| 5CT6-pdb | HEADER HYDROLASE 23-JUL-15 5CT6
TITLE WILD-TYPE BACILLUS SUBTILIS LIPASE A WITH 20% [BMIM][CL]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE ESTA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LIPASE A,TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS (STRAIN 168);
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: ESTA, LIP, LIPA, BSU02700;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.NORDWALD,J.G.PLAKS,J.R.SNELL,M.C.SOUSA,J.L.KAAR
REVDAT 1 04-NOV-15 5CT6 0
JRNL AUTH E.M.NORDWALD,J.G.PLAKS,J.R.SNELL,M.C.SOUSA,J.L.KAAR
JRNL TITL CRYSTALLOGRAPHIC INVESTIGATION OF IMIDAZOLIUM IONIC LIQUID
JRNL TITL 2 EFFECTS ON ENZYME STRUCTURE.
JRNL REF CHEMBIOCHEM 2015
JRNL REFN ESSN 1439-7633
JRNL PMID 26388426
JRNL DOI 10.1002/CBIC.201500398
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3_928
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25788
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.740
REMARK 3 FREE R VALUE TEST SET COUNT : 1997
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 47.9220 - 4.5824 0.99 1851 154 0.2075 0.2286
REMARK 3 2 4.5824 - 3.6376 1.00 1737 145 0.1542 0.2023
REMARK 3 3 3.6376 - 3.1778 1.00 1736 147 0.1820 0.2214
REMARK 3 4 3.1778 - 2.8873 1.00 1688 141 0.1833 0.2379
REMARK 3 5 2.8873 - 2.6804 1.00 1709 145 0.1766 0.2044
REMARK 3 6 2.6804 - 2.5224 1.00 1692 141 0.1823 0.2231
REMARK 3 7 2.5224 - 2.3961 1.00 1689 142 0.1749 0.2275
REMARK 3 8 2.3961 - 2.2918 1.00 1682 142 0.1845 0.2108
REMARK 3 9 2.2918 - 2.2035 1.00 1654 138 0.1860 0.2540
REMARK 3 10 2.2035 - 2.1275 1.00 1692 143 0.1962 0.1955
REMARK 3 11 2.1275 - 2.0610 1.00 1662 140 0.1999 0.2382
REMARK 3 12 2.0610 - 2.0021 1.00 1672 139 0.2415 0.2741
REMARK 3 13 2.0021 - 1.9494 1.00 1684 142 0.2608 0.3045
REMARK 3 14 1.9494 - 1.9018 1.00 1643 138 0.3609 0.4109
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 : 0.33
REMARK 3 B_SOL : 37.14
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.330
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) : 2.20420
REMARK 3 B22 (A**2) : 2.20420
REMARK 3 B33 (A**2) : -4.22880
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.011 2887
REMARK 3 ANGLE : 1.172 3897
REMARK 3 CHIRALITY : 0.078 419
REMARK 3 PLANARITY : 0.005 501
REMARK 3 DIHEDRAL : 14.791 1028
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 5CT6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212144.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25866
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5000
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) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 40.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35 % PEG 3350, 20 MM NASO4, 0.1M
REMARK 280 ETHANOLAMINE, 10MM ZNCL2, PH 9.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 56.17550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.45050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.45050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.26325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.45050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.45050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.08775
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.45050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.45050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 84.26325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.45050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.45050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.08775
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.17550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 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 GLU A 2
REMARK 465 GLU B 2
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 HE2 HIS A 3 H SER A 32 1.15
REMARK 500 HB3 ASP B 118 HG3 GLN B 121 1.24
REMARK 500 HE2 HIS B 3 H SER B 32 1.25
REMARK 500 HE22 GLN B 164 O HOH B 302 1.36
REMARK 500 OE1 GLN B 29 HZ2 LYS B 170 1.47
REMARK 500 HG1 THR B 180 O HOH B 305 1.56
REMARK 500 O HOH B 374 O HOH B 397 1.84
REMARK 500 O HOH B 329 O HOH B 346 1.86
REMARK 500 OD1 ASP B 144 O HOH B 301 1.91
REMARK 500 O HOH B 314 O HOH B 379 2.12
REMARK 500 OD1 ASN A 50 C7 BM0 A 203 2.14
REMARK 500 O HOH A 392 O HOH A 407 2.14
REMARK 500 O HOH A 354 O HOH A 389 2.15
REMARK 500 O HOH A 378 O HOH A 408 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 HE2 LYS B 69 O HOH A 362 5755 1.13
REMARK 500 CE LYS B 69 O HOH A 362 5755 1.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS B 35 CD - CE - NZ ANGL. DEV. = 14.5 DEGREES
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 77 -129.32 61.62
REMARK 500 LEU A 90 -140.26 -110.79
REMARK 500 ALA A 113 94.20 -62.05
REMARK 500 GLN A 121 107.32 -165.08
REMARK 500 SER B 77 -131.95 57.95
REMARK 500 LEU B 90 -140.59 -107.26
REMARK 500 ALA B 97 -66.53 -104.63
REMARK 500 GLN B 121 71.98 -159.88
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 407 DISTANCE = 5.83 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BM0 B 205
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CRI RELATED DB: PDB
REMARK 900 RELATED ID: 5CT4 RELATED DB: PDB
REMARK 900 RELATED ID: 5CT5 RELATED DB: PDB
REMARK 900 RELATED ID: 5CT8 RELATED DB: PDB
REMARK 900 RELATED ID: 5CT9 RELATED DB: PDB
REMARK 900 RELATED ID: 5CTA RELATED DB: PDB
DBREF 5CT6 A 2 181 UNP P37957 ESTA_BACSU 33 212
DBREF 5CT6 B 2 181 UNP P37957 ESTA_BACSU 33 212
SEQRES 1 A 180 GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY
SEQRES 2 A 180 ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL
SEQRES 3 A 180 SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP
SEQRES 4 A 180 PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO
SEQRES 5 A 180 VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR
SEQRES 6 A 180 GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY
SEQRES 7 A 180 GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY
SEQRES 8 A 180 GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA
SEQRES 9 A 180 ASN ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP
SEQRES 10 A 180 PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER
SEQRES 11 A 180 ALA ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP
SEQRES 12 A 180 GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE
SEQRES 13 A 180 GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS
SEQRES 14 A 180 GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 B 180 GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY
SEQRES 2 B 180 ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL
SEQRES 3 B 180 SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP
SEQRES 4 B 180 PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO
SEQRES 5 B 180 VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR
SEQRES 6 B 180 GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY
SEQRES 7 B 180 GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY
SEQRES 8 B 180 GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA
SEQRES 9 B 180 ASN ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP
SEQRES 10 B 180 PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER
SEQRES 11 B 180 ALA ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP
SEQRES 12 B 180 GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE
SEQRES 13 B 180 GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS
SEQRES 14 B 180 GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
HET CL A 201 1
HET BM0 A 202 25
HET BM0 A 203 50
HET BM0 A 204 25
HET BM0 A 205 25
HET BM0 A 206 25
HET CL B 201 1
HET CL B 202 1
HET BM0 B 203 25
HET BM0 B 204 25
HET BM0 B 205 25
HETNAM CL CHLORIDE ION
HETNAM BM0 1-BUTYL-3-METHYL-1H-IMIDAZOL-3-IUM
HETSYN BM0 1-BUTYL-3-METHYLIMIDAZOLIUM
FORMUL 3 CL 3(CL 1-)
FORMUL 4 BM0 8(C8 H15 N2 1+)
FORMUL 14 HOH *232(H2 O)
HELIX 1 AA1 ALA A 15 ASN A 18 5 4
HELIX 2 AA2 PHE A 19 GLN A 29 1 11
HELIX 3 AA3 SER A 32 ASP A 34 5 3
HELIX 4 AA4 THR A 47 GLY A 67 1 21
HELIX 5 AA5 MET A 78 LEU A 90 1 13
HELIX 6 AA6 ASP A 91 ASN A 94 5 4
HELIX 7 AA7 ALA A 105 THR A 109 5 5
HELIX 8 AA8 MET A 137 ARG A 142 1 6
HELIX 9 AA9 ILE A 157 TYR A 161 5 5
HELIX 10 AB1 SER A 162 ASN A 174 1 13
HELIX 11 AB2 ALA B 15 ASN B 18 5 4
HELIX 12 AB3 PHE B 19 GLN B 29 1 11
HELIX 13 AB4 SER B 32 ASP B 34 5 3
HELIX 14 AB5 THR B 47 GLY B 67 1 21
HELIX 15 AB6 MET B 78 LEU B 90 1 13
HELIX 16 AB7 ASP B 91 ASN B 94 5 4
HELIX 17 AB8 ALA B 105 THR B 109 5 5
HELIX 18 AB9 MET B 137 ARG B 142 1 6
HELIX 19 AC1 HIS B 156 TYR B 161 5 6
HELIX 20 AC2 SER B 162 ASN B 174 1 13
SHEET 1 AA1 6 LEU A 36 ALA A 38 0
SHEET 2 AA1 6 VAL A 6 VAL A 9 1 N VAL A 6 O TYR A 37
SHEET 3 AA1 6 VAL A 71 HIS A 76 1 O VAL A 74 N VAL A 9
SHEET 4 AA1 6 VAL A 96 LEU A 102 1 O ALA A 97 N VAL A 71
SHEET 5 AA1 6 LEU A 124 SER A 130 1 O ILE A 128 N THR A 101
SHEET 6 AA1 6 ARG A 147 ILE A 151 1 O VAL A 149 N SER A 127
SHEET 1 AA2 6 LEU B 36 ALA B 38 0
SHEET 2 AA2 6 VAL B 6 VAL B 9 1 N VAL B 6 O TYR B 37
SHEET 3 AA2 6 VAL B 71 HIS B 76 1 O ASP B 72 N VAL B 7
SHEET 4 AA2 6 VAL B 96 LEU B 102 1 O VAL B 100 N ILE B 73
SHEET 5 AA2 6 LEU B 124 SER B 130 1 O LEU B 124 N VAL B 99
SHEET 6 AA2 6 ARG B 147 ILE B 151 1 O ILE B 151 N TYR B 129
SITE 1 AC1 5 GLY A 155 HIS A 156 ILE A 157 GLY A 158
SITE 2 AC1 5 GLY B 155
SITE 1 AC2 7 ILE A 12 GLY A 13 GLY A 14 ASN A 18
SITE 2 AC2 7 SER A 77 HIS A 156 HOH A 305
SITE 1 AC3 9 TYR A 49 ASN A 50 HOH A 302 HIS B 3
SITE 2 AC3 9 LYS B 35 THR B 66 GLY B 67 ALA B 68
SITE 3 AC3 9 MET B 137
SITE 1 AC4 4 THR A 45 THR A 47 HOH A 396 LEU B 108
SITE 1 AC5 6 GLY A 116 ASP A 118 PRO A 119 LYS A 122
SITE 2 AC5 6 HOH A 375 HOH B 348
SITE 1 AC6 6 ASP A 34 LEU A 36 TYR A 37 ARG A 107
SITE 2 AC6 6 ARG A 142 ASP A 144
SITE 1 AC7 4 GLY A 155 HOH A 306 HIS B 156 ILE B 157
SITE 1 AC8 3 THR B 47 ASN B 48 HOH B 380
SITE 1 AC9 5 ILE A 157 TRP B 42 GLY B 158 TYR B 161
SITE 2 AC9 5 HOH B 367
SITE 1 AD1 7 ASP B 34 LEU B 36 TYR B 37 ARG B 107
SITE 2 AD1 7 ARG B 142 ASP B 144 HOH B 381
SITE 1 AD2 3 TYR A 161 PHE B 17 TYR B 161
CRYST1 74.901 74.901 112.351 90.00 90.00 90.00 P 43 21 2 16
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 0.013351 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013351 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008901 0.00000
TER 2717 ASN A 181
TER 5454 ASN B 181
MASTER 397 0 11 20 12 0 19 6 3017 2 225 28
END
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