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HEADER HYDROLASE 07-JAN-13 4INZ
TITLE THE CRYSTAL STRUCTURE OF M145A MUTANT OF AN EPOXIDE HYDROLASE FROM
TITLE 2 BACILLUS MEGATERIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOLUBLE EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.2.2.10;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 STRAIN: ECU1001 ISOLATE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS A/B HYDROLASE FOLD, ENZYMATIC RESOLUTION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.D.KONG,J.H.ZHOU,J.H.XU
REVDAT 1 12-FEB-14 4INZ 0
JRNL AUTH X.D.KONG,J.H.ZHOU,J.H.XU
JRNL TITL CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE FROM BACILLUS
JRNL TITL 2 MEGATERIUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_637)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 64070
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3246
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 36.9498 - 4.8311 0.91 2703 142 0.1997 0.2055
REMARK 3 2 4.8311 - 3.8359 0.85 2391 140 0.1561 0.1744
REMARK 3 3 3.8359 - 3.3514 0.94 2588 156 0.1577 0.1961
REMARK 3 4 3.3514 - 3.0451 0.99 2745 121 0.1673 0.2154
REMARK 3 5 3.0451 - 2.8270 0.99 2729 153 0.1676 0.2110
REMARK 3 6 2.8270 - 2.6603 0.99 2712 138 0.1559 0.2060
REMARK 3 7 2.6603 - 2.5271 0.99 2739 153 0.1394 0.2119
REMARK 3 8 2.5271 - 2.4171 0.99 2725 128 0.1396 0.2216
REMARK 3 9 2.4171 - 2.3241 0.99 2711 139 0.1313 0.1947
REMARK 3 10 2.3241 - 2.2439 0.99 2658 176 0.1216 0.1920
REMARK 3 11 2.2439 - 2.1738 0.99 2686 131 0.1201 0.2013
REMARK 3 12 2.1738 - 2.1116 0.99 2710 127 0.1264 0.1817
REMARK 3 13 2.1116 - 2.0561 0.98 2646 165 0.1209 0.2378
REMARK 3 14 2.0561 - 2.0059 0.99 2684 130 0.1204 0.1983
REMARK 3 15 2.0059 - 1.9603 0.98 2674 156 0.1230 0.1939
REMARK 3 16 1.9603 - 1.9186 0.98 2650 138 0.1307 0.2265
REMARK 3 17 1.9186 - 1.8802 0.97 2597 154 0.1368 0.2501
REMARK 3 18 1.8802 - 1.8447 0.97 2627 137 0.1696 0.2560
REMARK 3 19 1.8447 - 1.8118 0.97 2607 153 0.1848 0.2532
REMARK 3 20 1.8118 - 1.7811 0.97 2634 126 0.2155 0.2839
REMARK 3 21 1.7811 - 1.7523 0.95 2586 129 0.2461 0.2890
REMARK 3 22 1.7523 - 1.7254 0.94 2515 126 0.2666 0.3252
REMARK 3 23 1.7254 - 1.7000 0.92 2507 128 0.2929 0.3808
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 42.74
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.020
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) : -1.21440
REMARK 3 B22 (A**2) : 3.89260
REMARK 3 B33 (A**2) : -2.67830
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 : 0.005 4893
REMARK 3 ANGLE : 0.939 6640
REMARK 3 CHIRALITY : 0.071 681
REMARK 3 PLANARITY : 0.004 871
REMARK 3 DIHEDRAL : 13.351 1815
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 4INZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB076990.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 416525
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : 0.07300
REMARK 200 FOR THE DATA SET : 16.0920
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.43900
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: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 34% PEG 3000, 0.2M LITHIUM
REMARK 280 SULFATE , PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 31.91450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.01700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.82550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.01700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.91450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.82550
REMARK 290 SMTRY3 4 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 GLY A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 MET A -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MET A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 GLN A -6
REMARK 465 GLN A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 HIS B -14
REMARK 465 MET B -13
REMARK 465 ALA B -12
REMARK 465 SER B -11
REMARK 465 MET B -10
REMARK 465 THR B -9
REMARK 465 GLY B -8
REMARK 465 GLY B -7
REMARK 465 GLN B -6
REMARK 465 GLN B -5
REMARK 465 MET B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
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 PRO A 31 44.92 -106.94
REMARK 500 ASP A 32 -154.08 -90.44
REMARK 500 PHE A 33 -169.70 -173.23
REMARK 500 ASN A 59 -121.33 48.62
REMARK 500 ASP A 97 -126.00 59.16
REMARK 500 LYS A 207 72.66 -112.12
REMARK 500 ASN A 256 69.76 -101.30
REMARK 500 SER A 266 -131.71 -104.27
REMARK 500 PRO B 31 47.92 -106.95
REMARK 500 ASP B 32 -156.89 -90.51
REMARK 500 PHE B 33 -170.88 -170.59
REMARK 500 ASN B 59 -122.12 50.32
REMARK 500 ASP B 97 -129.69 61.69
REMARK 500 LYS B 207 71.33 -116.81
REMARK 500 SER B 266 -132.15 -105.74
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 542 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH B 599 DISTANCE = 5.77 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G00 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WILD TYPE ENZYME
REMARK 900 RELATED ID: 4G02 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WILD TYPE ENZYME COMPLEXED WITH A
REMARK 900 SUBSTRATE ANALOGUE
REMARK 900 RELATED ID: 4IO0 RELATED DB: PDB
DBREF 4INZ A 1 287 UNP G9BEX6 G9BEX6_BACME 1 287
DBREF 4INZ B 1 287 UNP G9BEX6 G9BEX6_BACME 1 287
SEQADV 4INZ GLY A -16 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ SER A -15 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ HIS A -14 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ MET A -13 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ ALA A -12 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ SER A -11 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ MET A -10 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ THR A -9 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLY A -8 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLY A -7 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLN A -6 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLN A -5 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ MET A -4 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLY A -3 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ ARG A -2 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLY A -1 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ SER A 0 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ ALA A 145 UNP G9BEX6 MET 145 ENGINEERED MUTATION
SEQADV 4INZ GLY B -16 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ SER B -15 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ HIS B -14 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ MET B -13 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ ALA B -12 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ SER B -11 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ MET B -10 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ THR B -9 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLY B -8 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLY B -7 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLN B -6 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLN B -5 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ MET B -4 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLY B -3 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ ARG B -2 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ GLY B -1 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ SER B 0 UNP G9BEX6 EXPRESSION TAG
SEQADV 4INZ ALA B 145 UNP G9BEX6 MET 145 ENGINEERED MUTATION
SEQRES 1 A 304 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 A 304 GLY ARG GLY SER MET SER LYS GLN TYR ILE ASN VAL ASN
SEQRES 3 A 304 GLY VAL ASN LEU HIS TYR ILE SER LYS GLY GLN GLY GLU
SEQRES 4 A 304 LEU MET LEU PHE LEU HIS GLY PHE PRO ASP PHE SER HIS
SEQRES 5 A 304 ILE TRP ARG HIS GLN ILE ASP GLU PHE SER ASN ASP PHE
SEQRES 6 A 304 HIS THR VAL ALA LEU ASP LEU ARG GLY TYR ASN LEU SER
SEQRES 7 A 304 GLU LYS PRO SER GLY LEU GLU SER TYR GLU ILE ASP VAL
SEQRES 8 A 304 LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU GLY LEU GLY
SEQRES 9 A 304 TYR SER SER CYS THR LEU VAL VAL HIS ASP TRP GLY ALA
SEQRES 10 A 304 GLY ILE GLY TRP THR PHE ALA TYR ARG TYR PRO GLU TYR
SEQRES 11 A 304 VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO HIS PRO TYR
SEQRES 12 A 304 THR PHE MET ARG GLU LEU ARG THR ASN LYS ASN GLN GLN
SEQRES 13 A 304 LYS ALA SER GLU TYR ALA LYS TRP PHE GLN LYS GLN GLU
SEQRES 14 A 304 VAL GLN ASP TYR MET GLU ARG ASP ASN PHE SER GLY LEU
SEQRES 15 A 304 ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS LYS GLY TYR
SEQRES 16 A 304 LEU THR ALA ASP ASP VAL GLN ALA TYR MET ASN SER TRP
SEQRES 17 A 304 GLU ASN GLY SER VAL LEU SER MET LEU SER TYR TYR ARG
SEQRES 18 A 304 ASN LEU LYS ILE PHE THR GLU GLU ASP LEU ARG ARG LYS
SEQRES 19 A 304 SER LEU PHE PRO LEU GLU GLU GLU VAL LEU ASN ILE PRO
SEQRES 20 A 304 VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO THR PHE MET
SEQRES 21 A 304 PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR VAL PRO ASN
SEQRES 22 A 304 ILE SER VAL HIS ARG LEU ALA GLU ALA SER HIS ALA PRO
SEQRES 23 A 304 GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN VAL MET TRP
SEQRES 24 A 304 ASN PHE LEU ASN LYS
SEQRES 1 B 304 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 B 304 GLY ARG GLY SER MET SER LYS GLN TYR ILE ASN VAL ASN
SEQRES 3 B 304 GLY VAL ASN LEU HIS TYR ILE SER LYS GLY GLN GLY GLU
SEQRES 4 B 304 LEU MET LEU PHE LEU HIS GLY PHE PRO ASP PHE SER HIS
SEQRES 5 B 304 ILE TRP ARG HIS GLN ILE ASP GLU PHE SER ASN ASP PHE
SEQRES 6 B 304 HIS THR VAL ALA LEU ASP LEU ARG GLY TYR ASN LEU SER
SEQRES 7 B 304 GLU LYS PRO SER GLY LEU GLU SER TYR GLU ILE ASP VAL
SEQRES 8 B 304 LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU GLY LEU GLY
SEQRES 9 B 304 TYR SER SER CYS THR LEU VAL VAL HIS ASP TRP GLY ALA
SEQRES 10 B 304 GLY ILE GLY TRP THR PHE ALA TYR ARG TYR PRO GLU TYR
SEQRES 11 B 304 VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO HIS PRO TYR
SEQRES 12 B 304 THR PHE MET ARG GLU LEU ARG THR ASN LYS ASN GLN GLN
SEQRES 13 B 304 LYS ALA SER GLU TYR ALA LYS TRP PHE GLN LYS GLN GLU
SEQRES 14 B 304 VAL GLN ASP TYR MET GLU ARG ASP ASN PHE SER GLY LEU
SEQRES 15 B 304 ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS LYS GLY TYR
SEQRES 16 B 304 LEU THR ALA ASP ASP VAL GLN ALA TYR MET ASN SER TRP
SEQRES 17 B 304 GLU ASN GLY SER VAL LEU SER MET LEU SER TYR TYR ARG
SEQRES 18 B 304 ASN LEU LYS ILE PHE THR GLU GLU ASP LEU ARG ARG LYS
SEQRES 19 B 304 SER LEU PHE PRO LEU GLU GLU GLU VAL LEU ASN ILE PRO
SEQRES 20 B 304 VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO THR PHE MET
SEQRES 21 B 304 PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR VAL PRO ASN
SEQRES 22 B 304 ILE SER VAL HIS ARG LEU ALA GLU ALA SER HIS ALA PRO
SEQRES 23 B 304 GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN VAL MET TRP
SEQRES 24 B 304 ASN PHE LEU ASN LYS
HET EDO A 301 4
HET PEG A 302 7
HET PEG B 301 7
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO C2 H6 O2
FORMUL 4 PEG 2(C4 H10 O3)
FORMUL 6 HOH *394(H2 O)
HELIX 1 1 PHE A 33 ILE A 36 5 4
HELIX 2 2 TRP A 37 SER A 45 1 9
HELIX 3 3 GLY A 66 TYR A 70 5 5
HELIX 4 4 GLU A 71 LEU A 86 1 16
HELIX 5 5 ASP A 97 TYR A 110 1 14
HELIX 6 6 HIS A 124 ASN A 135 1 12
HELIX 7 7 ASN A 135 SER A 142 1 8
HELIX 8 8 SER A 142 PHE A 148 1 7
HELIX 9 9 GLN A 149 GLN A 151 5 3
HELIX 10 10 GLU A 152 VAL A 169 1 18
HELIX 11 11 VAL A 169 LYS A 176 1 8
HELIX 12 12 THR A 180 GLY A 194 1 15
HELIX 13 13 SER A 195 ARG A 204 1 10
HELIX 14 14 THR A 210 ARG A 215 1 6
HELIX 15 15 MET A 243 ASP A 248 5 6
HELIX 16 16 GLY A 249 TYR A 253 5 5
HELIX 17 17 ALA A 268 LYS A 273 1 6
HELIX 18 18 LYS A 273 LYS A 287 1 15
HELIX 19 19 PHE B 33 ILE B 36 5 4
HELIX 20 20 TRP B 37 SER B 45 1 9
HELIX 21 21 GLY B 66 TYR B 70 5 5
HELIX 22 22 GLU B 71 LEU B 86 1 16
HELIX 23 23 ASP B 97 TYR B 110 1 14
HELIX 24 24 HIS B 124 ASN B 135 1 12
HELIX 25 25 ASN B 135 SER B 142 1 8
HELIX 26 26 GLU B 143 PHE B 148 1 6
HELIX 27 27 GLN B 151 LYS B 176 1 26
HELIX 28 28 THR B 180 GLY B 194 1 15
HELIX 29 29 SER B 195 ASN B 205 1 11
HELIX 30 30 THR B 210 ARG B 215 1 6
HELIX 31 31 MET B 243 ASP B 248 5 6
HELIX 32 32 GLY B 249 TYR B 253 5 5
HELIX 33 33 ALA B 268 LYS B 273 1 6
HELIX 34 34 LYS B 273 LYS B 287 1 15
SHEET 1 A 8 LYS A 3 VAL A 8 0
SHEET 2 A 8 VAL A 11 GLY A 19 -1 O VAL A 11 N VAL A 8
SHEET 3 A 8 HIS A 49 LEU A 53 -1 O ALA A 52 N ILE A 16
SHEET 4 A 8 LEU A 23 LEU A 27 1 N PHE A 26 O VAL A 51
SHEET 5 A 8 CYS A 91 VAL A 95 1 O VAL A 94 N LEU A 25
SHEET 6 A 8 VAL A 114 PHE A 120 1 O ILE A 118 N LEU A 93
SHEET 7 A 8 VAL A 231 GLY A 236 1 O GLN A 232 N ALA A 119
SHEET 8 A 8 ILE A 257 LEU A 262 1 O SER A 258 N ILE A 233
SHEET 1 B 8 TYR B 5 VAL B 8 0
SHEET 2 B 8 VAL B 11 LYS B 18 -1 O LEU B 13 N ILE B 6
SHEET 3 B 8 HIS B 49 LEU B 53 -1 O ALA B 52 N ILE B 16
SHEET 4 B 8 LEU B 23 LEU B 27 1 N PHE B 26 O VAL B 51
SHEET 5 B 8 CYS B 91 VAL B 95 1 O VAL B 94 N LEU B 25
SHEET 6 B 8 VAL B 114 PHE B 120 1 O PHE B 120 N VAL B 95
SHEET 7 B 8 VAL B 231 GLY B 236 1 O GLN B 232 N ALA B 119
SHEET 8 B 8 ILE B 257 LEU B 262 1 O LEU B 262 N TRP B 235
CISPEP 1 PHE A 30 PRO A 31 0 -2.76
CISPEP 2 PHE B 30 PRO B 31 0 -3.14
SITE 1 AC1 3 ARG A 130 ARG A 133 LYS A 176
SITE 1 AC2 4 TRP A 98 PRO A 123 TYR A 203 HOH A 424
SITE 1 AC3 4 TRP B 98 GLY B 101 PRO B 123 HOH B 447
CRYST1 63.829 77.651 120.034 90.00 90.00 90.00 P 21 21 21 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 0.015667 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008331 0.00000
TER 2383 LYS A 287
TER 4742 LYS B 287
MASTER 333 0 3 34 16 0 3 6 5123 2 18 48
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