ILE LEU SER ASP THR TYR ILE GLY ASP LYS TYR
SEQRES 13 B 259 ASP GLU ILE ILE GLU LYS GLY THR TYR ASP VAL GLU GLY
SEQRES 14 B 259 LEU LEU LEU GLY LYS GLU PHE LEU GLU ASP ILE LYS LYS
SEQRES 15 B 259 VAL ASN ILE PHE ASP ARG ALA SER ALA TYR ASN LYS GLN
SEQRES 16 B 259 SER LEU ILE ILE HIS GLY THR SER ASP GLU ILE VAL PRO
SEQRES 17 B 259 LEU SER THR SER GLU ARG TYR LEU GLU MET TYR GLY GLU
SEQRES 18 B 259 ASN THR SER LEU GLU LEU VAL GLU GLY ALA ASN HIS ILE
SEQRES 19 B 259 PHE GLU LYS ASN SER TRP GLU ASN ARG VAL ILE ASP LEU
SEQRES 20 B 259 THR LYS LYS TYR PHE SER GLY LYS LEU VAL LYS PHE
SEQRES 1 C 259 MET GLN LYS SER VAL GLU ILE LYS SER LYS SER LEU THR
SEQRES 2 C 259 LEU ARG GLY VAL LEU HIS MET PRO LEU GLU ALA LYS GLU
SEQRES 3 C 259 LYS LEU PRO ILE VAL VAL ILE TYR HIS GLY PHE CYS GLY
SEQRES 4 C 259 ASN LYS MET GLY PRO HIS PHE ILE PHE VAL LYS LEU ALA
SEQRES 5 C 259 ARG GLU LEU GLU LYS LEU GLY ILE ALA THR ILE ARG PHE
SEQRES 6 C 259 ASP PHE ALA GLY THR GLY GLU SER ASP GLY GLU PHE VAL
SEQRES 7 C 259 ASP MET THR PHE SER ASN GLU VAL TYR ASP ALA ASN VAL
SEQRES 8 C 259 ILE LEU ASP TYR VAL LYS THR LEU GLU PHE VAL ASP LYS
SEQRES 9 C 259 ASP ARG ILE SER ILE LEU GLY PHE SER MET GLY GLY ALA
SEQRES 10 C 259 ILE ALA SER VAL ILE ALA GLY ASP ARG LYS ASP GLU ILE
SEQRES 11 C 259 ASN THR LEU CYS LEU TRP ALA PRO ALA GLY ASN MET GLU
SEQRES 12 C 259 GLN ILE ILE LEU SER ASP THR TYR ILE GLY ASP LYS TYR
SEQRES 13 C 259 ASP GLU ILE ILE GLU LYS GLY THR TYR ASP VAL GLU GLY
SEQRES 14 C 259 LEU LEU LEU GLY LYS GLU PHE LEU GLU ASP ILE LYS LYS
SEQRES 15 C 259 VAL ASN ILE PHE ASP ARG ALA SER ALA TYR ASN LYS GLN
SEQRES 16 C 259 SER LEU ILE ILE HIS GLY THR SER ASP GLU ILE VAL PRO
SEQRES 17 C 259 LEU SER THR SER GLU ARG TYR LEU GLU MET TYR GLY GLU
SEQRES 18 C 259 ASN THR SER LEU GLU LEU VAL GLU GLY ALA ASN HIS ILE
SEQRES 19 C 259 PHE GLU LYS ASN SER TRP GLU ASN ARG VAL ILE ASP LEU
SEQRES 20 C 259 THR LYS LYS TYR PHE SER GLY LYS LEU VAL LYS PHE
SEQRES 1 D 259 MET GLN LYS SER VAL GLU ILE LYS SER LYS SER LEU THR
SEQRES 2 D 259 LEU ARG GLY VAL LEU HIS MET PRO LEU GLU ALA LYS GLU
SEQRES 3 D 259 LYS LEU PRO ILE VAL VAL ILE TYR HIS GLY PHE CYS GLY
SEQRES 4 D 259 ASN LYS MET GLY PRO HIS PHE ILE PHE VAL LYS LEU ALA
SEQRES 5 D 259 ARG GLU LEU GLU LYS LEU GLY ILE ALA THR ILE ARG PHE
SEQRES 6 D 259 ASP PHE ALA GLY THR GLY GLU SER ASP GLY GLU PHE VAL
SEQRES 7 D 259 ASP MET THR PHE SER ASN GLU VAL TYR ASP ALA ASN VAL
SEQRES 8 D 259 ILE LEU ASP TYR VAL LYS THR LEU GLU PHE VAL ASP LYS
SEQRES 9 D 259 ASP ARG ILE SER ILE LEU GLY PHE SER MET GLY GLY ALA
SEQRES 10 D 259 ILE ALA SER VAL ILE ALA GLY ASP ARG LYS ASP GLU ILE
SEQRES 11 D 259 ASN THR LEU CYS LEU TRP ALA PRO ALA GLY ASN MET GLU
SEQRES 12 D 259 GLN ILE ILE LEU SER ASP THR TYR ILE GLY ASP LYS TYR
SEQRES 13 D 259 ASP GLU ILE ILE GLU LYS GLY THR TYR ASP VAL GLU GLY
SEQRES 14 D 259 LEU LEU LEU GLY LYS GLU PHE LEU GLU ASP ILE LYS LYS
SEQRES 15 D 259 VAL ASN ILE PHE ASP ARG ALA SER ALA TYR ASN LYS GLN
SEQRES 16 D 259 SER LEU ILE ILE HIS GLY THR SER ASP GLU ILE VAL PRO
SEQRES 17 D 259 LEU SER THR SER GLU ARG TYR LEU GLU MET TYR GLY GLU
SEQRES 18 D 259 ASN THR SER LEU GLU LEU VAL GLU GLY ALA ASN HIS ILE
SEQRES 19 D 259 PHE GLU LYS ASN SER TRP GLU ASN ARG VAL ILE ASP LEU
SEQRES 20 D 259 THR LYS LYS TYR PHE SER GLY LYS LEU VAL LYS PHE
FORMUL 5 HOH *145(H2 O)
HELIX 1 AA1 GLY A 43 HIS A 45 5 3
HELIX 2 AA2 PHE A 46 LYS A 57 1 12
HELIX 3 AA3 GLU A 76 MET A 80 5 5
HELIX 4 AA4 THR A 81 LYS A 97 1 17
HELIX 5 AA5 SER A 113 ARG A 126 1 14
HELIX 6 AA6 LYS A 127 ILE A 130 5 4
HELIX 7 AA7 ASN A 141 SER A 148 1 8
HELIX 8 AA8 LYS A 155 GLY A 163 1 9
HELIX 9 AA9 LYS A 174 VAL A 183 1 10
HELIX 10 AB1 ASN A 184 ALA A 191 1 8
HELIX 11 AB2 PRO A 208 GLY A 220 1 13
HELIX 12 AB3 LYS A 237 SER A 253 1 17
HELIX 13 AB4 GLY B 43 HIS B 45 5 3
HELIX 14 AB5 PHE B 46 LEU B 58 1 13
HELIX 15 AB6 GLU B 76 MET B 80 5 5
HELIX 16 AB7 THR B 81 LYS B 97 1 17
HELIX 17 AB8 SER B 113 ARG B 126 1 14
HELIX 18 AB9 LYS B 127 ILE B 130 5 4
HELIX 19 AC1 ASN B 141 LEU B 147 1 7
HELIX 20 AC2 LYS B 155 GLY B 163 1 9
HELIX 21 AC3 LYS B 174 LYS B 181 1 8
HELIX 22 AC4 ASN B 184 ALA B 191 1 8
HELIX 23 AC5 PRO B 208 GLY B 220 1 13
HELIX 24 AC6 LYS B 237 VAL B 257 1 21
HELIX 25 AC7 GLY C 43 HIS C 45 5 3
HELIX 26 AC8 PHE C 46 LEU C 58 1 13
HELIX 27 AC9 GLU C 76 MET C 80 5 5
HELIX 28 AD1 THR C 81 LYS C 97 1 17
HELIX 29 AD2 SER C 113 ARG C 126 1 14
HELIX 30 AD3 LYS C 127 ILE C 130 5 4
HELIX 31 AD4 ASN C 141 SER C 148 1 8
HELIX 32 AD5 LYS C 155 GLY C 163 1 9
HELIX 33 AD6 LYS C 174 LYS C 181 1 8
HELIX 34 AD7 ASN C 184 ALA C 191 1 8
HELIX 35 AD8 PRO C 208 GLY C 220 1 13
HELIX 36 AD9 LYS C 237 VAL C 257 1 21
HELIX 37 AE1 GLY D 43 HIS D 45 5 3
HELIX 38 AE2 PHE D 46 LYS D 57 1 12
HELIX 39 AE3 GLU D 76 MET D 80 5 5
HELIX 40 AE4 THR D 81 LYS D 97 1 17
HELIX 41 AE5 SER D 113 ARG D 126 1 14
HELIX 42 AE6 LYS D 127 ILE D 130 5 4
HELIX 43 AE7 ASN D 141 SER D 148 1 8
HELIX 44 AE8 ILE D 152 ASP D 154 5 3
HELIX 45 AE9 LYS D 155 GLY D 163 1 9
HELIX 46 AF1 LYS D 174 LYS D 182 1 9
HELIX 47 AF2 ASN D 184 ALA D 191 1 8
HELIX 48 AF3 PRO D 208 GLY D 220 1 13
HELIX 49 AF4 LYS D 237 SER D 253 1 17
SHEET 1 AA1 8 GLN A 2 SER A 9 0
SHEET 2 AA1 8 LEU A 12 HIS A 19 -1 O LEU A 18 N LYS A 3
SHEET 3 AA1 8 ALA A 61 PHE A 65 -1 O THR A 62 N HIS A 19
SHEET 4 AA1 8 LEU A 28 TYR A 34 1 N PRO A 29 O ALA A 61
SHEET 5 AA1 8 VAL A 102 PHE A 112 1 O LEU A 110 N VAL A 32
SHEET 6 AA1 8 LEU A 133 TRP A 136 1 O TRP A 136 N GLY A 111
SHEET 7 AA1 8 SER A 196 GLY A 201 1 O LEU A 197 N LEU A 135
SHEET 8 AA1 8 THR A 223 VAL A 228 1 O GLU A 226 N ILE A 198
SHEET 1 AA2 2 THR A 164 VAL A 167 0
SHEET 2 AA2 2 LEU A 170 GLY A 173 -1 O LEU A 172 N TYR A 165
SHEET 1 AA3 8 GLN B 2 SER B 9 0
SHEET 2 AA3 8 LEU B 12 HIS B 19 -1 O LEU B 14 N ILE B 7
SHEET 3 AA3 8 ALA B 61 PHE B 65 -1 O THR B 62 N HIS B 19
SHEET 4 AA3 8 LEU B 28 TYR B 34 1 N PRO B 29 O ALA B 61
SHEET 5 AA3 8 VAL B 102 PHE B 112 1 O LEU B 110 N VAL B 32
SHEET 6 AA3 8 LEU B 133 TRP B 136 1 O TRP B 136 N GLY B 111
SHEET 7 AA3 8 SER B 196 GLY B 201 1 O LEU B 197 N LEU B 135
SHEET 8 AA3 8 THR B 223 VAL B 228 1 O GLU B 226 N ILE B 198
SHEET 1 AA4 2 THR B 164 VAL B 167 0
SHEET 2 AA4 2 LEU B 170 GLY B 173 -1 O LEU B 172 N TYR B 165
SHEET 1 AA5 8 GLN C 2 SER C 9 0
SHEET 2 AA5 8 LEU C 12 HIS C 19 -1 O LEU C 14 N ILE C 7
SHEET 3 AA5 8 ALA C 61 PHE C 65 -1 O THR C 62 N HIS C 19
SHEET 4 AA5 8 LEU C 28 TYR C 34 1 N PRO C 29 O ALA C 61
SHEET 5 AA5 8 VAL C 102 PHE C 112 1 O SER C 108 N VAL C 32
SHEET 6 AA5 8 LEU C 133 TRP C 136 1 O TRP C 136 N GLY C 111
SHEET 7 AA5 8 SER C 196 GLY C 201 1 O LEU C 197 N LEU C 135
SHEET 8 AA5 8 THR C 223 VAL C 228 1 O GLU C 226 N ILE C 198
SHEET 1 AA6 2 THR C 164 VAL C 167 0
SHEET 2 AA6 2 LEU C 170 GLY C 173 -1 O LEU C 172 N TYR C 165
SHEET 1 AA7 8 GLN D 2 SER D 9 0
SHEET 2 AA7 8 LEU D 12 HIS D 19 -1 O LEU D 14 N ILE D 7
SHEET 3 AA7 8 ALA D 61 PHE D 65 -1 O THR D 62 N HIS D 19
SHEET 4 AA7 8 LEU D 28 TYR D 34 1 N PRO D 29 O ALA D 61
SHEET 5 AA7 8 VAL D 102 PHE D 112 1 O LEU D 110 N VAL D 32
SHEET 6 AA7 8 LEU D 133 TRP D 136 1 O TRP D 136 N GLY D 111
SHEET 7 AA7 8 SER D 196 GLY D 201 1 O LEU D 197 N LEU D 135
SHEET 8 AA7 8 THR D 223 VAL D 228 1 O GLU D 226 N ILE D 198
SHEET 1 AA8 2 THR D 164 VAL D 167 0
SHEET 2 AA8 2 LEU D 170 GLY D 173 -1 O LEU D 172 N TYR D 165
CRYST1 69.260 69.260 213.116 90.00 90.00 90.00 P 41 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 0.014438 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014438 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004692 0.00000
TER 2035 VAL A 257
TER 4070 VAL B 257
TER 6105 VAL C 257
TER 8133 LEU D 256
MASTER 301 0 0 49 40 0 0 6 8274 4 0 80
END |