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HEADER HYDROLASE 13-DEC-13 4NZZ
TITLE CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE FROM 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
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 STRAIN: ECU1001;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS A/B HYDROLASE FOLD, EPOXIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.D.KONG,J.H.ZHOU,J.H.XU
REVDAT 1 29-OCT-14 4NZZ 0
JRNL AUTH X.D.KONG,S.YUAN,L.LI,J.H.XU,J.H.XU,J.H.ZHOU
JRNL TITL ENGINEERING OF AN EPOXIDE HYDROLASE FOR EFFICIENT
JRNL TITL 2 BIORESOLUTION OF BULKY PHARMACO SUBSTRATES
JRNL REF PROC.NATL.ACAD.SCI.USA 2014
JRNL REFN ESSN 1091-6490
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_637)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 57830
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2918
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 35.5909 - 4.8244 0.98 2914 129 0.1515 0.1896
REMARK 3 2 4.8244 - 3.8307 1.00 2804 138 0.1344 0.1597
REMARK 3 3 3.8307 - 3.3469 1.00 2775 141 0.1653 0.2180
REMARK 3 4 3.3469 - 3.0411 1.00 2738 147 0.1989 0.2257
REMARK 3 5 3.0411 - 2.8232 1.00 2747 156 0.2016 0.2471
REMARK 3 6 2.8232 - 2.6568 1.00 2715 167 0.1989 0.2529
REMARK 3 7 2.6568 - 2.5238 1.00 2682 163 0.1972 0.2285
REMARK 3 8 2.5238 - 2.4140 0.99 2727 147 0.1986 0.2654
REMARK 3 9 2.4140 - 2.3210 0.99 2692 136 0.2029 0.2512
REMARK 3 10 2.3210 - 2.2410 0.99 2705 127 0.2031 0.2710
REMARK 3 11 2.2410 - 2.1709 0.99 2661 148 0.2073 0.2539
REMARK 3 12 2.1709 - 2.1089 0.98 2666 143 0.2050 0.2873
REMARK 3 13 2.1089 - 2.0534 0.97 2655 133 0.2134 0.2603
REMARK 3 14 2.0534 - 2.0033 0.97 2618 130 0.2244 0.2777
REMARK 3 15 2.0033 - 1.9577 0.96 2567 140 0.2254 0.2642
REMARK 3 16 1.9577 - 1.9161 0.95 2587 148 0.2234 0.2407
REMARK 3 17 1.9161 - 1.8777 0.93 2488 140 0.2207 0.2753
REMARK 3 18 1.8777 - 1.8423 0.91 2470 116 0.2417 0.3132
REMARK 3 19 1.8423 - 1.8094 0.88 2388 126 0.2674 0.3855
REMARK 3 20 1.8094 - 1.7787 0.84 2201 132 0.3051 0.3716
REMARK 3 21 1.7787 - 1.7500 0.77 2112 111 0.3274 0.3874
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 38.57
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.780
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) : -3.25990
REMARK 3 B22 (A**2) : 9.25800
REMARK 3 B33 (A**2) : -5.99800
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 : 0.007 5006
REMARK 3 ANGLE : 0.995 6804
REMARK 3 CHIRALITY : 0.075 693
REMARK 3 PLANARITY : 0.004 901
REMARK 3 DIHEDRAL : 14.355 1862
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 4NZZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-14.
REMARK 100 THE RCSB ID CODE IS RCSB083868.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59760
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.749
REMARK 200 RESOLUTION RANGE LOW (A) : 64.333
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
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: SAD
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 (%): 38.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M LICL, 0.1M TRIS-HCL, 28% PEG
REMARK 280 6000, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K,
REMARK 280 EVAPORATION
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 32.11550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.40400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.00300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.40400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.11550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.00300
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 MET A -32
REMARK 465 GLY A -31
REMARK 465 SER A -30
REMARK 465 SER A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 HIS A -23
REMARK 465 SER A -22
REMARK 465 SER A -21
REMARK 465 GLY A -20
REMARK 465 LEU A -19
REMARK 465 VAL A -18
REMARK 465 PRO A -17
REMARK 465 ARG A -16
REMARK 465 GLY A -15
REMARK 465 SER A -14
REMARK 465 HIS A -13
REMARK 465 MET A -12
REMARK 465 ALA A -11
REMARK 465 SER A -10
REMARK 465 MET A -9
REMARK 465 THR A -8
REMARK 465 GLY A -7
REMARK 465 GLY A -6
REMARK 465 GLN A -5
REMARK 465 GLN A -4
REMARK 465 MET A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 GLY A 0
REMARK 465 MET B -32
REMARK 465 GLY B -31
REMARK 465 SER B -30
REMARK 465 SER B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 HIS B -25
REMARK 465 HIS B -24
REMARK 465 HIS B -23
REMARK 465 SER B -22
REMARK 465 SER B -21
REMARK 465 GLY B -20
REMARK 465 LEU B -19
REMARK 465 VAL B -18
REMARK 465 PRO B -17
REMARK 465 ARG B -16
REMARK 465 GLY B -15
REMARK 465 SER B -14
REMARK 465 HIS B -13
REMARK 465 MET B -12
REMARK 465 ALA B -11
REMARK 465 SER B -10
REMARK 465 MET B -9
REMARK 465 THR B -8
REMARK 465 GLY B -7
REMARK 465 GLY B -6
REMARK 465 GLN B -5
REMARK 465 GLN B -4
REMARK 465 MET B -3
REMARK 465 GLY B -2
REMARK 465 ARG B -1
REMARK 465 GLY B 0
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 43.87 -108.32
REMARK 500 ASP A 32 -158.94 -87.75
REMARK 500 ASN A 59 -117.55 45.94
REMARK 500 LYS A 63 78.16 -118.74
REMARK 500 ASP A 97 -133.50 58.65
REMARK 500 LYS A 207 68.89 -110.87
REMARK 500 SER A 266 -131.77 -107.21
REMARK 500 PRO B 31 43.91 -106.56
REMARK 500 ASP B 32 -155.70 -92.57
REMARK 500 PHE B 33 -169.22 -169.61
REMARK 500 ASN B 59 -119.41 50.06
REMARK 500 ASP B 97 -129.97 58.27
REMARK 500 LYS B 207 73.07 -111.00
REMARK 500 SER B 266 -136.41 -107.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O08 RELATED DB: PDB
DBREF 4NZZ A 1 287 UNP G9BEX6 G9BEX6_BACME 1 287
DBREF 4NZZ B 1 287 UNP G9BEX6 G9BEX6_BACME 1 287
SEQADV 4NZZ MET A -32 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY A -31 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER A -30 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER A -29 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS A -28 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS A -27 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS A -26 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS A -25 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS A -24 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS A -23 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER A -22 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER A -21 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY A -20 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ LEU A -19 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ VAL A -18 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ PRO A -17 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ ARG A -16 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY A -15 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER A -14 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS A -13 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ MET A -12 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ ALA A -11 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER A -10 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ MET A -9 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ THR A -8 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY A -7 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY A -6 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLN A -5 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLN A -4 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ MET A -3 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY A -2 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ ARG A -1 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY A 0 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ MET B -32 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY B -31 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER B -30 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER B -29 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS B -28 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS B -27 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS B -26 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS B -25 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS B -24 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS B -23 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER B -22 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER B -21 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY B -20 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ LEU B -19 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ VAL B -18 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ PRO B -17 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ ARG B -16 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY B -15 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER B -14 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ HIS B -13 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ MET B -12 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ ALA B -11 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ SER B -10 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ MET B -9 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ THR B -8 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY B -7 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY B -6 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLN B -5 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLN B -4 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ MET B -3 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY B -2 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ ARG B -1 UNP G9BEX6 EXPRESSION TAG
SEQADV 4NZZ GLY B 0 UNP G9BEX6 EXPRESSION TAG
SEQRES 1 A 320 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 320 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 320 GLY GLN GLN MET GLY ARG GLY MET SER LYS GLN TYR ILE
SEQRES 4 A 320 ASN VAL ASN GLY VAL ASN LEU HIS TYR ILE SER LYS GLY
SEQRES 5 A 320 GLN GLY GLU LEU MET LEU PHE LEU HIS GLY PHE PRO ASP
SEQRES 6 A 320 PHE SER HIS ILE TRP ARG HIS GLN ILE ASP GLU PHE SER
SEQRES 7 A 320 ASN ASP PHE HIS THR VAL ALA LEU ASP LEU ARG GLY TYR
SEQRES 8 A 320 ASN LEU SER GLU LYS PRO SER GLY LEU GLU SER TYR GLU
SEQRES 9 A 320 ILE ASP VAL LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU
SEQRES 10 A 320 GLY LEU GLY TYR SER SER CYS THR LEU VAL VAL HIS ASP
SEQRES 11 A 320 TRP GLY ALA GLY ILE GLY TRP THR PHE ALA TYR ARG TYR
SEQRES 12 A 320 PRO GLU TYR VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO
SEQRES 13 A 320 HIS PRO TYR THR PHE MET ARG GLU LEU ARG THR ASN LYS
SEQRES 14 A 320 ASN GLN GLN LYS ALA SER GLU TYR MET LYS TRP PHE GLN
SEQRES 15 A 320 LYS GLN GLU VAL GLN ASP TYR MET GLU ARG ASP ASN PHE
SEQRES 16 A 320 SER GLY LEU ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS
SEQRES 17 A 320 LYS GLY TYR LEU THR ALA ASP ASP VAL GLN ALA TYR MET
SEQRES 18 A 320 ASN SER TRP GLU ASN GLY SER VAL LEU SER MET LEU SER
SEQRES 19 A 320 TYR TYR ARG ASN LEU LYS ILE PHE THR GLU GLU ASP LEU
SEQRES 20 A 320 ARG ARG LYS SER LEU PHE PRO LEU GLU GLU GLU VAL LEU
SEQRES 21 A 320 ASN ILE PRO VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO
SEQRES 22 A 320 THR PHE MET PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR
SEQRES 23 A 320 VAL PRO ASN ILE SER VAL HIS ARG LEU ALA GLU ALA SER
SEQRES 24 A 320 HIS ALA PRO GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN
SEQRES 25 A 320 VAL MET TRP ASN PHE LEU ASN LYS
SEQRES 1 B 320 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 320 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 B 320 GLY GLN GLN MET GLY ARG GLY MET SER LYS GLN TYR ILE
SEQRES 4 B 320 ASN VAL ASN GLY VAL ASN LEU HIS TYR ILE SER LYS GLY
SEQRES 5 B 320 GLN GLY GLU LEU MET LEU PHE LEU HIS GLY PHE PRO ASP
SEQRES 6 B 320 PHE SER HIS ILE TRP ARG HIS GLN ILE ASP GLU PHE SER
SEQRES 7 B 320 ASN ASP PHE HIS THR VAL ALA LEU ASP LEU ARG GLY TYR
SEQRES 8 B 320 ASN LEU SER GLU LYS PRO SER GLY LEU GLU SER TYR GLU
SEQRES 9 B 320 ILE ASP VAL LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU
SEQRES 10 B 320 GLY LEU GLY TYR SER SER CYS THR LEU VAL VAL HIS ASP
SEQRES 11 B 320 TRP GLY ALA GLY ILE GLY TRP THR PHE ALA TYR ARG TYR
SEQRES 12 B 320 PRO GLU TYR VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO
SEQRES 13 B 320 HIS PRO TYR THR PHE MET ARG GLU LEU ARG THR ASN LYS
SEQRES 14 B 320 ASN GLN GLN LYS ALA SER GLU TYR MET LYS TRP PHE GLN
SEQRES 15 B 320 LYS GLN GLU VAL GLN ASP TYR MET GLU ARG ASP ASN PHE
SEQRES 16 B 320 SER GLY LEU ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS
SEQRES 17 B 320 LYS GLY TYR LEU THR ALA ASP ASP VAL GLN ALA TYR MET
SEQRES 18 B 320 ASN SER TRP GLU ASN GLY SER VAL LEU SER MET LEU SER
SEQRES 19 B 320 TYR TYR ARG ASN LEU LYS ILE PHE THR GLU GLU ASP LEU
SEQRES 20 B 320 ARG ARG LYS SER LEU PHE PRO LEU GLU GLU GLU VAL LEU
SEQRES 21 B 320 ASN ILE PRO VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO
SEQRES 22 B 320 THR PHE MET PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR
SEQRES 23 B 320 VAL PRO ASN ILE SER VAL HIS ARG LEU ALA GLU ALA SER
SEQRES 24 B 320 HIS ALA PRO GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN
SEQRES 25 B 320 VAL MET TRP ASN PHE LEU ASN LYS
FORMUL 3 HOH *414(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 GLU A 152 LYS A 176 1 25
HELIX 10 10 THR A 180 GLY A 194 1 15
HELIX 11 11 SER A 195 TYR A 202 1 8
HELIX 12 12 TYR A 203 LEU A 206 5 4
HELIX 13 13 MET A 243 ASP A 248 5 6
HELIX 14 14 GLY A 249 TYR A 253 5 5
HELIX 15 15 ALA A 268 LYS A 273 1 6
HELIX 16 16 LYS A 273 LYS A 287 1 15
HELIX 17 17 PHE B 33 ILE B 36 5 4
HELIX 18 18 TRP B 37 SER B 45 1 9
HELIX 19 19 GLY B 66 TYR B 70 5 5
HELIX 20 20 GLU B 71 LEU B 86 1 16
HELIX 21 21 ASP B 97 TYR B 110 1 14
HELIX 22 22 HIS B 124 ASN B 135 1 12
HELIX 23 23 ASN B 135 SER B 142 1 8
HELIX 24 24 SER B 142 PHE B 148 1 7
HELIX 25 25 GLN B 149 GLN B 151 5 3
HELIX 26 26 GLU B 152 LYS B 176 1 25
HELIX 27 27 THR B 180 GLY B 194 1 15
HELIX 28 28 SER B 195 ARG B 204 1 10
HELIX 29 29 THR B 210 ARG B 215 1 6
HELIX 30 30 MET B 243 ASP B 248 5 6
HELIX 31 31 GLY B 249 TYR B 253 5 5
HELIX 32 32 ALA B 268 LYS B 273 1 6
HELIX 33 33 LYS B 273 ASN B 286 1 14
SHEET 1 A 8 SER A 2 VAL A 8 0
SHEET 2 A 8 VAL A 11 LYS A 18 -1 O LEU A 13 N ILE A 6
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 THR A 92 N LEU A 23
SHEET 6 A 8 VAL A 114 ALA A 119 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 LEU A 117
SHEET 8 A 8 ILE A 257 LEU A 262 1 O LEU A 262 N TRP A 235
SHEET 1 B 8 SER B 2 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 MET B 24 O VAL B 51
SHEET 5 B 8 CYS B 91 VAL B 95 1 O THR B 92 N LEU B 23
SHEET 6 B 8 VAL B 114 ALA B 119 1 O ILE B 118 N LEU B 93
SHEET 7 B 8 VAL B 231 GLY B 236 1 O ILE B 234 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 -3.42
CISPEP 2 PHE B 30 PRO B 31 0 -2.88
CRYST1 64.231 76.006 120.808 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 0.015569 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013157 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008278 0.00000
TER 2433 LYS A 287
TER 4852 LYS B 287
MASTER 327 0 0 33 16 0 0 6 5162 2 0 50
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