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HEADER HYDROLASE 18-JUL-18 6AAE
TITLE CRYSTAL STRUCTURE OF CHLORAMPHENICOL-METABOLIZAING ENZYME ESTDL136
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: TO MAKE ESTDL136 CRYSTAL, INTERNAL RESIDUES FROM P37
COMPND 8 TO P39 WERE DELETED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 GENE: ESTDL136;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS CHLORAMPHENICOL, METAGENOME, HORNOME SENSITIVE LIPASE, HSL, ESTDL136,
KEYWDS 2 ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.KIM,P.A.KANG,K.T.HAN,S.W.LEE,S.K.RHEE
REVDAT 1 06-FEB-19 6AAE 0
JRNL AUTH S.H.KIM,P.A.KANG,K.T.HAN,S.W.LEE,S.K.RHEE
JRNL TITL CRYSTAL STRUCTURE OF CHLORAMPHENICOL-METABOLIZING ENZYME
JRNL TITL 2 ESTDL136 FROM A METAGENOME.
JRNL REF PLOS ONE V. 14 10298 2019
JRNL REFN ESSN 1932-6203
JRNL PMID 30645605
JRNL DOI 10.1371/JOURNAL.PONE.0210298
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 99964
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 32.2638 - 3.9529 1.00 7418 150 0.1468 0.1706
REMARK 3 2 3.9529 - 3.1384 1.00 7121 146 0.1591 0.2015
REMARK 3 3 3.1384 - 2.7419 1.00 7077 144 0.1846 0.2025
REMARK 3 4 2.7419 - 2.4913 1.00 7014 143 0.1895 0.2200
REMARK 3 5 2.4913 - 2.3128 1.00 7024 144 0.1893 0.2430
REMARK 3 6 2.3128 - 2.1765 1.00 6986 143 0.2241 0.2769
REMARK 3 7 2.1765 - 2.0675 1.00 6976 142 0.2082 0.2257
REMARK 3 8 2.0675 - 1.9775 1.00 6927 141 0.2202 0.2335
REMARK 3 9 1.9775 - 1.9014 1.00 6944 142 0.2646 0.2927
REMARK 3 10 1.9014 - 1.8358 1.00 6917 142 0.2640 0.3134
REMARK 3 11 1.8358 - 1.7784 1.00 6920 141 0.2426 0.2927
REMARK 3 12 1.7784 - 1.7276 1.00 6983 142 0.2570 0.2958
REMARK 3 13 1.7276 - 1.6821 1.00 6875 141 0.2688 0.2607
REMARK 3 14 1.6821 - 1.6410 0.98 6783 138 0.2864 0.3076
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.160
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 4994
REMARK 3 ANGLE : 1.068 6747
REMARK 3 CHIRALITY : 0.043 716
REMARK 3 PLANARITY : 0.005 882
REMARK 3 DIHEDRAL : 15.370 1795
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 6AAE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1300008421.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-14
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 : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100067
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
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: PHENIX
REMARK 200 STARTING MODEL: 1U4N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 500MM AMMONIUM FLUORIDE (PH6.5), 30%
REMARK 280 PEG3350, 5% GLYCEROL AND 120MM TCEP, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 59.47150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.79300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.47150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.79300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 10590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 MET A 1
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 MET B 1
REMARK 465 HIS B 316
REMARK 465 HIS B 317
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 A 661 O HOH A 712 2.15
REMARK 500 O HOH A 683 O HOH A 703 2.16
REMARK 500 O1 PEG B 406 O1 PEG B 407 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 ASP A 54 109.97 -58.60
REMARK 500 SER A 153 -122.34 60.82
REMARK 500 TYR A 181 65.41 25.55
REMARK 500 TYR A 202 -74.91 77.78
REMARK 500 ALA A 227 -67.76 -92.20
REMARK 500 MET B 17 -178.20 177.02
REMARK 500 SER B 153 -121.24 61.16
REMARK 500 TYR B 181 64.70 24.37
REMARK 500 TYR B 202 -50.50 74.03
REMARK 500 ALA B 227 -61.89 -99.11
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 746 DISTANCE = 6.04 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 414
DBREF 6AAE A 1 307 UNP G3CR02 G3CR02_9BACT 1 310
DBREF 6AAE B 1 307 UNP G3CR02 G3CR02_9BACT 1 310
SEQADV 6AAE A UNP G3CR02 PRO 37 DELETION
SEQADV 6AAE A UNP G3CR02 MET 38 DELETION
SEQADV 6AAE A UNP G3CR02 PRO 39 DELETION
SEQADV 6AAE LEU A 308 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE GLU A 309 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS A 310 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS A 311 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS A 312 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS A 313 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS A 314 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS A 315 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS A 316 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS A 317 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE B UNP G3CR02 PRO 37 DELETION
SEQADV 6AAE B UNP G3CR02 MET 38 DELETION
SEQADV 6AAE B UNP G3CR02 PRO 39 DELETION
SEQADV 6AAE LEU B 308 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE GLU B 309 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS B 310 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS B 311 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS B 312 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS B 313 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS B 314 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS B 315 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS B 316 UNP G3CR02 EXPRESSION TAG
SEQADV 6AAE HIS B 317 UNP G3CR02 EXPRESSION TAG
SEQRES 1 A 317 MET PRO LEU ASN PRO HIS VAL GLU ALA LEU LEU GLN MET
SEQRES 2 A 317 MET ALA GLN MET PRO ALA PRO ASP PHE SER VAL ALA ASN
SEQRES 3 A 317 PRO ALA GLU ILE ARG ALA VAL PHE ASP ASN LEU ALA ALA
SEQRES 4 A 317 PRO PRO GLN VAL ALA ARG VAL GLU ASN ILE ALA ILE SER
SEQRES 5 A 317 LEU ASP GLY ARG ASP LEU ASP ALA ARG LEU TYR VAL PRO
SEQRES 6 A 317 GLU ASP ALA ASP GLU ARG PRO ALA LEU MET VAL TYR TYR
SEQRES 7 A 317 HIS GLY GLY GLY TRP VAL ILE GLY THR LEU ASP THR HIS
SEQRES 8 A 317 ASP GLY THR CYS ARG ALA LEU ALA GLN LYS SER GLY CYS
SEQRES 9 A 317 ALA VAL LEU SER ILE ALA TYR ARG LEU ALA PRO GLU TYR
SEQRES 10 A 317 ARG TYR PRO ALA PRO ALA GLU ASP CYS TYR ASP ALA LEU
SEQRES 11 A 317 VAL TRP ALA LYS GLN ASN ALA ALA THR LEU GLY VAL ASP
SEQRES 12 A 317 GLY ASP ARG LEU ALA VAL GLY GLY ASP SER ALA GLY GLY
SEQRES 13 A 317 ASN LEU ALA ALA ALA VAL ALA ILE MET ALA ARG ASP ARG
SEQRES 14 A 317 ASN GLY PRO ALA LEU ARG HIS GLN LEU LEU ILE TYR PRO
SEQRES 15 A 317 VAL THR ASP ASN ASP PHE THR LEU ALA SER TYR ALA GLU
SEQRES 16 A 317 ASN GLY GLY GLY GLU TYR TYR LEU SER THR ASP GLY MET
SEQRES 17 A 317 ARG TRP PHE TRP GLY HIS TYR LEU GLY ASP THR ALA ALA
SEQRES 18 A 317 GLU ASN ALA PRO LEU ALA ALA VAL LEU ASN VAL ALA ASP
SEQRES 19 A 317 LEU SER GLY LEU ALA PRO ALA THR VAL ILE THR ALA GLU
SEQRES 20 A 317 TYR ASP PRO LEU ARG ASP GLU GLY ILE ALA TYR ALA LYS
SEQRES 21 A 317 LYS LEU ASP ALA ALA GLY VAL PRO VAL ASP ALA ALA THR
SEQRES 22 A 317 ALA PRO GLY MET ILE HIS GLY PHE PHE SER MET PHE GLU
SEQRES 23 A 317 ALA VAL PRO ASP SER TRP GLU TRP ILE GLU ARG GLY ALA
SEQRES 24 A 317 SER ASN LEU LYS ARG ASP LEU ALA LEU GLU HIS HIS HIS
SEQRES 25 A 317 HIS HIS HIS HIS HIS
SEQRES 1 B 317 MET PRO LEU ASN PRO HIS VAL GLU ALA LEU LEU GLN MET
SEQRES 2 B 317 MET ALA GLN MET PRO ALA PRO ASP PHE SER VAL ALA ASN
SEQRES 3 B 317 PRO ALA GLU ILE ARG ALA VAL PHE ASP ASN LEU ALA ALA
SEQRES 4 B 317 PRO PRO GLN VAL ALA ARG VAL GLU ASN ILE ALA ILE SER
SEQRES 5 B 317 LEU ASP GLY ARG ASP LEU ASP ALA ARG LEU TYR VAL PRO
SEQRES 6 B 317 GLU ASP ALA ASP GLU ARG PRO ALA LEU MET VAL TYR TYR
SEQRES 7 B 317 HIS GLY GLY GLY TRP VAL ILE GLY THR LEU ASP THR HIS
SEQRES 8 B 317 ASP GLY THR CYS ARG ALA LEU ALA GLN LYS SER GLY CYS
SEQRES 9 B 317 ALA VAL LEU SER ILE ALA TYR ARG LEU ALA PRO GLU TYR
SEQRES 10 B 317 ARG TYR PRO ALA PRO ALA GLU ASP CYS TYR ASP ALA LEU
SEQRES 11 B 317 VAL TRP ALA LYS GLN ASN ALA ALA THR LEU GLY VAL ASP
SEQRES 12 B 317 GLY ASP ARG LEU ALA VAL GLY GLY ASP SER ALA GLY GLY
SEQRES 13 B 317 ASN LEU ALA ALA ALA VAL ALA ILE MET ALA ARG ASP ARG
SEQRES 14 B 317 ASN GLY PRO ALA LEU ARG HIS GLN LEU LEU ILE TYR PRO
SEQRES 15 B 317 VAL THR ASP ASN ASP PHE THR LEU ALA SER TYR ALA GLU
SEQRES 16 B 317 ASN GLY GLY GLY GLU TYR TYR LEU SER THR ASP GLY MET
SEQRES 17 B 317 ARG TRP PHE TRP GLY HIS TYR LEU GLY ASP THR ALA ALA
SEQRES 18 B 317 GLU ASN ALA PRO LEU ALA ALA VAL LEU ASN VAL ALA ASP
SEQRES 19 B 317 LEU SER GLY LEU ALA PRO ALA THR VAL ILE THR ALA GLU
SEQRES 20 B 317 TYR ASP PRO LEU ARG ASP GLU GLY ILE ALA TYR ALA LYS
SEQRES 21 B 317 LYS LEU ASP ALA ALA GLY VAL PRO VAL ASP ALA ALA THR
SEQRES 22 B 317 ALA PRO GLY MET ILE HIS GLY PHE PHE SER MET PHE GLU
SEQRES 23 B 317 ALA VAL PRO ASP SER TRP GLU TRP ILE GLU ARG GLY ALA
SEQRES 24 B 317 SER ASN LEU LYS ARG ASP LEU ALA LEU GLU HIS HIS HIS
SEQRES 25 B 317 HIS HIS HIS HIS HIS
HET 1PE A 401 16
HET 1PE A 402 16
HET PEG A 403 7
HET PEG A 404 7
HET PEG A 405 7
HET 1PE B 401 16
HET 1PE B 402 16
HET 1PE B 403 16
HET 1PE B 404 16
HET PEG B 405 7
HET PEG B 406 7
HET PEG B 407 7
HET PEG B 408 7
HET PEG B 409 7
HET PEG B 410 7
HET PEG B 411 7
HET PEG B 412 7
HET PEG B 413 7
HET PEG B 414 7
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN 1PE PEG400
FORMUL 3 1PE 6(C10 H22 O6)
FORMUL 5 PEG 13(C4 H10 O3)
FORMUL 22 HOH *487(H2 O)
HELIX 1 AA1 ASN A 4 GLN A 16 1 13
HELIX 2 AA2 ASN A 26 ALA A 39 1 14
HELIX 3 AA3 HIS A 91 GLY A 103 1 13
HELIX 4 AA4 PRO A 120 ASN A 136 1 17
HELIX 5 AA5 ASN A 136 GLY A 141 1 6
HELIX 6 AA6 SER A 153 ARG A 169 1 17
HELIX 7 AA7 LEU A 190 GLY A 197 1 8
HELIX 8 AA8 SER A 204 GLY A 217 1 14
HELIX 9 AA9 ALA A 220 ALA A 224 5 5
HELIX 10 AB1 ALA A 228 VAL A 232 5 5
HELIX 11 AB2 LEU A 251 ALA A 265 1 15
HELIX 12 AB3 GLY A 280 PHE A 285 5 6
HELIX 13 AB4 ASP A 290 LEU A 306 1 17
HELIX 14 AB5 ASN B 4 ALA B 15 1 12
HELIX 15 AB6 ASN B 26 ASP B 35 1 10
HELIX 16 AB7 HIS B 91 GLY B 103 1 13
HELIX 17 AB8 PRO B 120 ASN B 136 1 17
HELIX 18 AB9 ASN B 136 GLY B 141 1 6
HELIX 19 AC1 SER B 153 ARG B 169 1 17
HELIX 20 AC2 LEU B 190 GLY B 197 1 8
HELIX 21 AC3 SER B 204 GLY B 217 1 14
HELIX 22 AC4 ALA B 220 ALA B 224 5 5
HELIX 23 AC5 ALA B 228 VAL B 232 5 5
HELIX 24 AC6 LEU B 251 ALA B 265 1 15
HELIX 25 AC7 GLY B 280 PHE B 285 5 6
HELIX 26 AC8 ASP B 290 LEU B 306 1 17
SHEET 1 AA1 8 ARG A 45 LEU A 53 0
SHEET 2 AA1 8 ARG A 56 VAL A 64 -1 O LEU A 58 N ILE A 51
SHEET 3 AA1 8 ALA A 105 ILE A 109 -1 O SER A 108 N ARG A 61
SHEET 4 AA1 8 LEU A 74 TYR A 78 1 N MET A 75 O LEU A 107
SHEET 5 AA1 8 LEU A 147 ASP A 152 1 O ALA A 148 N VAL A 76
SHEET 6 AA1 8 HIS A 176 ILE A 180 1 O LEU A 178 N VAL A 149
SHEET 7 AA1 8 ALA A 241 ALA A 246 1 O THR A 242 N LEU A 179
SHEET 8 AA1 8 VAL A 269 ALA A 274 1 O ALA A 274 N THR A 245
SHEET 1 AA2 8 ARG B 45 LEU B 53 0
SHEET 2 AA2 8 ARG B 56 VAL B 64 -1 O LEU B 58 N ILE B 51
SHEET 3 AA2 8 ALA B 105 ILE B 109 -1 O VAL B 106 N TYR B 63
SHEET 4 AA2 8 LEU B 74 TYR B 78 1 N TYR B 77 O LEU B 107
SHEET 5 AA2 8 LEU B 147 ASP B 152 1 O ALA B 148 N VAL B 76
SHEET 6 AA2 8 HIS B 176 ILE B 180 1 O LEU B 178 N VAL B 149
SHEET 7 AA2 8 ALA B 241 ALA B 246 1 O THR B 242 N LEU B 179
SHEET 8 AA2 8 VAL B 269 ALA B 274 1 O ALA B 274 N THR B 245
CISPEP 1 ALA A 114 PRO A 115 0 1.99
CISPEP 2 TYR A 119 PRO A 120 0 5.39
CISPEP 3 ALA B 114 PRO B 115 0 1.86
CISPEP 4 TYR B 119 PRO B 120 0 6.47
SITE 1 AC1 7 ASP A 152 SER A 153 TYR A 202 HIS A 279
SITE 2 AC1 7 GLY A 280 SER A 283 1PE B 402
SITE 1 AC2 6 GLU A 47 TRP A 132 THR A 139 LEU A 140
SITE 2 AC2 6 GLU B 47 THR B 139
SITE 1 AC3 2 GLU A 8 GLU B 200
SITE 1 AC4 4 GLN A 100 LYS A 101 TRP A 292 GLU A 296
SITE 1 AC5 4 ASP A 206 ARG A 209 GLY A 213 PHE B 22
SITE 1 AC6 8 MET A 14 GLY B 81 ASP B 152 SER B 153
SITE 2 AC6 8 TYR B 202 HIS B 279 HOH B 502 HOH B 656
SITE 1 AC7 7 MET A 13 1PE A 401 MET B 13 MET B 14
SITE 2 AC7 7 ALA B 38 HOH B 502 HOH B 545
SITE 1 AC8 10 ALA A 28 ASP B 67 ASP B 69 GLN B 100
SITE 2 AC8 10 LYS B 101 SER B 102 GLY B 103 LYS B 303
SITE 3 AC8 10 PEG B 406 HOH B 549
SITE 1 AC9 12 GLU B 116 ARG B 118 HIS B 214 ARG B 304
SITE 2 AC9 12 ASP B 305 ALA B 307 GLU B 309 HOH B 521
SITE 3 AC9 12 HOH B 539 HOH B 543 HOH B 663 HOH B 686
SITE 1 AD1 5 ALA A 25 PHE B 211 HOH B 504 HOH B 642
SITE 2 AD1 5 HOH B 646
SITE 1 AD2 5 GLN B 100 LYS B 101 GLU B 296 1PE B 403
SITE 2 AD2 5 PEG B 407
SITE 1 AD3 6 ASN B 36 GLN B 100 LYS B 101 TRP B 292
SITE 2 AD3 6 GLU B 296 PEG B 406
SITE 1 AD4 3 TYR B 248 HOH B 598 HOH B 600
SITE 1 AD5 4 VAL A 24 ALA A 25 ASN A 26 ASP B 270
SITE 1 AD6 5 ARG B 112 PRO B 120 ALA B 121 HOH B 529
SITE 2 AD6 5 HOH B 616
SITE 1 AD7 8 ARG B 45 VAL B 64 PRO B 65 ALA B 68
SITE 2 AD7 8 ASP B 69 GLU B 70 LEU B 140 GLY B 141
SITE 1 AD8 5 ALA B 271 ALA B 272 TRP B 294 ARG B 297
SITE 2 AD8 5 HOH B 551
SITE 1 AD9 9 VAL A 46 VAL B 46 ASN B 48 ARG B 61
SITE 2 AD9 9 HOH B 509 HOH B 577 HOH B 585 HOH B 618
SITE 3 AD9 9 HOH B 620
SITE 1 AE1 6 ALA B 166 GLY B 171 PRO B 172 LEU B 174
SITE 2 AE1 6 GLY B 237 ALA B 239
CRYST1 118.943 153.586 44.243 90.00 90.00 90.00 P 21 21 2 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 0.008407 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006511 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022602 0.00000
TER 2323 GLU A 309
TER 4706 HIS B 315
MASTER 354 0 19 26 16 0 36 6 5378 2 187 50
END |