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HEADER HYDROLASE 12-APR-24 8Z2G
TITLE MHET BOUND FORM OF PET-DEGRADING CUTINASE MUTANT CUT190*SS_S176A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMONOSPORA VIRIDIS;
SOURCE 3 ORGANISM_TAXID: 1852;
SOURCE 4 GENE: CUT190, SAMN02982918_2340;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI B(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE80L
KEYWDS PROTEIN ENGINEERING, POLYESTERASE, METAL BINDING, AROMATIC LIGAND,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.NUMOTO,F.KONDO,G.J.BEKKER,Z.LIAO,M.YAMASHITA,A.IIDA,N.ITO,N.KAMIYA,
AUTHOR 2 M.ODA
REVDAT 1 06-NOV-24 8Z2G 0
JRNL AUTH N.NUMOTO,F.KONDO,G.J.BEKKER,Z.LIAO,M.YAMASHITA,A.IIDA,N.ITO,
JRNL AUTH 2 N.KAMIYA,M.ODA
JRNL TITL STRUCTURAL DYNAMICS OF THE CA 2+ -REGULATED CUTINASE TOWARDS
JRNL TITL 2 STRUCTURE-BASED IMPROVEMENT OF PET DEGRADATION ACTIVITY.
JRNL REF INT.J.BIOL.MACROMOL. V. 281 36597 2024
JRNL REFN ISSN 0141-8130
JRNL PMID 39419144
JRNL DOI 10.1016/J.IJBIOMAC.2024.136597
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 64.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 39006
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1961
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 48.0100 - 4.5700 0.94 2644 139 0.1474 0.1883
REMARK 3 2 4.5700 - 3.6300 0.91 2579 142 0.1517 0.1989
REMARK 3 3 3.6300 - 3.1700 0.94 2636 142 0.1935 0.1975
REMARK 3 4 3.1700 - 2.8800 0.93 2630 126 0.1997 0.2363
REMARK 3 5 2.8800 - 2.6700 0.94 2639 140 0.2065 0.2105
REMARK 3 6 2.6700 - 2.5200 0.95 2662 138 0.2233 0.2656
REMARK 3 7 2.5200 - 2.3900 0.95 2646 131 0.2323 0.2564
REMARK 3 8 2.3900 - 2.2900 0.94 2644 144 0.2373 0.2559
REMARK 3 9 2.2900 - 2.2000 0.95 2676 146 0.2498 0.3116
REMARK 3 10 2.2000 - 2.1200 0.95 2666 139 0.2656 0.2721
REMARK 3 11 2.1200 - 2.0600 0.95 2695 144 0.2702 0.3108
REMARK 3 12 2.0600 - 2.0000 0.95 2674 142 0.2741 0.3008
REMARK 3 13 2.0000 - 1.9500 0.95 2633 136 0.2811 0.3438
REMARK 3 14 1.9500 - 1.9000 0.93 2630 143 0.2789 0.2716
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.303
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.14
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 4172
REMARK 3 ANGLE : 0.534 5679
REMARK 3 CHIRALITY : 0.042 606
REMARK 3 PLANARITY : 0.006 744
REMARK 3 DIHEDRAL : 12.653 1540
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 8Z2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-APR-24.
REMARK 100 THE DEPOSITION ID IS D_1300046810.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-21
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 : SPRING-8
REMARK 200 BEAMLINE : BL45XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39011
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 48.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12400
REMARK 200 FOR THE DATA SET : 6.9000
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) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.66300
REMARK 200 FOR SHELL : 1.400
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: 7CTS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.13 M AMMONIUM SULFATE, 0.66 M MES PH
REMARK 280 6.5, 20% (W/V) PEG MONOMETHYL ETHER 5,000, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 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 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 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 GLY A 45
REMARK 465 LYS A 305
REMARK 465 LEU A 306
REMARK 465 ASN A 307
REMARK 465 GLY B 45
REMARK 465 LYS B 305
REMARK 465 LEU B 306
REMARK 465 ASN B 307
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 176 -110.90 56.83
REMARK 500 HIS A 230 -78.64 -123.06
REMARK 500 PRO A 243 98.27 -65.86
REMARK 500 ALA B 176 -111.78 57.56
REMARK 500 HIS B 230 -79.00 -124.50
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 B 609 DISTANCE = 5.82 ANGSTROMS
DBREF 8Z2G A 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
DBREF 8Z2G B 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
SEQADV 8Z2G GLY A 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 8Z2G PRO A 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 8Z2G HIS A 123 UNP W0TJ64 GLN 123 ENGINEERED MUTATION
SEQADV 8Z2G ALA A 138 UNP W0TJ64 GLN 138 ENGINEERED MUTATION
SEQADV 8Z2G ALA A 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 8Z2G HIS A 202 UNP W0TJ64 ASN 202 ENGINEERED MUTATION
SEQADV 8Z2G PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 8Z2G SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 8Z2G CYS A 250 UNP W0TJ64 ASP 250 ENGINEERED MUTATION
SEQADV 8Z2G CYS A 296 UNP W0TJ64 GLU 296 ENGINEERED MUTATION
SEQADV 8Z2G LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 8Z2G LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 8Z2G ASN A 307 UNP W0TJ64 EXPRESSION TAG
SEQADV 8Z2G GLY B 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 8Z2G PRO B 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 8Z2G HIS B 123 UNP W0TJ64 GLN 123 ENGINEERED MUTATION
SEQADV 8Z2G ALA B 138 UNP W0TJ64 GLN 138 ENGINEERED MUTATION
SEQADV 8Z2G ALA B 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 8Z2G HIS B 202 UNP W0TJ64 ASN 202 ENGINEERED MUTATION
SEQADV 8Z2G PRO B 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 8Z2G SER B 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 8Z2G CYS B 250 UNP W0TJ64 ASP 250 ENGINEERED MUTATION
SEQADV 8Z2G CYS B 296 UNP W0TJ64 GLU 296 ENGINEERED MUTATION
SEQADV 8Z2G LYS B 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 8Z2G LEU B 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 8Z2G ASN B 307 UNP W0TJ64 EXPRESSION TAG
SEQRES 1 A 263 GLY PRO ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 263 ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER VAL ALA
SEQRES 3 A 263 THR GLU ARG VAL SER SER PHE ALA SER GLY PHE GLY GLY
SEQRES 4 A 263 GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU GLY THR
SEQRES 5 A 263 PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR ALA SER
SEQRES 6 A 263 GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL ALA SER
SEQRES 7 A 263 HIS GLY PHE ILE VAL PHE THR ILE ASP THR ASN THR ARG
SEQRES 8 A 263 LEU ASP ALA PRO GLY GLN ARG GLY ARG GLN LEU LEU ALA
SEQRES 9 A 263 ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG LYS VAL
SEQRES 10 A 263 ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL MET GLY
SEQRES 11 A 263 HIS ALA MET GLY GLY GLY GLY SER LEU GLU ALA THR VAL
SEQRES 12 A 263 MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU THR PRO
SEQRES 13 A 263 TRP HIS LEU ASP LYS THR TRP GLY GLN VAL GLN VAL PRO
SEQRES 14 A 263 THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE ALA PRO
SEQRES 15 A 263 VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER LEU PRO
SEQRES 16 A 263 SER SER LEU PRO LYS ALA TYR MET GLU LEU CYS GLY ALA
SEQRES 17 A 263 THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR ILE ALA
SEQRES 18 A 263 LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL ASP GLU
SEQRES 19 A 263 ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN PRO THR
SEQRES 20 A 263 ASP ARG ALA ILE CYS GLU TYR ARG SER THR CYS PRO TYR
SEQRES 21 A 263 LYS LEU ASN
SEQRES 1 B 263 GLY PRO ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 B 263 ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER VAL ALA
SEQRES 3 B 263 THR GLU ARG VAL SER SER PHE ALA SER GLY PHE GLY GLY
SEQRES 4 B 263 GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU GLY THR
SEQRES 5 B 263 PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR ALA SER
SEQRES 6 B 263 GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL ALA SER
SEQRES 7 B 263 HIS GLY PHE ILE VAL PHE THR ILE ASP THR ASN THR ARG
SEQRES 8 B 263 LEU ASP ALA PRO GLY GLN ARG GLY ARG GLN LEU LEU ALA
SEQRES 9 B 263 ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG LYS VAL
SEQRES 10 B 263 ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL MET GLY
SEQRES 11 B 263 HIS ALA MET GLY GLY GLY GLY SER LEU GLU ALA THR VAL
SEQRES 12 B 263 MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU THR PRO
SEQRES 13 B 263 TRP HIS LEU ASP LYS THR TRP GLY GLN VAL GLN VAL PRO
SEQRES 14 B 263 THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE ALA PRO
SEQRES 15 B 263 VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER LEU PRO
SEQRES 16 B 263 SER SER LEU PRO LYS ALA TYR MET GLU LEU CYS GLY ALA
SEQRES 17 B 263 THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR ILE ALA
SEQRES 18 B 263 LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL ASP GLU
SEQRES 19 B 263 ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN PRO THR
SEQRES 20 B 263 ASP ARG ALA ILE CYS GLU TYR ARG SER THR CYS PRO TYR
SEQRES 21 B 263 LYS LEU ASN
HET NH4 A 401 1
HET BTB A 402 14
HET C9C A 403 15
HET GOL B 401 6
HET C9C B 402 15
HETNAM NH4 AMMONIUM ION
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETNAM C9C 4-(2-HYDROXYETHYLOXYCARBONYL)BENZOIC ACID
HETNAM GOL GLYCEROL
HETSYN BTB BIS-TRIS BUFFER
HETSYN C9C MONOHYDROXYETHYL TEREPHTHALATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NH4 H4 N 1+
FORMUL 4 BTB C8 H19 N O5
FORMUL 5 C9C 2(C10 H10 O5)
FORMUL 6 GOL C3 H8 O3
FORMUL 8 HOH *258(H2 O)
HELIX 1 AA1 THR A 56 ALA A 62 1 7
HELIX 2 AA2 SER A 109 MET A 113 5 5
HELIX 3 AA3 SER A 114 SER A 122 1 9
HELIX 4 AA4 ALA A 138 ARG A 156 1 19
HELIX 5 AA5 ASP A 158 GLU A 163 1 6
HELIX 6 AA6 ALA A 176 ARG A 189 1 14
HELIX 7 AA7 HIS A 230 LEU A 238 1 9
HELIX 8 AA8 PHE A 255 ILE A 259 5 5
HELIX 9 AA9 ASN A 261 ASP A 277 1 17
HELIX 10 AB1 ASP A 279 ARG A 281 5 3
HELIX 11 AB2 TYR A 282 CYS A 287 1 6
HELIX 12 AB3 THR B 56 GLU B 61 1 6
HELIX 13 AB4 SER B 109 SER B 114 5 6
HELIX 14 AB5 TRP B 115 SER B 122 1 8
HELIX 15 AB6 ALA B 138 ARG B 156 1 19
HELIX 16 AB7 ASP B 158 GLU B 163 1 6
HELIX 17 AB8 ALA B 176 ARG B 189 1 14
HELIX 18 AB9 HIS B 230 LEU B 238 1 9
HELIX 19 AC1 PHE B 255 ILE B 259 5 5
HELIX 20 AC2 ASN B 261 ASP B 277 1 17
HELIX 21 AC3 ASP B 279 ARG B 281 5 3
HELIX 22 AC4 TYR B 282 CYS B 287 1 6
SHEET 1 AA1 6 VAL A 69 VAL A 74 0
SHEET 2 AA1 6 GLY A 84 PRO A 89 -1 O GLY A 84 N VAL A 74
SHEET 3 AA1 6 ILE A 126 ILE A 130 -1 O VAL A 127 N TYR A 87
SHEET 4 AA1 6 PHE A 97 ALA A 103 1 N VAL A 102 O PHE A 128
SHEET 5 AA1 6 LEU A 165 HIS A 175 1 O ASP A 166 N PHE A 97
SHEET 6 AA1 6 ALA A 194 LEU A 198 1 O LEU A 198 N GLY A 174
SHEET 1 AA2 3 THR A 214 ALA A 219 0
SHEET 2 AA2 3 LYS A 244 LEU A 249 1 O LEU A 249 N GLY A 218
SHEET 3 AA2 3 ILE A 295 SER A 300 -1 O CYS A 296 N GLU A 248
SHEET 1 AA3 6 VAL B 69 VAL B 74 0
SHEET 2 AA3 6 GLY B 84 PRO B 89 -1 O ILE B 86 N GLU B 72
SHEET 3 AA3 6 PHE B 125 ILE B 130 -1 O VAL B 127 N TYR B 87
SHEET 4 AA3 6 PHE B 97 ALA B 103 1 N GLY B 98 O ILE B 126
SHEET 5 AA3 6 LEU B 165 HIS B 175 1 O ASP B 166 N PHE B 97
SHEET 6 AA3 6 ALA B 194 LEU B 198 1 O LEU B 198 N GLY B 174
SHEET 1 AA4 3 THR B 214 ALA B 219 0
SHEET 2 AA4 3 LYS B 244 LEU B 249 1 O MET B 247 N GLY B 218
SHEET 3 AA4 3 ILE B 295 SER B 300 -1 O ARG B 299 N TYR B 246
SSBOND 1 CYS A 250 CYS A 296 1555 1555 2.03
SSBOND 2 CYS A 287 CYS A 302 1555 1555 2.03
SSBOND 3 CYS B 250 CYS B 296 1555 1555 2.03
SSBOND 4 CYS B 287 CYS B 302 1555 1555 2.03
CISPEP 1 CYS A 287 PRO A 288 0 -1.89
CISPEP 2 CYS A 302 PRO A 303 0 -0.13
CISPEP 3 CYS B 287 PRO B 288 0 -0.11
CISPEP 4 CYS B 302 PRO B 303 0 -1.45
CRYST1 83.025 83.025 64.501 90.00 90.00 120.00 P 3 6
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 0.012045 0.006954 0.000000 0.00000
SCALE2 0.000000 0.013908 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015504 0.00000
TER 2006 TYR A 304
TER 4012 TYR B 304
MASTER 254 0 5 22 18 0 0 6 4319 2 58 42
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