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HEADER HYDROLASE 25-JUL-24 9IW9
TITLE CRYSTAL STRUCTURE OF KBPETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KBPETASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KIBDELOSPORANGIUM BANGUIENSE;
SOURCE 3 ORGANISM_TAXID: 1365924;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PETASE, S9 FAMILY PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.H.WU
REVDAT 1 30-JUL-25 9IW9 0
JRNL AUTH B.WU,B.ZHONG,L.ZHENG,R.HUANG,S.JIANG,M.LI,L.HONG,P.TAN
JRNL TITL HARNESSING PROTEIN LANGUAGE MODEL FOR STRUCTURE-BASED
JRNL TITL 2 DISCOVERY OF HIGHLY EFFICIENT AND ROBUST PET HYDROLASES.
JRNL REF NAT COMMUN V. 16 6211 2025
JRNL REFN ESSN 2041-1723
JRNL PMID 40617831
JRNL DOI 10.1038/S41467-025-61599-Z
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.1_3865
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 3 NUMBER OF REFLECTIONS : 164893
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1785
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 31.3300 - 4.1100 0.90 12352 141 0.1322 0.1316
REMARK 3 2 4.1100 - 3.2600 0.89 12236 131 0.1403 0.1608
REMARK 3 3 3.2600 - 2.8500 0.91 12474 141 0.1680 0.2270
REMARK 3 4 2.8500 - 2.5900 0.93 12821 172 0.1592 0.1879
REMARK 3 5 2.5900 - 2.4100 0.94 12912 152 0.1554 0.1799
REMARK 3 6 2.4100 - 2.2600 0.91 12503 140 0.1569 0.1773
REMARK 3 7 2.2600 - 2.1500 0.93 12751 148 0.1650 0.1495
REMARK 3 8 2.1500 - 2.0600 0.93 13020 129 0.1710 0.1815
REMARK 3 9 2.0600 - 1.9800 0.91 12459 150 0.1862 0.1800
REMARK 3 10 1.9800 - 1.9100 0.88 12101 148 0.2053 0.2349
REMARK 3 11 1.9100 - 1.8500 0.91 12532 133 0.2212 0.2280
REMARK 3 12 1.8500 - 1.8000 0.90 12387 161 0.2489 0.2891
REMARK 3 13 1.8000 - 1.7500 0.90 12467 132 0.2663 0.3014
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) : 0.187
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.942
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.82
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 : 0.014 7705
REMARK 3 ANGLE : 1.598 10526
REMARK 3 CHIRALITY : 0.085 1115
REMARK 3 PLANARITY : 0.010 1398
REMARK 3 DIHEDRAL : 13.739 2590
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 9IW9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 30-JUL-24.
REMARK 100 THE DEPOSITION ID IS D_1300049815.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5-7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL02U1
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 EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 164893
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 31.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.06559
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54430
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.540
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28-34% POLYETHYLENE GLYCOL 3000, 0.1 M
REMARK 280 HEPES, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 52.39900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 PHE C 3
REMARK 465 ALA C 4
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 PHE D 3
REMARK 465 ALA D 4
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 CYS A 239 N CA C O CB SG
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 HOH B 401 O HOH B 466 2.10
REMARK 500 OG SER A 27 O HOH A 301 2.12
REMARK 500 OD2 ASP D 245 O HOH D 301 2.13
REMARK 500 O HOH A 308 O HOH A 426 2.15
REMARK 500 O HOH C 417 O HOH D 450 2.16
REMARK 500 O HOH C 312 O HOH C 472 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 HOH A 331 O HOH D 453 1655 2.17
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 SER A 108 -21.84 -141.78
REMARK 500 SER A 128 -124.95 65.59
REMARK 500 HIS A 184 -84.55 -117.81
REMARK 500 SER B 128 -125.09 65.20
REMARK 500 ALA B 179 62.42 -119.96
REMARK 500 HIS B 184 -85.23 -120.08
REMARK 500 SER C 128 -125.27 65.57
REMARK 500 HIS C 184 -79.85 -125.55
REMARK 500 SER D 108 -25.21 -143.66
REMARK 500 SER D 128 -122.07 67.70
REMARK 500 HIS D 184 -86.19 -129.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 492 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH C 519 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH C 520 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH C 521 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH D 518 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH D 519 DISTANCE = 6.74 ANGSTROMS
DBREF 9IW9 A 1 254 PDB 9IW9 9IW9 1 254
DBREF 9IW9 B 1 254 PDB 9IW9 9IW9 1 254
DBREF 9IW9 C 1 254 PDB 9IW9 9IW9 1 254
DBREF 9IW9 D 1 254 PDB 9IW9 9IW9 1 254
SEQRES 1 A 254 MET ALA PHE ALA ASP GLU ILE GLY GLN ALA PRO THR ALA
SEQRES 2 A 254 ALA ASN ILE THR GLY ASP GLY SER PHE SER THR SER SER
SEQRES 3 A 254 SER ALA ILE PHE GLY GLN SER GLY PHE GLY GLY GLY THR
SEQRES 4 A 254 ALA TYR TYR PRO ASN THR ALA GLY LYS TYR PRO VAL VAL
SEQRES 5 A 254 ALA PHE ALA PRO GLY PHE LEU SER ASP TRP ASN ALA LEU
SEQRES 6 A 254 ASN TRP LEU GLY PRO ARG VAL ALA SER TRP GLY PHE VAL
SEQRES 7 A 254 VAL VAL GLY VAL ASN THR ASN THR PRO PHE ASP PHE PRO
SEQRES 8 A 254 ASP ALA ARG GLY ASP GLN LEU LEU ALA ALA LEU ASN TRP
SEQRES 9 A 254 ALA VAL ASN SER ALA PRO ALA ALA VAL ARG ASP LYS ALA
SEQRES 10 A 254 ASP GLY SER ARG ARG GLY VAL SER GLY TRP SER MET GLY
SEQRES 11 A 254 GLY GLY GLY THR LEU GLU ALA LEU ALA LYS ASP THR THR
SEQRES 12 A 254 GLY THR VAL LYS ALA GLY VAL PRO LEU ALA PRO TRP HIS
SEQRES 13 A 254 THR ASN LYS THR TRP SER LYS VAL THR GLU PRO VAL PHE
SEQRES 14 A 254 ILE ILE GLY GLY GLN ASN ASP SER VAL ALA ALA PRO ALA
SEQRES 15 A 254 SER HIS ALA ILE PRO PHE TYR ASN SER LEU GLY GLY PRO
SEQRES 16 A 254 LYS SER TYR LEU GLU ARG ALA GLY ALA ASP HIS PHE PHE
SEQRES 17 A 254 PRO THR LYS SER ASN GLY THR VAL SER ARG ALA VAL VAL
SEQRES 18 A 254 SER PHE PHE LYS ARG HIS VAL SER ALA ASP THR ARG PHE
SEQRES 19 A 254 THR PRO PHE LEU CYS GLY PHE SER GLY LEU ASP VAL SER
SEQRES 20 A 254 ASN PHE ARG SER ASN SER CYS
SEQRES 1 B 254 MET ALA PHE ALA ASP GLU ILE GLY GLN ALA PRO THR ALA
SEQRES 2 B 254 ALA ASN ILE THR GLY ASP GLY SER PHE SER THR SER SER
SEQRES 3 B 254 SER ALA ILE PHE GLY GLN SER GLY PHE GLY GLY GLY THR
SEQRES 4 B 254 ALA TYR TYR PRO ASN THR ALA GLY LYS TYR PRO VAL VAL
SEQRES 5 B 254 ALA PHE ALA PRO GLY PHE LEU SER ASP TRP ASN ALA LEU
SEQRES 6 B 254 ASN TRP LEU GLY PRO ARG VAL ALA SER TRP GLY PHE VAL
SEQRES 7 B 254 VAL VAL GLY VAL ASN THR ASN THR PRO PHE ASP PHE PRO
SEQRES 8 B 254 ASP ALA ARG GLY ASP GLN LEU LEU ALA ALA LEU ASN TRP
SEQRES 9 B 254 ALA VAL ASN SER ALA PRO ALA ALA VAL ARG ASP LYS ALA
SEQRES 10 B 254 ASP GLY SER ARG ARG GLY VAL SER GLY TRP SER MET GLY
SEQRES 11 B 254 GLY GLY GLY THR LEU GLU ALA LEU ALA LYS ASP THR THR
SEQRES 12 B 254 GLY THR VAL LYS ALA GLY VAL PRO LEU ALA PRO TRP HIS
SEQRES 13 B 254 THR ASN LYS THR TRP SER LYS VAL THR GLU PRO VAL PHE
SEQRES 14 B 254 ILE ILE GLY GLY GLN ASN ASP SER VAL ALA ALA PRO ALA
SEQRES 15 B 254 SER HIS ALA ILE PRO PHE TYR ASN SER LEU GLY GLY PRO
SEQRES 16 B 254 LYS SER TYR LEU GLU ARG ALA GLY ALA ASP HIS PHE PHE
SEQRES 17 B 254 PRO THR LYS SER ASN GLY THR VAL SER ARG ALA VAL VAL
SEQRES 18 B 254 SER PHE PHE LYS ARG HIS VAL SER ALA ASP THR ARG PHE
SEQRES 19 B 254 THR PRO PHE LEU CYS GLY PHE SER GLY LEU ASP VAL SER
SEQRES 20 B 254 ASN PHE ARG SER ASN SER CYS
SEQRES 1 C 254 MET ALA PHE ALA ASP GLU ILE GLY GLN ALA PRO THR ALA
SEQRES 2 C 254 ALA ASN ILE THR GLY ASP GLY SER PHE SER THR SER SER
SEQRES 3 C 254 SER ALA ILE PHE GLY GLN SER GLY PHE GLY GLY GLY THR
SEQRES 4 C 254 ALA TYR TYR PRO ASN THR ALA GLY LYS TYR PRO VAL VAL
SEQRES 5 C 254 ALA PHE ALA PRO GLY PHE LEU SER ASP TRP ASN ALA LEU
SEQRES 6 C 254 ASN TRP LEU GLY PRO ARG VAL ALA SER TRP GLY PHE VAL
SEQRES 7 C 254 VAL VAL GLY VAL ASN THR ASN THR PRO PHE ASP PHE PRO
SEQRES 8 C 254 ASP ALA ARG GLY ASP GLN LEU LEU ALA ALA LEU ASN TRP
SEQRES 9 C 254 ALA VAL ASN SER ALA PRO ALA ALA VAL ARG ASP LYS ALA
SEQRES 10 C 254 ASP GLY SER ARG ARG GLY VAL SER GLY TRP SER MET GLY
SEQRES 11 C 254 GLY GLY GLY THR LEU GLU ALA LEU ALA LYS ASP THR THR
SEQRES 12 C 254 GLY THR VAL LYS ALA GLY VAL PRO LEU ALA PRO TRP HIS
SEQRES 13 C 254 THR ASN LYS THR TRP SER LYS VAL THR GLU PRO VAL PHE
SEQRES 14 C 254 ILE ILE GLY GLY GLN ASN ASP SER VAL ALA ALA PRO ALA
SEQRES 15 C 254 SER HIS ALA ILE PRO PHE TYR ASN SER LEU GLY GLY PRO
SEQRES 16 C 254 LYS SER TYR LEU GLU ARG ALA GLY ALA ASP HIS PHE PHE
SEQRES 17 C 254 PRO THR LYS SER ASN GLY THR VAL SER ARG ALA VAL VAL
SEQRES 18 C 254 SER PHE PHE LYS ARG HIS VAL SER ALA ASP THR ARG PHE
SEQRES 19 C 254 THR PRO PHE LEU CYS GLY PHE SER GLY LEU ASP VAL SER
SEQRES 20 C 254 ASN PHE ARG SER ASN SER CYS
SEQRES 1 D 254 MET ALA PHE ALA ASP GLU ILE GLY GLN ALA PRO THR ALA
SEQRES 2 D 254 ALA ASN ILE THR GLY ASP GLY SER PHE SER THR SER SER
SEQRES 3 D 254 SER ALA ILE PHE GLY GLN SER GLY PHE GLY GLY GLY THR
SEQRES 4 D 254 ALA TYR TYR PRO ASN THR ALA GLY LYS TYR PRO VAL VAL
SEQRES 5 D 254 ALA PHE ALA PRO GLY PHE LEU SER ASP TRP ASN ALA LEU
SEQRES 6 D 254 ASN TRP LEU GLY PRO ARG VAL ALA SER TRP GLY PHE VAL
SEQRES 7 D 254 VAL VAL GLY VAL ASN THR ASN THR PRO PHE ASP PHE PRO
SEQRES 8 D 254 ASP ALA ARG GLY ASP GLN LEU LEU ALA ALA LEU ASN TRP
SEQRES 9 D 254 ALA VAL ASN SER ALA PRO ALA ALA VAL ARG ASP LYS ALA
SEQRES 10 D 254 ASP GLY SER ARG ARG GLY VAL SER GLY TRP SER MET GLY
SEQRES 11 D 254 GLY GLY GLY THR LEU GLU ALA LEU ALA LYS ASP THR THR
SEQRES 12 D 254 GLY THR VAL LYS ALA GLY VAL PRO LEU ALA PRO TRP HIS
SEQRES 13 D 254 THR ASN LYS THR TRP SER LYS VAL THR GLU PRO VAL PHE
SEQRES 14 D 254 ILE ILE GLY GLY GLN ASN ASP SER VAL ALA ALA PRO ALA
SEQRES 15 D 254 SER HIS ALA ILE PRO PHE TYR ASN SER LEU GLY GLY PRO
SEQRES 16 D 254 LYS SER TYR LEU GLU ARG ALA GLY ALA ASP HIS PHE PHE
SEQRES 17 D 254 PRO THR LYS SER ASN GLY THR VAL SER ARG ALA VAL VAL
SEQRES 18 D 254 SER PHE PHE LYS ARG HIS VAL SER ALA ASP THR ARG PHE
SEQRES 19 D 254 THR PRO PHE LEU CYS GLY PHE SER GLY LEU ASP VAL SER
SEQRES 20 D 254 ASN PHE ARG SER ASN SER CYS
FORMUL 5 HOH *823(H2 O)
HELIX 1 AA1 ASP A 61 ASN A 66 5 6
HELIX 2 AA2 TRP A 67 SER A 74 1 8
HELIX 3 AA3 PHE A 90 SER A 108 1 19
HELIX 4 AA4 PRO A 110 ASP A 115 1 6
HELIX 5 AA5 MET A 129 ASP A 141 1 13
HELIX 6 AA6 HIS A 184 LEU A 192 1 9
HELIX 7 AA7 PHE A 207 LYS A 211 5 5
HELIX 8 AA8 ASN A 213 VAL A 228 1 16
HELIX 9 AA9 ASP A 231 CYS A 239 5 9
HELIX 10 AB1 ASP B 61 ASN B 66 5 6
HELIX 11 AB2 TRP B 67 SER B 74 1 8
HELIX 12 AB3 PHE B 90 SER B 108 1 19
HELIX 13 AB4 PRO B 110 ASP B 115 1 6
HELIX 14 AB5 SER B 128 ASP B 141 1 14
HELIX 15 AB6 HIS B 184 LEU B 192 1 9
HELIX 16 AB7 PHE B 207 LYS B 211 5 5
HELIX 17 AB8 ASN B 213 VAL B 228 1 16
HELIX 18 AB9 ASP B 231 CYS B 239 5 9
HELIX 19 AC1 ASP C 61 ASN C 66 5 6
HELIX 20 AC2 TRP C 67 SER C 74 1 8
HELIX 21 AC3 PHE C 90 SER C 108 1 19
HELIX 22 AC4 PRO C 110 ASP C 115 1 6
HELIX 23 AC5 SER C 128 ASP C 141 1 14
HELIX 24 AC6 HIS C 184 LEU C 192 1 9
HELIX 25 AC7 PHE C 207 LYS C 211 5 5
HELIX 26 AC8 ASN C 213 VAL C 228 1 16
HELIX 27 AC9 ASP C 231 CYS C 239 5 9
HELIX 28 AD1 ASP D 61 ASN D 66 5 6
HELIX 29 AD2 TRP D 67 SER D 74 1 8
HELIX 30 AD3 PHE D 90 SER D 108 1 19
HELIX 31 AD4 PRO D 110 ASP D 115 1 6
HELIX 32 AD5 SER D 128 ASP D 141 1 14
HELIX 33 AD6 HIS D 184 LEU D 192 1 9
HELIX 34 AD7 PHE D 207 LYS D 211 5 5
HELIX 35 AD8 ASN D 213 VAL D 228 1 16
HELIX 36 AD9 ASP D 231 CYS D 239 5 9
SHEET 1 AA1 6 THR A 24 ILE A 29 0
SHEET 2 AA1 6 GLY A 37 PRO A 43 -1 O ALA A 40 N SER A 27
SHEET 3 AA1 6 VAL A 78 ASN A 83 -1 O GLY A 81 N THR A 39
SHEET 4 AA1 6 TYR A 49 ALA A 55 1 N VAL A 52 O VAL A 78
SHEET 5 AA1 6 ALA A 117 SER A 128 1 O ASP A 118 N TYR A 49
SHEET 6 AA1 6 VAL A 146 PRO A 154 1 O LEU A 152 N GLY A 126
SHEET 1 AA2 3 VAL A 168 GLY A 173 0
SHEET 2 AA2 3 LYS A 196 ARG A 201 1 O SER A 197 N ILE A 170
SHEET 3 AA2 3 VAL A 246 SER A 251 -1 O ARG A 250 N TYR A 198
SHEET 1 AA3 6 THR B 24 ALA B 28 0
SHEET 2 AA3 6 GLY B 37 PRO B 43 -1 O ALA B 40 N SER B 27
SHEET 3 AA3 6 VAL B 78 ASN B 83 -1 O GLY B 81 N THR B 39
SHEET 4 AA3 6 TYR B 49 ALA B 55 1 N VAL B 52 O VAL B 78
SHEET 5 AA3 6 ALA B 117 TRP B 127 1 O ASP B 118 N TYR B 49
SHEET 6 AA3 6 VAL B 146 LEU B 152 1 O LEU B 152 N GLY B 126
SHEET 1 AA4 3 VAL B 168 GLY B 173 0
SHEET 2 AA4 3 LYS B 196 ARG B 201 1 O ARG B 201 N GLY B 172
SHEET 3 AA4 3 VAL B 246 SER B 251 -1 O ARG B 250 N TYR B 198
SHEET 1 AA5 6 THR C 24 ALA C 28 0
SHEET 2 AA5 6 GLY C 37 PRO C 43 -1 O ALA C 40 N SER C 27
SHEET 3 AA5 6 VAL C 78 ASN C 83 -1 O GLY C 81 N THR C 39
SHEET 4 AA5 6 TYR C 49 ALA C 55 1 N VAL C 52 O VAL C 78
SHEET 5 AA5 6 ALA C 117 TRP C 127 1 O ASP C 118 N TYR C 49
SHEET 6 AA5 6 VAL C 146 LEU C 152 1 O LEU C 152 N GLY C 126
SHEET 1 AA6 3 VAL C 168 GLY C 173 0
SHEET 2 AA6 3 LYS C 196 ARG C 201 1 O ARG C 201 N GLY C 172
SHEET 3 AA6 3 VAL C 246 SER C 251 -1 O ASN C 248 N GLU C 200
SHEET 1 AA7 6 THR D 24 ILE D 29 0
SHEET 2 AA7 6 GLY D 37 PRO D 43 -1 O ALA D 40 N SER D 27
SHEET 3 AA7 6 VAL D 78 ASN D 83 -1 O GLY D 81 N THR D 39
SHEET 4 AA7 6 TYR D 49 ALA D 55 1 N VAL D 52 O VAL D 78
SHEET 5 AA7 6 ALA D 117 TRP D 127 1 O ASP D 118 N TYR D 49
SHEET 6 AA7 6 VAL D 146 LEU D 152 1 O LEU D 152 N GLY D 126
SHEET 1 AA8 3 VAL D 168 GLY D 173 0
SHEET 2 AA8 3 LYS D 196 ARG D 201 1 O ARG D 201 N GLY D 172
SHEET 3 AA8 3 VAL D 246 SER D 251 -1 O ASN D 248 N GLU D 200
SSBOND 1 CYS A 239 CYS A 254 1555 1555 2.76
SSBOND 2 CYS B 239 CYS B 254 1555 1555 2.08
SSBOND 3 CYS C 239 CYS C 254 1555 1555 2.14
SSBOND 4 CYS D 239 CYS D 254 1555 1555 2.12
CRYST1 62.496 104.798 71.020 90.00 93.83 90.00 P 1 21 1 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 0.016001 0.000000 0.001071 0.00000
SCALE2 0.000000 0.009542 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014112 0.00000
TER 1880 CYS A 254
TER 3753 CYS B 254
TER 5611 CYS C 254
TER 7477 CYS D 254
MASTER 319 0 0 36 36 0 0 6 8251 4 8 80
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