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HEADER HYDROLASE 10-JAN-17 5UGZ
TITLE CRYSTAL STRUCTURE OF CLBQ FROM THE COLIBACTIN NRPS/PKS PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE THIOESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: THIOESTERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: CLBQ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS TYPE-II THIOESTERASE, COLIBACTIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.S.GUNTAKA,S.D.BRUNER
REVDAT 1 20-SEP-17 5UGZ 0
JRNL AUTH N.S.GUNTAKA,A.R.HEALY,J.M.CRAWFORD,S.B.HERZON,S.D.BRUNER
JRNL TITL STRUCTURE AND FUNCTIONAL ANALYSIS OF CLBQ, AN UNUSUAL
JRNL TITL 2 INTERMEDIATE-RELEASING THIOESTERASE FROM THE COLIBACTIN
JRNL TITL 3 BIOSYNTHETIC PATHWAY.
JRNL REF ACS CHEM. BIOL. 2017
JRNL REFN ESSN 1554-8937
JRNL PMID 28846367
JRNL DOI 10.1021/ACSCHEMBIO.7B00479
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 36949
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.230
REMARK 3 FREE R VALUE TEST SET COUNT : 1932
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 22.4179 - 4.7692 0.93 2555 133 0.1343 0.1734
REMARK 3 2 4.7692 - 3.7914 0.93 2503 139 0.1120 0.1656
REMARK 3 3 3.7914 - 3.3139 0.94 2558 139 0.1343 0.1931
REMARK 3 4 3.3139 - 3.0117 0.95 2502 109 0.1510 0.1934
REMARK 3 5 3.0117 - 2.7963 0.94 2536 141 0.1601 0.2196
REMARK 3 6 2.7963 - 2.6317 0.94 2484 139 0.1657 0.2081
REMARK 3 7 2.6317 - 2.5001 0.94 2523 122 0.1703 0.2617
REMARK 3 8 2.5001 - 2.3914 0.93 2491 152 0.1676 0.2345
REMARK 3 9 2.3914 - 2.2994 0.93 2498 149 0.1672 0.2397
REMARK 3 10 2.2994 - 2.2201 0.94 2492 125 0.1760 0.2214
REMARK 3 11 2.2201 - 2.1508 0.94 2499 124 0.1807 0.2451
REMARK 3 12 2.1508 - 2.0893 0.93 2507 128 0.1939 0.2241
REMARK 3 13 2.0893 - 2.0344 0.92 2449 153 0.1864 0.2566
REMARK 3 14 2.0344 - 1.9848 0.91 2417 147 0.2046 0.2867
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 29.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.007 3950
REMARK 3 ANGLE : 0.902 5358
REMARK 3 CHIRALITY : 0.050 588
REMARK 3 PLANARITY : 0.005 686
REMARK 3 DIHEDRAL : 13.195 2314
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 5UGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225841.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-16
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 : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9767
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36972
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 38.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.41600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: 3FLB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, LITHIUM SULPHATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 47.49700
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
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 463 O HOH B 509 1.89
REMARK 500 O HOH A 462 O HOH A 480 2.02
REMARK 500 OE1 GLN A 191 CD1 ILE A 209 2.05
REMARK 500 O HOH B 481 O HOH B 503 2.09
REMARK 500 O HOH B 511 O HOH B 513 2.11
REMARK 500 O HOH A 432 O HOH A 486 2.13
REMARK 500 ND1 HIS A 120 OE1 GLU A 163 2.17
REMARK 500 NH1 ARG B 206 O HOH B 401 2.18
REMARK 500 O HOH B 408 O HOH B 502 2.18
REMARK 500 O HOH B 422 O HOH B 464 2.19
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 78 -118.86 56.80
REMARK 500 ALA A 113 65.19 -64.78
REMARK 500 ALA A 169 155.43 -46.84
REMARK 500 ASP A 214 -156.52 -92.25
REMARK 500 SER B 78 -113.36 61.40
REMARK 500 LEU B 134 72.31 -164.10
REMARK 500 THR B 137 143.90 172.14
REMARK 500 ASP B 140 43.18 -105.84
REMARK 500 ARG B 143 -31.01 -132.20
REMARK 500 ALA B 171 -6.51 -59.87
REMARK 500 ARG B 203 -168.10 -101.99
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 506 DISTANCE = 5.87 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BME A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BME B 301 and CYS B
REMARK 800 49
DBREF 5UGZ A 1 240 UNP Q0P7K7 Q0P7K7_ECOLX 1 240
DBREF 5UGZ B 1 240 UNP Q0P7K7 Q0P7K7_ECOLX 1 240
SEQADV 5UGZ MET A -19 UNP Q0P7K7 INITIATING METHIONINE
SEQADV 5UGZ GLY A -18 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER A -17 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER A -16 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS A -15 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS A -14 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS A -13 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS A -12 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS A -11 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS A -10 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER A -9 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER A -8 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ GLY A -7 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ LEU A -6 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ VAL A -5 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ PRO A -4 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ ARG A -3 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ GLY A -2 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER A -1 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS A 0 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ MET B -19 UNP Q0P7K7 INITIATING METHIONINE
SEQADV 5UGZ GLY B -18 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER B -17 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER B -16 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS B -15 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS B -14 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS B -13 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS B -12 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS B -11 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS B -10 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER B -9 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER B -8 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ GLY B -7 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ LEU B -6 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ VAL B -5 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ PRO B -4 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ ARG B -3 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ GLY B -2 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ SER B -1 UNP Q0P7K7 EXPRESSION TAG
SEQADV 5UGZ HIS B 0 UNP Q0P7K7 EXPRESSION TAG
SEQRES 1 A 260 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 260 LEU VAL PRO ARG GLY SER HIS MET SER ASN ILE SER LEU
SEQRES 3 A 260 TYR CYS LEU PRO TYR SER GLY GLY SER ALA ALA MET TYR
SEQRES 4 A 260 TYR LYS TRP ARG SER VAL LEU SER ASP ASN ILE THR LEU
SEQRES 5 A 260 ARG PRO LEU GLU PRO ALA GLY ARG GLY THR ARG ILE ARG
SEQRES 6 A 260 GLN PRO LEU CYS LEU THR MET VAL ASP ALA VAL ALA ASP
SEQRES 7 A 260 LEU TYR GLN GLN PHE VAL LYS HIS TYR THR GLY GLY ASP
SEQRES 8 A 260 TYR ALA ILE PHE GLY HIS SER LEU GLY GLY ILE MET ALA
SEQRES 9 A 260 PHE GLU LEU VAL HIS TYR ILE LEU ASP HIS GLY HIS ASP
SEQRES 10 A 260 MET PRO CYS ALA LEU PHE PHE SER GLY CYS ARG PRO PRO
SEQRES 11 A 260 ASP ARG ALA SER HIS GLU VAL ILE LEU HIS THR LEU PRO
SEQRES 12 A 260 ASP GLN ALA PHE MET GLU GLU ILE VAL LYS LEU GLY GLY
SEQRES 13 A 260 THR PRO VAL ASP VAL PHE ARG ASN LYS GLU LEU MET THR
SEQRES 14 A 260 ILE PHE THR PRO ILE ILE LYS ASN ASP TYR ARG LEU TYR
SEQRES 15 A 260 GLU GLN TYR VAL PHE GLN ALA LYS ALA ARG THR LEU THR
SEQRES 16 A 260 CYS PRO ILE VAL LEU PHE HIS GLY ASP ALA ASP ASN LEU
SEQRES 17 A 260 VAL MET GLN ASP GLU LEU LEU ALA TRP GLU LYS PHE THR
SEQRES 18 A 260 THR ARG LYS THR ARG THR ILE ILE PHE PRO ALA ALA ASP
SEQRES 19 A 260 HIS PHE PHE VAL ASP LYS HIS PHE GLU GLN VAL VAL GLY
SEQRES 20 A 260 TYR VAL ASN GLN THR ILE GLU SER LEU GLU ILE VAL GLY
SEQRES 1 B 260 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 260 LEU VAL PRO ARG GLY SER HIS MET SER ASN ILE SER LEU
SEQRES 3 B 260 TYR CYS LEU PRO TYR SER GLY GLY SER ALA ALA MET TYR
SEQRES 4 B 260 TYR LYS TRP ARG SER VAL LEU SER ASP ASN ILE THR LEU
SEQRES 5 B 260 ARG PRO LEU GLU PRO ALA GLY ARG GLY THR ARG ILE ARG
SEQRES 6 B 260 GLN PRO LEU CYS LEU THR MET VAL ASP ALA VAL ALA ASP
SEQRES 7 B 260 LEU TYR GLN GLN PHE VAL LYS HIS TYR THR GLY GLY ASP
SEQRES 8 B 260 TYR ALA ILE PHE GLY HIS SER LEU GLY GLY ILE MET ALA
SEQRES 9 B 260 PHE GLU LEU VAL HIS TYR ILE LEU ASP HIS GLY HIS ASP
SEQRES 10 B 260 MET PRO CYS ALA LEU PHE PHE SER GLY CYS ARG PRO PRO
SEQRES 11 B 260 ASP ARG ALA SER HIS GLU VAL ILE LEU HIS THR LEU PRO
SEQRES 12 B 260 ASP GLN ALA PHE MET GLU GLU ILE VAL LYS LEU GLY GLY
SEQRES 13 B 260 THR PRO VAL ASP VAL PHE ARG ASN LYS GLU LEU MET THR
SEQRES 14 B 260 ILE PHE THR PRO ILE ILE LYS ASN ASP TYR ARG LEU TYR
SEQRES 15 B 260 GLU GLN TYR VAL PHE GLN ALA LYS ALA ARG THR LEU THR
SEQRES 16 B 260 CYS PRO ILE VAL LEU PHE HIS GLY ASP ALA ASP ASN LEU
SEQRES 17 B 260 VAL MET GLN ASP GLU LEU LEU ALA TRP GLU LYS PHE THR
SEQRES 18 B 260 THR ARG LYS THR ARG THR ILE ILE PHE PRO ALA ALA ASP
SEQRES 19 B 260 HIS PHE PHE VAL ASP LYS HIS PHE GLU GLN VAL VAL GLY
SEQRES 20 B 260 TYR VAL ASN GLN THR ILE GLU SER LEU GLU ILE VAL GLY
HET BME A 301 10
HET BME B 301 10
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 3 BME 2(C2 H6 O S)
FORMUL 5 HOH *225(H2 O)
HELIX 1 AA1 SER A 15 VAL A 25 5 11
HELIX 2 AA2 ARG A 40 ILE A 44 5 5
HELIX 3 AA3 THR A 51 VAL A 64 1 14
HELIX 4 AA4 SER A 78 HIS A 94 1 17
HELIX 5 AA5 PRO A 123 GLY A 135 1 13
HELIX 6 AA6 PRO A 138 PHE A 142 5 5
HELIX 7 AA7 ASN A 144 GLN A 164 1 21
HELIX 8 AA8 MET A 190 THR A 201 5 12
HELIX 9 AA9 PHE A 216 HIS A 221 1 6
HELIX 10 AB1 HIS A 221 GLY A 240 1 20
HELIX 11 AB2 ALA B 16 LYS B 21 1 6
HELIX 12 AB3 TRP B 22 VAL B 25 5 4
HELIX 13 AB4 ARG B 40 ILE B 44 5 5
HELIX 14 AB5 THR B 51 TYR B 67 1 17
HELIX 15 AB6 SER B 78 GLY B 95 1 18
HELIX 16 AB7 PRO B 123 ILE B 131 1 9
HELIX 17 AB8 ASN B 144 GLN B 164 1 21
HELIX 18 AB9 MET B 190 THR B 201 5 12
HELIX 19 AC1 PHE B 216 HIS B 221 1 6
HELIX 20 AC2 HIS B 221 GLY B 240 1 20
SHEET 1 AA1 6 ILE A 30 PRO A 34 0
SHEET 2 AA1 6 ILE A 4 LEU A 9 1 N LEU A 6 O ARG A 33
SHEET 3 AA1 6 ASP A 71 HIS A 77 1 O PHE A 75 N TYR A 7
SHEET 4 AA1 6 ALA A 101 SER A 105 1 O PHE A 103 N ILE A 74
SHEET 5 AA1 6 ILE A 178 GLY A 183 1 O VAL A 179 N LEU A 102
SHEET 6 AA1 6 THR A 205 PHE A 210 1 O PHE A 210 N HIS A 182
SHEET 1 AA2 6 ILE B 30 PRO B 34 0
SHEET 2 AA2 6 ILE B 4 LEU B 9 1 N ILE B 4 O THR B 31
SHEET 3 AA2 6 ASP B 71 HIS B 77 1 O ALA B 73 N SER B 5
SHEET 4 AA2 6 ALA B 101 SER B 105 1 O SER B 105 N GLY B 76
SHEET 5 AA2 6 ILE B 178 GLY B 183 1 O VAL B 179 N LEU B 102
SHEET 6 AA2 6 THR B 205 PHE B 210 1 O ARG B 206 N LEU B 180
LINK SG CYS B 49 S2 BME B 301 1555 1555 2.00
SITE 1 AC1 5 PRO A 47 CYS A 49 ASP A 54 ASP A 58
SITE 2 AC1 5 HOH A 405
SITE 1 AC2 8 ALA B 38 PRO B 47 LEU B 48 LEU B 50
SITE 2 AC2 8 THR B 51 ASN B 157 HOH B 403 HOH B 423
CRYST1 44.971 94.994 68.444 90.00 109.18 90.00 P 1 21 1 4
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 0.022237 0.000000 0.007734 0.00000
SCALE2 0.000000 0.010527 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015469 0.00000
TER 1918 GLY A 240
TER 3836 GLY B 240
MASTER 322 0 2 20 12 0 4 6 4067 2 21 40
END |