| content |
HEADER HYDROLASE 27-FEB-24 8S6D
TITLE FUMONISIN B1 ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUMONISIN B1 ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.87;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAULOBACTER SP.;
SOURCE 3 ORGANISM_TAXID: 78;
SOURCE 4 ATCC: 55552;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: PPS-9010;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PD912
KEYWDS MYCOTOXIN, ESTERASE, FUMONISIN B1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.N.NAGY,D.J.INCZE,Z.BATA,Z.MOLNAR,I.LEVELES,B.G.VERTESSY,L.POPPE
REVDAT 1 12-FEB-25 8S6D 0
JRNL AUTH D.J.INCZE,Z.MOLNAR,G.N.NAGY,I.LEVELES,B.G.VERTESSY,L.POPPE,
JRNL AUTH 2 Z.BATA
JRNL TITL UNDERSTANDING THE MOLECULAR MECHANISM OF FUMONISIN ESTERASES
JRNL TITL 2 BY KINETIC AND STRUCTURAL STUDIES.
JRNL REF FOOD CHEM V. 473 43110 2025
JRNL REFN ISSN 0308-8146
JRNL PMID 39892340
JRNL DOI 10.1016/J.FOODCHEM.2025.143110
REMARK 2
REMARK 2 RESOLUTION. 2.24 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 24935
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1232
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 53.1100 - 4.6600 1.00 2896 157 0.1669 0.1636
REMARK 3 2 4.6600 - 3.7000 0.91 2546 115 0.1504 0.1686
REMARK 3 3 3.7000 - 3.2300 0.82 2264 122 0.1810 0.2102
REMARK 3 4 3.2300 - 2.9400 1.00 2723 156 0.1949 0.2329
REMARK 3 5 2.9400 - 2.7300 1.00 2717 139 0.2001 0.2339
REMARK 3 6 2.7300 - 2.5700 1.00 2734 147 0.2009 0.2842
REMARK 3 7 2.5700 - 2.4400 1.00 2710 133 0.1962 0.2431
REMARK 3 8 2.4400 - 2.3300 0.99 2709 140 0.1928 0.2839
REMARK 3 9 2.3300 - 2.2410 0.89 2395 123 0.2129 0.2418
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.51
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 : 0.003 3698
REMARK 3 ANGLE : 0.596 5048
REMARK 3 CHIRALITY : 0.043 533
REMARK 3 PLANARITY : 0.006 682
REMARK 3 DIHEDRAL : 12.688 1324
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 39 THROUGH 273 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8730 20.7203 35.9096
REMARK 3 T TENSOR
REMARK 3 T11: 0.1658 T22: 0.1722
REMARK 3 T33: 0.1650 T12: 0.0124
REMARK 3 T13: -0.0084 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.5466 L22: 0.6247
REMARK 3 L33: 0.6004 L12: -0.0075
REMARK 3 L13: -0.1691 L23: -0.1496
REMARK 3 S TENSOR
REMARK 3 S11: -0.0158 S12: 0.0068 S13: -0.0374
REMARK 3 S21: 0.0504 S22: 0.0174 S23: -0.0056
REMARK 3 S31: 0.0299 S32: 0.0013 S33: -0.0051
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 274 THROUGH 340 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7061 36.6879 31.7164
REMARK 3 T TENSOR
REMARK 3 T11: 0.1911 T22: 0.2048
REMARK 3 T33: 0.1995 T12: 0.0188
REMARK 3 T13: -0.0110 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 0.3178 L22: 0.4840
REMARK 3 L33: 0.8997 L12: 0.1647
REMARK 3 L13: -0.4436 L23: 0.0188
REMARK 3 S TENSOR
REMARK 3 S11: 0.0242 S12: 0.1024 S13: 0.0855
REMARK 3 S21: 0.0224 S22: 0.0662 S23: 0.0571
REMARK 3 S31: -0.1758 S32: -0.0780 S33: -0.0644
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 341 THROUGH 398 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3298 40.3921 6.9836
REMARK 3 T TENSOR
REMARK 3 T11: 0.2205 T22: 0.2318
REMARK 3 T33: 0.2045 T12: 0.0260
REMARK 3 T13: -0.0167 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.5248 L22: 1.5900
REMARK 3 L33: 1.1562 L12: -0.5123
REMARK 3 L13: 0.5492 L23: -0.2708
REMARK 3 S TENSOR
REMARK 3 S11: 0.0956 S12: -0.0154 S13: 0.0590
REMARK 3 S21: -0.1921 S22: -0.0055 S23: 0.2084
REMARK 3 S31: -0.0051 S32: -0.0995 S33: -0.0789
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 399 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5778 19.5385 12.3266
REMARK 3 T TENSOR
REMARK 3 T11: 0.1893 T22: 0.2237
REMARK 3 T33: 0.1672 T12: -0.0024
REMARK 3 T13: -0.0048 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 1.3258 L22: 0.8122
REMARK 3 L33: 0.8290 L12: 0.0338
REMARK 3 L13: 0.1677 L23: 0.2419
REMARK 3 S TENSOR
REMARK 3 S11: -0.0584 S12: 0.2005 S13: -0.0094
REMARK 3 S21: -0.2172 S22: 0.0305 S23: 0.0321
REMARK 3 S31: -0.0052 S32: -0.0848 S33: 0.0113
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 8S6D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-24.
REMARK 100 THE DEPOSITION ID IS D_1292136817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97628
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JUN 30, 2023
REMARK 200 BUILT=20230630
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC 1.0.5 (20230726)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24938
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.241
REMARK 200 RESOLUTION RANGE LOW (A) : 53.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.03757
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25940
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.720
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 W/V % PEG 6000, 100 MM POTASSIUM
REMARK 280 CHLORIDE, 100 MM HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+1/2
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 0.00000
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 0.00000
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 42.65400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.10850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 58.87500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.65400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.10850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 58.87500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.65400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.10850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 58.87500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.65400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.10850
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 58.87500
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 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 872 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 922 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 31
REMARK 465 ALA A 32
REMARK 465 GLY A 33
REMARK 465 ALA A 34
REMARK 465 ALA A 35
REMARK 465 THR A 36
REMARK 465 ALA A 37
REMARK 465 THR A 38
REMARK 465 ASP A 524
REMARK 465 GLY A 525
REMARK 465 ALA A 526
REMARK 465 LYS A 527
REMARK 465 ALA A 528
REMARK 465 GLY A 529
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 ARG A 303 CG CD NE CZ NH1 NH2
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 ALA A 149 47.14 -81.28
REMARK 500 ASN A 173 -150.67 58.01
REMARK 500 SER A 227 -126.60 55.37
REMARK 500 HIS A 315 -64.32 -109.57
REMARK 500 PRO A 332 48.66 -78.93
REMARK 500 PHE A 399 -56.75 -136.94
REMARK 500 THR A 434 -166.64 -106.58
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8S6D A 31 529 PDB 8S6D 8S6D 31 529
SEQRES 1 A 499 MET ALA GLY ALA ALA THR ALA THR ASP PHE PRO VAL ARG
SEQRES 2 A 499 ARG THR ASP LEU GLY GLN VAL GLN GLY LEU ALA GLY ASP
SEQRES 3 A 499 VAL MET SER PHE ARG GLY ILE PRO TYR ALA ALA PRO PRO
SEQRES 4 A 499 VAL GLY GLY LEU ARG TRP LYS PRO PRO GLN HIS ALA ARG
SEQRES 5 A 499 PRO TRP ALA GLY VAL ARG PRO ALA THR GLN PHE GLY SER
SEQRES 6 A 499 ASP CYS PHE GLY ALA ALA TYR LEU ARG LYS GLY SER LEU
SEQRES 7 A 499 ALA PRO GLY VAL SER GLU ASP CYS LEU TYR LEU ASN VAL
SEQRES 8 A 499 TRP ALA PRO SER GLY ALA LYS PRO GLY GLN TYR PRO VAL
SEQRES 9 A 499 MET VAL TRP VAL TYR GLY GLY GLY PHE ALA GLY GLY THR
SEQRES 10 A 499 ALA ALA MET PRO TYR TYR ASP GLY GLU ALA LEU ALA ARG
SEQRES 11 A 499 GLN GLY VAL VAL VAL VAL THR PHE ASN TYR ARG THR ASN
SEQRES 12 A 499 ILE LEU GLY PHE PHE ALA HIS PRO GLY LEU SER ARG GLU
SEQRES 13 A 499 SER PRO THR GLY THR SER GLY ASN TYR GLY LEU LEU ASP
SEQRES 14 A 499 ILE LEU ALA ALA LEU ARG TRP VAL GLN SER ASN ALA ARG
SEQRES 15 A 499 ALA PHE GLY GLY ASP PRO GLY ARG VAL THR VAL PHE GLY
SEQRES 16 A 499 GLU SER ALA GLY ALA SER ALA ILE GLY LEU LEU LEU THR
SEQRES 17 A 499 SER PRO LEU SER LYS GLY LEU PHE ARG GLY ALA ILE LEU
SEQRES 18 A 499 GLU SER PRO GLY LEU THR ARG PRO LEU ALA THR LEU ALA
SEQRES 19 A 499 ASP SER ALA ALA SER GLY GLU ARG LEU ASP ALA ASP LEU
SEQRES 20 A 499 SER ARG LEU ARG SER THR ASP PRO ALA THR LEU MET ALA
SEQRES 21 A 499 ARG ALA ASP ALA ALA ARG PRO ALA SER ARG ASP LEU ARG
SEQRES 22 A 499 ARG PRO ARG PRO THR GLY PRO ILE VAL ASP GLY HIS VAL
SEQRES 23 A 499 LEU PRO GLN THR ASP SER ALA ALA ILE ALA ALA GLY GLN
SEQRES 24 A 499 LEU ALA PRO VAL ARG VAL LEU ILE GLY THR ASN ALA ASP
SEQRES 25 A 499 GLU GLY ARG ALA PHE LEU GLY ARG ALA PRO MET GLU THR
SEQRES 26 A 499 PRO ALA ASP TYR GLN ALA TYR LEU GLU ALA GLN PHE GLY
SEQRES 27 A 499 ASP GLN ALA ALA ALA VAL ALA ALA CYS TYR PRO LEU ASP
SEQRES 28 A 499 GLY ARG ALA THR PRO LYS GLU MET VAL ALA ARG ILE PHE
SEQRES 29 A 499 GLY ASP ASN GLN PHE ASN ARG GLY VAL SER ALA PHE SER
SEQRES 30 A 499 GLU ALA LEU VAL ARG GLN GLY ALA PRO VAL TRP ARG TYR
SEQRES 31 A 499 GLN PHE ASN GLY ASN THR GLU GLY GLY ARG ALA PRO ALA
SEQRES 32 A 499 THR HIS GLY ALA GLU ILE PRO TYR VAL PHE GLY VAL PHE
SEQRES 33 A 499 LYS LEU ASP GLU LEU GLY LEU PHE ASP TRP PRO PRO GLU
SEQRES 34 A 499 GLY PRO THR PRO ALA ASP ARG ALA LEU GLY GLN LEU MET
SEQRES 35 A 499 SER SER ALA TRP VAL ARG PHE ALA LYS ASN GLY ASP PRO
SEQRES 36 A 499 ALA GLY ASP ALA LEU THR TRP PRO ALA TYR SER THR GLY
SEQRES 37 A 499 LYS SER THR MET THR PHE GLY PRO GLU GLY ARG ALA ALA
SEQRES 38 A 499 VAL VAL SER PRO GLY PRO SER ILE PRO PRO CYS ALA ASP
SEQRES 39 A 499 GLY ALA LYS ALA GLY
FORMUL 2 HOH *325(H2 O)
HELIX 1 AA1 VAL A 70 ARG A 74 5 5
HELIX 2 AA2 ALA A 100 ARG A 104 5 5
HELIX 3 AA3 MET A 150 ASP A 154 5 5
HELIX 4 AA4 GLY A 155 ARG A 160 1 6
HELIX 5 AA5 THR A 172 PHE A 177 1 6
HELIX 6 AA6 HIS A 180 SER A 187 1 8
HELIX 7 AA7 ASN A 194 ALA A 211 1 18
HELIX 8 AA8 ARG A 212 PHE A 214 5 3
HELIX 9 AA9 SER A 227 LEU A 237 1 11
HELIX 10 AB1 THR A 238 LYS A 243 5 6
HELIX 11 AB2 THR A 262 ASP A 274 1 13
HELIX 12 AB3 ASP A 276 SER A 282 1 7
HELIX 13 AB4 ASP A 284 ALA A 295 1 12
HELIX 14 AB5 THR A 320 GLY A 328 1 9
HELIX 15 AB6 ASP A 342 LEU A 348 5 7
HELIX 16 AB7 THR A 355 GLY A 368 1 14
HELIX 17 AB8 GLN A 370 TYR A 378 1 9
HELIX 18 AB9 THR A 385 PHE A 399 1 15
HELIX 19 AC1 PHE A 399 GLN A 413 1 15
HELIX 20 AC2 GLU A 438 GLY A 444 1 7
HELIX 21 AC3 THR A 462 GLY A 483 1 22
SHEET 1 AA1 3 VAL A 42 THR A 45 0
SHEET 2 AA1 3 GLY A 48 GLN A 51 -1 O VAL A 50 N ARG A 43
SHEET 3 AA1 3 VAL A 87 PRO A 89 1 O ARG A 88 N GLN A 49
SHEET 1 AA210 VAL A 57 PRO A 64 0
SHEET 2 AA210 TYR A 118 PRO A 124 -1 O LEU A 119 N ILE A 63
SHEET 3 AA210 VAL A 164 PHE A 168 -1 O THR A 167 N ASN A 120
SHEET 4 AA210 TYR A 132 VAL A 138 1 N TRP A 137 O VAL A 166
SHEET 5 AA210 GLY A 216 GLU A 226 1 O THR A 222 N VAL A 134
SHEET 6 AA210 GLY A 248 GLU A 252 1 O GLY A 248 N VAL A 223
SHEET 7 AA210 ARG A 334 ASN A 340 1 O LEU A 336 N LEU A 251
SHEET 8 AA210 VAL A 417 PHE A 422 1 O PHE A 422 N THR A 339
SHEET 9 AA210 THR A 501 PHE A 504 1 O MET A 502 N ARG A 419
SHEET 10 AA210 ALA A 510 VAL A 513 -1 O ALA A 511 N THR A 503
SSBOND 1 CYS A 97 CYS A 116 1555 1555 2.04
SSBOND 2 CYS A 377 CYS A 522 1555 1555 2.03
CISPEP 1 SER A 514 PRO A 515 0 -0.51
CRYST1 85.308 106.217 117.750 90.00 90.00 90.00 I 2 2 2 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 0.011722 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009415 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008493 0.00000
TER 3597 ALA A 523
MASTER 334 0 0 21 13 0 0 6 3921 1 4 39
END |