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HEADER HYDROLASE 25-AUG-22 8GOL
TITLE CRYSTAL STRUCTURE OF SULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PUTATIVE HYDROLASE;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HANSSCHLEGELIA ZHIHUAIAE;
SOURCE 3 ORGANISM_TAXID: 405005;
SOURCE 4 GENE: EK403_17710;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SULE, WILD TYPE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.LIU,T.RAN,W.WANG,J.HE
REVDAT 1 02-AUG-23 8GOL 0
JRNL AUTH B.LIU,W.WANG,J.QIU,X.HUANG,S.QIU,Y.BAO,S.XU,L.RUAN,T.RAN,
JRNL AUTH 2 J.HE
JRNL TITL CRYSTAL STRUCTURES OF HERBICIDE-DETOXIFYING ESTERASE REVEAL
JRNL TITL 2 A LID LOOP AFFECTING SUBSTRATE BINDING AND ACTIVITY.
JRNL REF NAT COMMUN V. 14 4343 2023
JRNL REFN ESSN 2041-1723
JRNL PMID 37468532
JRNL DOI 10.1038/S41467-023-40103-5
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX V 1.16
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 168060
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
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) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.71
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 : 0.006 11498
REMARK 3 ANGLE : 0.856 15638
REMARK 3 CHIRALITY : 0.057 1622
REMARK 3 PLANARITY : 0.006 2061
REMARK 3 DIHEDRAL : 16.972 6710
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 8GOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-AUG-22.
REMARK 100 THE DEPOSITION ID IS D_1300031421.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 168217
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 49.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 4Q34
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
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 83.33050
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -25.99512
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 72.44215
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 GLU A 2
REMARK 465 THR A 3
REMARK 465 ASP A 4
REMARK 465 ASN A 5
REMARK 465 VAL A 6
REMARK 465 GLU A 7
REMARK 465 LEU A 8
REMARK 465 ALA A 9
REMARK 465 GLN A 10
REMARK 465 SER A 11
REMARK 465 GLU A 361
REMARK 465 SER A 362
REMARK 465 LEU A 363
REMARK 465 GLU A 364
REMARK 465 HIS A 365
REMARK 465 HIS A 366
REMARK 465 HIS A 367
REMARK 465 HIS A 368
REMARK 465 HIS A 369
REMARK 465 HIS A 370
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 THR B 3
REMARK 465 ASP B 4
REMARK 465 ASN B 5
REMARK 465 VAL B 6
REMARK 465 GLU B 7
REMARK 465 LEU B 8
REMARK 465 ALA B 9
REMARK 465 GLN B 10
REMARK 465 SER B 11
REMARK 465 HIS B 367
REMARK 465 HIS B 368
REMARK 465 HIS B 369
REMARK 465 HIS B 370
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 THR C 3
REMARK 465 ASP C 4
REMARK 465 ASN C 5
REMARK 465 VAL C 6
REMARK 465 GLU C 7
REMARK 465 LEU C 8
REMARK 465 ALA C 9
REMARK 465 GLN C 10
REMARK 465 SER C 11
REMARK 465 GLU C 361
REMARK 465 SER C 362
REMARK 465 LEU C 363
REMARK 465 GLU C 364
REMARK 465 HIS C 365
REMARK 465 HIS C 366
REMARK 465 HIS C 367
REMARK 465 HIS C 368
REMARK 465 HIS C 369
REMARK 465 HIS C 370
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 THR D 3
REMARK 465 ASP D 4
REMARK 465 ASN D 5
REMARK 465 VAL D 6
REMARK 465 GLU D 7
REMARK 465 LEU D 8
REMARK 465 ALA D 9
REMARK 465 GLN D 10
REMARK 465 SER D 11
REMARK 465 GLU D 361
REMARK 465 SER D 362
REMARK 465 LEU D 363
REMARK 465 GLU D 364
REMARK 465 HIS D 365
REMARK 465 HIS D 366
REMARK 465 HIS D 367
REMARK 465 HIS D 368
REMARK 465 HIS D 369
REMARK 465 HIS D 370
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 122 -144.26 -138.44
REMARK 500 GLU A 130 -120.65 51.52
REMARK 500 SER A 183 44.90 -84.82
REMARK 500 SER A 209 -114.48 49.91
REMARK 500 SER A 209 -112.05 46.20
REMARK 500 LYS A 252 -0.91 67.88
REMARK 500 PHE A 334 66.26 -118.65
REMARK 500 PHE B 122 -143.99 -136.86
REMARK 500 GLU B 130 -127.09 54.37
REMARK 500 SER B 183 46.72 -80.15
REMARK 500 SER B 209 -115.68 53.31
REMARK 500 LYS B 253 -52.34 -148.62
REMARK 500 ASN B 340 31.47 -99.88
REMARK 500 ASN B 360 151.11 73.11
REMARK 500 ARG C 66 72.67 55.21
REMARK 500 PHE C 122 -146.03 -139.99
REMARK 500 GLU C 130 -120.92 48.95
REMARK 500 SER C 183 47.79 -83.93
REMARK 500 SER C 209 -115.04 52.66
REMARK 500 PHE C 334 65.28 -118.72
REMARK 500 ARG D 66 72.17 53.17
REMARK 500 PHE D 122 -146.57 -138.62
REMARK 500 GLU D 130 -127.26 53.78
REMARK 500 SER D 183 46.97 -83.11
REMARK 500 SER D 209 -117.90 53.53
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 D 857 DISTANCE = 5.98 ANGSTROMS
DBREF 8GOL A 2 362 UNP G9I933 G9I933_9HYPH 38 398
DBREF 8GOL B 2 362 UNP G9I933 G9I933_9HYPH 38 398
DBREF 8GOL C 2 362 UNP G9I933 G9I933_9HYPH 38 398
DBREF 8GOL D 2 362 UNP G9I933 G9I933_9HYPH 38 398
SEQADV 8GOL MET A 1 UNP G9I933 INITIATING METHIONINE
SEQADV 8GOL LEU A 363 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL GLU A 364 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS A 365 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS A 366 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS A 367 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS A 368 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS A 369 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS A 370 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL MET B 1 UNP G9I933 INITIATING METHIONINE
SEQADV 8GOL LEU B 363 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL GLU B 364 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS B 365 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS B 366 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS B 367 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS B 368 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS B 369 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS B 370 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL MET C 1 UNP G9I933 INITIATING METHIONINE
SEQADV 8GOL LEU C 363 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL GLU C 364 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS C 365 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS C 366 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS C 367 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS C 368 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS C 369 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS C 370 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL MET D 1 UNP G9I933 INITIATING METHIONINE
SEQADV 8GOL LEU D 363 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL GLU D 364 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS D 365 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS D 366 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS D 367 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS D 368 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS D 369 UNP G9I933 EXPRESSION TAG
SEQADV 8GOL HIS D 370 UNP G9I933 EXPRESSION TAG
SEQRES 1 A 370 MET GLU THR ASP ASN VAL GLU LEU ALA GLN SER LYS ARG
SEQRES 2 A 370 LYS VAL VAL LEU ALA GLU GLN GLY SER PHE TYR ILE GLY
SEQRES 3 A 370 GLY ARG THR VAL THR GLY PRO GLY LYS PHE ASP PRO SER
SEQRES 4 A 370 LYS PRO VAL ILE PRO TYR SER ASN GLU GLY ALA THR PHE
SEQRES 5 A 370 TYR ILE ASN GLN MET TYR VAL ASN PHE GLN ALA PRO VAL
SEQRES 6 A 370 ARG PRO ARG GLY LEU PRO LEU VAL PHE TRP HIS GLY GLY
SEQRES 7 A 370 GLY LEU THR GLY HIS ILE TRP GLU SER THR PRO ASP GLY
SEQRES 8 A 370 ARG PRO GLY PHE GLN THR LEU PHE VAL GLN ASP ARG HIS
SEQRES 9 A 370 THR VAL TYR THR ILE ASP GLN PRO GLY ARG GLY ARG GLY
SEQRES 10 A 370 ASN ILE PRO THR PHE ASN GLY PRO PHE GLY GLN LEU GLU
SEQRES 11 A 370 GLU GLU SER ILE VAL ASN THR VAL THR GLY ASN SER SER
SEQRES 12 A 370 LYS GLU GLY ALA TRP VAL ARG ASP ARG LEU GLY PRO ALA
SEQRES 13 A 370 PRO GLY GLN PHE PHE GLU ASN SER GLN PHE PRO ARG GLY
SEQRES 14 A 370 TYR GLU ASP ASN TYR PHE LYS GLU MET GLY PHE SER PRO
SEQRES 15 A 370 SER ILE SER SER ASP GLU ILE VAL ASP ALA VAL VAL LYS
SEQRES 16 A 370 LEU VAL THR HIS ILE GLY PRO CYS VAL LEU VAL THR HIS
SEQRES 17 A 370 SER ALA SER GLY VAL LEU GLY MET ARG VAL ALA THR HIS
SEQRES 18 A 370 ALA LYS ASN VAL ARG GLY ILE VAL ALA TYR GLU PRO ALA
SEQRES 19 A 370 THR SER ILE PHE PRO LYS GLY LYS VAL PRO GLU ILE PRO
SEQRES 20 A 370 PRO LEU ALA ASP LYS LYS SER GLN ILE PHE PRO PRO PHE
SEQRES 21 A 370 GLU ILE GLN GLU SER TYR PHE LYS LYS LEU ALA LYS ILE
SEQRES 22 A 370 PRO ILE GLN PHE VAL PHE GLY ASP ASN ILE PRO LYS ASN
SEQRES 23 A 370 PRO LYS SER ALA TYR TRP PHE LEU ASP TRP TRP ARG VAL
SEQRES 24 A 370 THR ARG TYR ALA HIS SER LEU SER LEU GLU ALA ILE ASN
SEQRES 25 A 370 LYS LEU GLY GLY GLN ALA SER LEU LEU ASP LEU PRO THR
SEQRES 26 A 370 ALA GLY LEU ARG GLY ASN THR HIS PHE PRO PHE THR ASP
SEQRES 27 A 370 ARG ASN ASN VAL GLN VAL ALA SER LEU LEU SER ASP PHE
SEQRES 28 A 370 LEU GLY LYS HIS GLY LEU ASP GLN ASN GLU SER LEU GLU
SEQRES 29 A 370 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 370 MET GLU THR ASP ASN VAL GLU LEU ALA GLN SER LYS ARG
SEQRES 2 B 370 LYS VAL VAL LEU ALA GLU GLN GLY SER PHE TYR ILE GLY
SEQRES 3 B 370 GLY ARG THR VAL THR GLY PRO GLY LYS PHE ASP PRO SER
SEQRES 4 B 370 LYS PRO VAL ILE PRO TYR SER ASN GLU GLY ALA THR PHE
SEQRES 5 B 370 TYR ILE ASN GLN MET TYR VAL ASN PHE GLN ALA PRO VAL
SEQRES 6 B 370 ARG PRO ARG GLY LEU PRO LEU VAL PHE TRP HIS GLY GLY
SEQRES 7 B 370 GLY LEU THR GLY HIS ILE TRP GLU SER THR PRO ASP GLY
SEQRES 8 B 370 ARG PRO GLY PHE GLN THR LEU PHE VAL GLN ASP ARG HIS
SEQRES 9 B 370 THR VAL TYR THR ILE ASP GLN PRO GLY ARG GLY ARG GLY
SEQRES 10 B 370 ASN ILE PRO THR PHE ASN GLY PRO PHE GLY GLN LEU GLU
SEQRES 11 B 370 GLU GLU SER ILE VAL ASN THR VAL THR GLY ASN SER SER
SEQRES 12 B 370 LYS GLU GLY ALA TRP VAL ARG ASP ARG LEU GLY PRO ALA
SEQRES 13 B 370 PRO GLY GLN PHE PHE GLU ASN SER GLN PHE PRO ARG GLY
SEQRES 14 B 370 TYR GLU ASP ASN TYR PHE LYS GLU MET GLY PHE SER PRO
SEQRES 15 B 370 SER ILE SER SER ASP GLU ILE VAL ASP ALA VAL VAL LYS
SEQRES 16 B 370 LEU VAL THR HIS ILE GLY PRO CYS VAL LEU VAL THR HIS
SEQRES 17 B 370 SER ALA SER GLY VAL LEU GLY MET ARG VAL ALA THR HIS
SEQRES 18 B 370 ALA LYS ASN VAL ARG GLY ILE VAL ALA TYR GLU PRO ALA
SEQRES 19 B 370 THR SER ILE PHE PRO LYS GLY LYS VAL PRO GLU ILE PRO
SEQRES 20 B 370 PRO LEU ALA ASP LYS LYS SER GLN ILE PHE PRO PRO PHE
SEQRES 21 B 370 GLU ILE GLN GLU SER TYR PHE LYS LYS LEU ALA LYS ILE
SEQRES 22 B 370 PRO ILE GLN PHE VAL PHE GLY ASP ASN ILE PRO LYS ASN
SEQRES 23 B 370 PRO LYS SER ALA TYR TRP PHE LEU ASP TRP TRP ARG VAL
SEQRES 24 B 370 THR ARG TYR ALA HIS SER LEU SER LEU GLU ALA ILE ASN
SEQRES 25 B 370 LYS LEU GLY GLY GLN ALA SER LEU LEU ASP LEU PRO THR
SEQRES 26 B 370 ALA GLY LEU ARG GLY ASN THR HIS PHE PRO PHE THR ASP
SEQRES 27 B 370 ARG ASN ASN VAL GLN VAL ALA SER LEU LEU SER ASP PHE
SEQRES 28 B 370 LEU GLY LYS HIS GLY LEU ASP GLN ASN GLU SER LEU GLU
SEQRES 29 B 370 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 370 MET GLU THR ASP ASN VAL GLU LEU ALA GLN SER LYS ARG
SEQRES 2 C 370 LYS VAL VAL LEU ALA GLU GLN GLY SER PHE TYR ILE GLY
SEQRES 3 C 370 GLY ARG THR VAL THR GLY PRO GLY LYS PHE ASP PRO SER
SEQRES 4 C 370 LYS PRO VAL ILE PRO TYR SER ASN GLU GLY ALA THR PHE
SEQRES 5 C 370 TYR ILE ASN GLN MET TYR VAL ASN PHE GLN ALA PRO VAL
SEQRES 6 C 370 ARG PRO ARG GLY LEU PRO LEU VAL PHE TRP HIS GLY GLY
SEQRES 7 C 370 GLY LEU THR GLY HIS ILE TRP GLU SER THR PRO ASP GLY
SEQRES 8 C 370 ARG PRO GLY PHE GLN THR LEU PHE VAL GLN ASP ARG HIS
SEQRES 9 C 370 THR VAL TYR THR ILE ASP GLN PRO GLY ARG GLY ARG GLY
SEQRES 10 C 370 ASN ILE PRO THR PHE ASN GLY PRO PHE GLY GLN LEU GLU
SEQRES 11 C 370 GLU GLU SER ILE VAL ASN THR VAL THR GLY ASN SER SER
SEQRES 12 C 370 LYS GLU GLY ALA TRP VAL ARG ASP ARG LEU GLY PRO ALA
SEQRES 13 C 370 PRO GLY GLN PHE PHE GLU ASN SER GLN PHE PRO ARG GLY
SEQRES 14 C 370 TYR GLU ASP ASN TYR PHE LYS GLU MET GLY PHE SER PRO
SEQRES 15 C 370 SER ILE SER SER ASP GLU ILE VAL ASP ALA VAL VAL LYS
SEQRES 16 C 370 LEU VAL THR HIS ILE GLY PRO CYS VAL LEU VAL THR HIS
SEQRES 17 C 370 SER ALA SER GLY VAL LEU GLY MET ARG VAL ALA THR HIS
SEQRES 18 C 370 ALA LYS ASN VAL ARG GLY ILE VAL ALA TYR GLU PRO ALA
SEQRES 19 C 370 THR SER ILE PHE PRO LYS GLY LYS VAL PRO GLU ILE PRO
SEQRES 20 C 370 PRO LEU ALA ASP LYS LYS SER GLN ILE PHE PRO PRO PHE
SEQRES 21 C 370 GLU ILE GLN GLU SER TYR PHE LYS LYS LEU ALA LYS ILE
SEQRES 22 C 370 PRO ILE GLN PHE VAL PHE GLY ASP ASN ILE PRO LYS ASN
SEQRES 23 C 370 PRO LYS SER ALA TYR TRP PHE LEU ASP TRP TRP ARG VAL
SEQRES 24 C 370 THR ARG TYR ALA HIS SER LEU SER LEU GLU ALA ILE ASN
SEQRES 25 C 370 LYS LEU GLY GLY GLN ALA SER LEU LEU ASP LEU PRO THR
SEQRES 26 C 370 ALA GLY LEU ARG GLY ASN THR HIS PHE PRO PHE THR ASP
SEQRES 27 C 370 ARG ASN ASN VAL GLN VAL ALA SER LEU LEU SER ASP PHE
SEQRES 28 C 370 LEU GLY LYS HIS GLY LEU ASP GLN ASN GLU SER LEU GLU
SEQRES 29 C 370 HIS HIS HIS HIS HIS HIS
SEQRES 1 D 370 MET GLU THR ASP ASN VAL GLU LEU ALA GLN SER LYS ARG
SEQRES 2 D 370 LYS VAL VAL LEU ALA GLU GLN GLY SER PHE TYR ILE GLY
SEQRES 3 D 370 GLY ARG THR VAL THR GLY PRO GLY LYS PHE ASP PRO SER
SEQRES 4 D 370 LYS PRO VAL ILE PRO TYR SER ASN GLU GLY ALA THR PHE
SEQRES 5 D 370 TYR ILE ASN GLN MET TYR VAL ASN PHE GLN ALA PRO VAL
SEQRES 6 D 370 ARG PRO ARG GLY LEU PRO LEU VAL PHE TRP HIS GLY GLY
SEQRES 7 D 370 GLY LEU THR GLY HIS ILE TRP GLU SER THR PRO ASP GLY
SEQRES 8 D 370 ARG PRO GLY PHE GLN THR LEU PHE VAL GLN ASP ARG HIS
SEQRES 9 D 370 THR VAL TYR THR ILE ASP GLN PRO GLY ARG GLY ARG GLY
SEQRES 10 D 370 ASN ILE PRO THR PHE ASN GLY PRO PHE GLY GLN LEU GLU
SEQRES 11 D 370 GLU GLU SER ILE VAL ASN THR VAL THR GLY ASN SER SER
SEQRES 12 D 370 LYS GLU GLY ALA TRP VAL ARG ASP ARG LEU GLY PRO ALA
SEQRES 13 D 370 PRO GLY GLN PHE PHE GLU ASN SER GLN PHE PRO ARG GLY
SEQRES 14 D 370 TYR GLU ASP ASN TYR PHE LYS GLU MET GLY PHE SER PRO
SEQRES 15 D 370 SER ILE SER SER ASP GLU ILE VAL ASP ALA VAL VAL LYS
SEQRES 16 D 370 LEU VAL THR HIS ILE GLY PRO CYS VAL LEU VAL THR HIS
SEQRES 17 D 370 SER ALA SER GLY VAL LEU GLY MET ARG VAL ALA THR HIS
SEQRES 18 D 370 ALA LYS ASN VAL ARG GLY ILE VAL ALA TYR GLU PRO ALA
SEQRES 19 D 370 THR SER ILE PHE PRO LYS GLY LYS VAL PRO GLU ILE PRO
SEQRES 20 D 370 PRO LEU ALA ASP LYS LYS SER GLN ILE PHE PRO PRO PHE
SEQRES 21 D 370 GLU ILE GLN GLU SER TYR PHE LYS LYS LEU ALA LYS ILE
SEQRES 22 D 370 PRO ILE GLN PHE VAL PHE GLY ASP ASN ILE PRO LYS ASN
SEQRES 23 D 370 PRO LYS SER ALA TYR TRP PHE LEU ASP TRP TRP ARG VAL
SEQRES 24 D 370 THR ARG TYR ALA HIS SER LEU SER LEU GLU ALA ILE ASN
SEQRES 25 D 370 LYS LEU GLY GLY GLN ALA SER LEU LEU ASP LEU PRO THR
SEQRES 26 D 370 ALA GLY LEU ARG GLY ASN THR HIS PHE PRO PHE THR ASP
SEQRES 27 D 370 ARG ASN ASN VAL GLN VAL ALA SER LEU LEU SER ASP PHE
SEQRES 28 D 370 LEU GLY LYS HIS GLY LEU ASP GLN ASN GLU SER LEU GLU
SEQRES 29 D 370 HIS HIS HIS HIS HIS HIS
HET IJC A 401 25
HET GOL A 402 6
HET IJC B 401 25
HET GOL B 402 6
HET IJC C 401 25
HET GOL C 402 6
HET IJC D 401 25
HET GOL D 402 6
HETNAM IJC 2-[(4-CHLORANYL-6-METHOXY-PYRIMIDIN-2-YL)
HETNAM 2 IJC CARBAMOYLSULFAMOYL]BENZOIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 IJC 4(C13 H11 CL N4 O6 S)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 13 HOH *1456(H2 O)
HELIX 1 AA1 GLY A 82 SER A 87 1 6
HELIX 2 AA2 GLY A 94 ASP A 102 1 9
HELIX 3 AA3 SER A 143 ASP A 151 1 9
HELIX 4 AA4 TYR A 170 LYS A 176 1 7
HELIX 5 AA5 SER A 185 GLY A 201 1 17
HELIX 6 AA6 ALA A 210 ALA A 222 1 13
HELIX 7 AA7 GLN A 263 LYS A 268 1 6
HELIX 8 AA8 LYS A 269 LYS A 272 5 4
HELIX 9 AA9 TYR A 291 LEU A 314 1 24
HELIX 10 AB1 PRO A 324 GLY A 327 5 4
HELIX 11 AB2 PHE A 334 ASP A 338 5 5
HELIX 12 AB3 ASN A 340 HIS A 355 1 16
HELIX 13 AB4 GLY B 82 SER B 87 1 6
HELIX 14 AB5 GLY B 94 ASP B 102 1 9
HELIX 15 AB6 SER B 143 ASP B 151 1 9
HELIX 16 AB7 TYR B 170 GLU B 177 1 8
HELIX 17 AB8 SER B 185 GLY B 201 1 17
HELIX 18 AB9 ALA B 210 ALA B 222 1 13
HELIX 19 AC1 GLN B 263 LYS B 268 1 6
HELIX 20 AC2 LYS B 269 LYS B 272 5 4
HELIX 21 AC3 TYR B 291 LEU B 314 1 24
HELIX 22 AC4 PRO B 324 GLY B 327 5 4
HELIX 23 AC5 PHE B 334 ASP B 338 5 5
HELIX 24 AC6 ASN B 340 HIS B 355 1 16
HELIX 25 AC7 GLY C 82 SER C 87 1 6
HELIX 26 AC8 GLY C 94 ASP C 102 1 9
HELIX 27 AC9 SER C 143 ASP C 151 1 9
HELIX 28 AD1 TYR C 170 LYS C 176 1 7
HELIX 29 AD2 SER C 185 GLY C 201 1 17
HELIX 30 AD3 ALA C 210 ALA C 222 1 13
HELIX 31 AD4 GLN C 263 LYS C 268 1 6
HELIX 32 AD5 LYS C 269 LYS C 272 5 4
HELIX 33 AD6 TYR C 291 LEU C 314 1 24
HELIX 34 AD7 PRO C 324 GLY C 327 5 4
HELIX 35 AD8 PHE C 334 ASP C 338 5 5
HELIX 36 AD9 ASN C 340 HIS C 355 1 16
HELIX 37 AE1 GLY D 82 SER D 87 1 6
HELIX 38 AE2 GLY D 94 ASP D 102 1 9
HELIX 39 AE3 SER D 143 ASP D 151 1 9
HELIX 40 AE4 TYR D 170 GLU D 177 1 8
HELIX 41 AE5 SER D 185 GLY D 201 1 17
HELIX 42 AE6 ALA D 210 ALA D 222 1 13
HELIX 43 AE7 GLN D 263 LYS D 268 1 6
HELIX 44 AE8 LYS D 269 LYS D 272 5 4
HELIX 45 AE9 TYR D 291 LEU D 314 1 24
HELIX 46 AF1 PHE D 334 ASP D 338 5 5
HELIX 47 AF2 ASN D 340 HIS D 355 1 16
SHEET 1 AA116 GLN A 317 ASP A 322 0
SHEET 2 AA116 PRO A 274 PHE A 279 1 N PHE A 277 O LEU A 321
SHEET 3 AA116 VAL A 225 TYR A 231 1 N ALA A 230 O VAL A 278
SHEET 4 AA116 CYS A 203 HIS A 208 1 N CYS A 203 O ARG A 226
SHEET 5 AA116 LEU A 72 TRP A 75 1 N TRP A 75 O VAL A 206
SHEET 6 AA116 VAL A 106 ASP A 110 1 O TYR A 107 N LEU A 72
SHEET 7 AA116 MET A 57 PRO A 64 -1 N ASN A 60 O THR A 108
SHEET 8 AA116 VAL A 15 ILE A 25 -1 N GLY A 21 O PHE A 61
SHEET 9 AA116 VAL B 15 ILE B 25 -1 O VAL B 15 N LEU A 17
SHEET 10 AA116 MET B 57 PRO B 64 -1 O PHE B 61 N GLY B 21
SHEET 11 AA116 VAL B 106 ASP B 110 -1 O THR B 108 N ASN B 60
SHEET 12 AA116 LEU B 72 TRP B 75 1 N LEU B 72 O TYR B 107
SHEET 13 AA116 CYS B 203 HIS B 208 1 O VAL B 206 N TRP B 75
SHEET 14 AA116 VAL B 225 TYR B 231 1 O ARG B 226 N CYS B 203
SHEET 15 AA116 PRO B 274 PHE B 279 1 O VAL B 278 N ALA B 230
SHEET 16 AA116 GLN B 317 ASP B 322 1 O LEU B 321 N PHE B 277
SHEET 1 AA2 2 ARG A 28 THR A 31 0
SHEET 2 AA2 2 THR A 51 ILE A 54 -1 O PHE A 52 N VAL A 30
SHEET 1 AA3 2 GLY A 124 PRO A 125 0
SHEET 2 AA3 2 VAL B 138 THR B 139 -1 O THR B 139 N GLY A 124
SHEET 1 AA4 2 GLN A 128 LEU A 129 0
SHEET 2 AA4 2 GLU A 132 SER A 133 -1 O GLU A 132 N LEU A 129
SHEET 1 AA5 2 VAL A 138 THR A 139 0
SHEET 2 AA5 2 GLY B 124 PRO B 125 -1 O GLY B 124 N THR A 139
SHEET 1 AA6 2 ILE A 237 PRO A 239 0
SHEET 2 AA6 2 PHE A 260 ILE A 262 1 O PHE A 260 N PHE A 238
SHEET 1 AA7 2 ARG B 28 THR B 31 0
SHEET 2 AA7 2 THR B 51 ILE B 54 -1 O PHE B 52 N VAL B 30
SHEET 1 AA8 2 GLN B 128 LEU B 129 0
SHEET 2 AA8 2 GLU B 132 SER B 133 -1 O GLU B 132 N LEU B 129
SHEET 1 AA9 2 ILE B 237 PRO B 239 0
SHEET 2 AA9 2 PHE B 260 ILE B 262 1 O PHE B 260 N PHE B 238
SHEET 1 AB1 8 LEU C 17 ILE C 25 0
SHEET 2 AB1 8 MET C 57 PRO C 64 -1 O PHE C 61 N GLY C 21
SHEET 3 AB1 8 VAL C 106 ASP C 110 -1 O THR C 108 N ASN C 60
SHEET 4 AB1 8 LEU C 72 TRP C 75 1 N PHE C 74 O TYR C 107
SHEET 5 AB1 8 CYS C 203 HIS C 208 1 O VAL C 206 N TRP C 75
SHEET 6 AB1 8 VAL C 225 TYR C 231 1 O ARG C 226 N CYS C 203
SHEET 7 AB1 8 PRO C 274 PHE C 279 1 O VAL C 278 N ALA C 230
SHEET 8 AB1 8 GLN C 317 ASP C 322 1 O LEU C 321 N PHE C 277
SHEET 1 AB2 2 ARG C 28 THR C 31 0
SHEET 2 AB2 2 THR C 51 ILE C 54 -1 O PHE C 52 N VAL C 30
SHEET 1 AB3 2 GLN C 128 LEU C 129 0
SHEET 2 AB3 2 GLU C 132 SER C 133 -1 O GLU C 132 N LEU C 129
SHEET 1 AB4 2 ILE C 237 PRO C 239 0
SHEET 2 AB4 2 PHE C 260 ILE C 262 1 O PHE C 260 N PHE C 238
SHEET 1 AB5 8 LEU D 17 ILE D 25 0
SHEET 2 AB5 8 MET D 57 PRO D 64 -1 O ALA D 63 N GLU D 19
SHEET 3 AB5 8 VAL D 106 ASP D 110 -1 O THR D 108 N ASN D 60
SHEET 4 AB5 8 LEU D 72 TRP D 75 1 N LEU D 72 O TYR D 107
SHEET 5 AB5 8 CYS D 203 HIS D 208 1 O VAL D 206 N TRP D 75
SHEET 6 AB5 8 VAL D 225 TYR D 231 1 O ARG D 226 N CYS D 203
SHEET 7 AB5 8 PRO D 274 PHE D 279 1 O VAL D 278 N ALA D 230
SHEET 8 AB5 8 GLN D 317 ASP D 322 1 O LEU D 321 N PHE D 277
SHEET 1 AB6 2 ARG D 28 THR D 31 0
SHEET 2 AB6 2 THR D 51 ILE D 54 -1 O PHE D 52 N VAL D 30
SHEET 1 AB7 2 GLN D 128 LEU D 129 0
SHEET 2 AB7 2 GLU D 132 SER D 133 -1 O GLU D 132 N LEU D 129
SHEET 1 AB8 2 ILE D 237 PRO D 239 0
SHEET 2 AB8 2 PHE D 260 ILE D 262 1 O PHE D 260 N PHE D 238
CISPEP 1 ILE A 43 PRO A 44 0 8.77
CISPEP 2 ILE B 43 PRO B 44 0 -0.21
CISPEP 3 ILE C 43 PRO C 44 0 0.63
CISPEP 4 ILE D 43 PRO D 44 0 -0.10
CRYST1 55.422 166.661 76.965 90.00 109.74 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 0.018043 0.000000 0.006475 0.00000
SCALE2 0.000000 0.006000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013804 0.00000
TER 2743 ASN A 360
TER 5546 HIS B 366
TER 8297 ASN C 360
TER 11037 ASN D 360
MASTER 339 0 8 47 60 0 0 612588 4 124 116
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