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HEADER HYDROLASE 30-MAY-24 9C2G
TITLE ISOBUTYLENE EPOXIDE HYDROLASE FROM MYCOLICIBACTERIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOBUTYLENE EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.3.23.10;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOLICIBACTERIUM;
SOURCE 3 ORGANISM_TAXID: 1547487;
SOURCE 4 STRAIN: ELW1;
SOURCE 5 GENE: IBCK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A+
KEYWDS BACTERIAL EPOXIDE HYDROLASE, 2-METHYLPROPENE (ISOBUTYLENE),
KEYWDS 2 ALPHA/BETA HYDROLASE FOLD, SOLUBLE EPOXIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.B.ROSE,P.SWARTZ,N.W.FAULKNER
REVDAT 1 01-OCT-25 9C2G 0
JRNL AUTH N.W.FAULKNER,J.B.JOYCE,C.SMITH,P.SWARTZ,R.B.ROSE,E.S.MILLER,
JRNL AUTH 2 M.R.HYMAN
JRNL TITL CHARACTERIZATION OF AN ISOBUTYLENE EPOXIDE HYDROLASE (IBCK)
JRNL TITL 2 FROM THE ISOBUTYLENE-CATABOLIZING BACTERIUM
JRNL TITL 3 MYCOLICIBACTERIUM SP. ELW1.
JRNL REF APPL.ENVIRON.MICROBIOL. V. 91 39325 2025
JRNL REFN ESSN 1098-5336
JRNL PMID 40856435
JRNL DOI 10.1128/AEM.00393-25
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21_5207
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 80736
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.460
REMARK 3 FREE R VALUE TEST SET COUNT : 1990
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 47.3000 - 5.5200 0.99 6587 166 0.1733 0.2229
REMARK 3 2 5.5100 - 4.3800 0.99 6260 157 0.1400 0.1548
REMARK 3 3 4.3800 - 3.8300 0.98 6159 157 0.1414 0.2046
REMARK 3 4 3.8300 - 3.4800 0.98 6065 153 0.1595 0.2041
REMARK 3 5 3.4800 - 3.2300 0.95 5859 148 0.1829 0.2314
REMARK 3 6 3.2300 - 3.0400 0.91 5674 144 0.2104 0.2528
REMARK 3 7 3.0400 - 2.8900 0.90 5530 139 0.2201 0.3074
REMARK 3 8 2.8800 - 2.7600 0.88 5468 138 0.2051 0.2600
REMARK 3 9 2.7600 - 2.6500 0.87 5361 137 0.2122 0.2670
REMARK 3 10 2.6500 - 2.5600 0.87 5306 134 0.2234 0.3083
REMARK 3 11 2.5600 - 2.4800 0.86 5313 135 0.2224 0.3139
REMARK 3 12 2.4800 - 2.4100 0.85 5173 131 0.2186 0.2961
REMARK 3 13 2.4100 - 2.3500 0.84 5200 132 0.2224 0.2255
REMARK 3 14 2.3500 - 2.2900 0.79 4791 119 0.2247 0.2922
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 : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.904
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.76
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 : 0.003 14637
REMARK 3 ANGLE : 0.567 19936
REMARK 3 CHIRALITY : 0.043 2114
REMARK 3 PLANARITY : 0.005 2563
REMARK 3 DIHEDRAL : 13.759 5131
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0351 -16.0724 26.4064
REMARK 3 T TENSOR
REMARK 3 T11: 0.2546 T22: 0.3235
REMARK 3 T33: 0.2992 T12: -0.0070
REMARK 3 T13: 0.0472 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.1893 L22: 0.3727
REMARK 3 L33: 0.1806 L12: -0.0451
REMARK 3 L13: -0.0563 L23: 0.1467
REMARK 3 S TENSOR
REMARK 3 S11: 0.0453 S12: -0.0162 S13: 0.0663
REMARK 3 S21: -0.1299 S22: 0.0318 S23: -0.0238
REMARK 3 S31: -0.1341 S32: 0.0109 S33: -0.0781
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 9C2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1000283962.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-AUG-16
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 : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81304
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 47.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.63400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M MGSO4, 0.1 M MES:NAOH, PH 6.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 24.20850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.86000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.50250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.86000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.20850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.50250
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, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -96.83400
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 90.50250
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 110.86000
REMARK 350
REMARK 350 BIOMOLECULE: 3
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: 2800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 THR A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 PHE A 7
REMARK 465 ALA A 8
REMARK 465 THR A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
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 465 THR B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 PHE B 7
REMARK 465 ALA B 8
REMARK 465 THR B 9
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 THR C 3
REMARK 465 ALA C 4
REMARK 465 SER C 5
REMARK 465 SER C 6
REMARK 465 PHE C 7
REMARK 465 ALA C 8
REMARK 465 THR C 9
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 THR D 3
REMARK 465 ALA D 4
REMARK 465 SER D 5
REMARK 465 SER D 6
REMARK 465 PHE D 7
REMARK 465 ALA D 8
REMARK 465 THR D 9
REMARK 465 PRO D 10
REMARK 465 LYS D 303
REMARK 465 MET E -19
REMARK 465 GLY E -18
REMARK 465 SER E -17
REMARK 465 SER E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 HIS E -10
REMARK 465 SER E -9
REMARK 465 SER E -8
REMARK 465 GLY E -7
REMARK 465 LEU E -6
REMARK 465 VAL E -5
REMARK 465 PRO E -4
REMARK 465 ARG E -3
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 MET E 1
REMARK 465 THR E 2
REMARK 465 THR E 3
REMARK 465 ALA E 4
REMARK 465 SER E 5
REMARK 465 SER E 6
REMARK 465 PHE E 7
REMARK 465 ALA E 8
REMARK 465 THR E 9
REMARK 465 PRO E 10
REMARK 465 MET F -19
REMARK 465 GLY F -18
REMARK 465 SER F -17
REMARK 465 SER F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 HIS F -10
REMARK 465 SER F -9
REMARK 465 SER F -8
REMARK 465 GLY F -7
REMARK 465 LEU F -6
REMARK 465 VAL F -5
REMARK 465 PRO F -4
REMARK 465 ARG F -3
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 THR F 3
REMARK 465 ALA F 4
REMARK 465 SER F 5
REMARK 465 SER F 6
REMARK 465 PHE F 7
REMARK 465 ALA F 8
REMARK 465 THR F 9
REMARK 465 PRO F 10
REMARK 465 ALA F 11
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 149 CG CD OE1 OE2
REMARK 470 GLU A 198 CG CD OE1 OE2
REMARK 470 LYS A 269 CE NZ
REMARK 470 GLU A 280 CD OE1 OE2
REMARK 470 VAL B 12 CG1 CG2
REMARK 470 ARG B 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 16 CG CD OE1 OE2
REMARK 470 ASN B 21 CG OD1 ND2
REMARK 470 LYS B 269 CE NZ
REMARK 470 LYS B 303 CE NZ
REMARK 470 ARG C 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 16 CG CD OE1 OE2
REMARK 470 GLU C 17 CG CD OE1 OE2
REMARK 470 GLU C 149 CG CD OE1 OE2
REMARK 470 GLU C 242 CG CD OE1 OE2
REMARK 470 LYS D 129 CE NZ
REMARK 470 LYS D 269 CD CE NZ
REMARK 470 GLU D 296 CD OE1 OE2
REMARK 470 ARG E 14 CG CD NE CZ NH1 NH2
REMARK 470 ASN E 21 CG OD1 ND2
REMARK 470 GLU E 22 CG CD OE1 OE2
REMARK 470 ILE E 23 CG1 CG2 CD1
REMARK 470 LEU E 25 CG CD1 CD2
REMARK 470 LYS E 30 CG CD CE NZ
REMARK 470 ILE E 31 CG1 CG2 CD1
REMARK 470 LYS E 81 CD CE NZ
REMARK 470 GLU E 105 OE1 OE2
REMARK 470 ILE E 108 CG1 CG2 CD1
REMARK 470 GLU E 110 CG CD OE1 OE2
REMARK 470 GLU E 149 CG CD OE1 OE2
REMARK 470 LYS E 183 CG CD CE NZ
REMARK 470 TYR E 208 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS E 214 CG CD CE NZ
REMARK 470 GLU E 238 CG CD OE1 OE2
REMARK 470 GLU E 296 CG CD OE1 OE2
REMARK 470 LYS E 303 CE NZ
REMARK 470 GLU F 16 CB CG CD OE1 OE2
REMARK 470 ILE F 23 CG1 CG2 CD1
REMARK 470 LYS F 30 CG CD CE NZ
REMARK 470 GLU F 64 CG CD OE1 OE2
REMARK 470 LEU F 84 CG CD1 CD2
REMARK 470 GLU F 105 OE1 OE2
REMARK 470 LYS F 129 NZ
REMARK 470 GLU F 149 CG CD OE1 OE2
REMARK 470 LYS F 183 CG CD CE NZ
REMARK 470 LYS F 214 CG CD CE NZ
REMARK 470 GLU F 238 CD OE1 OE2
REMARK 470 LEU F 239 CG CD1 CD2
REMARK 470 GLU F 242 CG CD OE1 OE2
REMARK 470 GLU F 296 CG CD OE1 OE2
REMARK 470 LYS F 303 CG CD CE NZ
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 HH21 ARG E 35 OD2 ASP E 67 1.57
REMARK 500 HZ3 LYS A 183 OD1 ASP A 202 1.58
REMARK 500 OD1 ASP E 104 HH22 ARG E 133 1.59
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 83 107.56 -29.75
REMARK 500 ASP A 117 -132.02 54.68
REMARK 500 ASN A 273 82.50 -154.41
REMARK 500 PHE A 285 76.75 -116.41
REMARK 500 PHE A 302 41.35 -91.14
REMARK 500 ALA B 11 -1.67 -150.11
REMARK 500 GLU B 17 33.05 -89.89
REMARK 500 ASP B 83 113.45 -21.59
REMARK 500 ASP B 117 -130.84 56.51
REMARK 500 ASN B 132 -14.89 -49.69
REMARK 500 ASN B 273 76.19 -155.33
REMARK 500 PHE B 285 76.81 -117.59
REMARK 500 PHE B 302 41.63 -90.09
REMARK 500 PHE C 51 -173.50 -175.57
REMARK 500 ASP C 83 112.36 -34.77
REMARK 500 ASP C 117 -132.62 57.85
REMARK 500 ILE C 135 -70.64 -97.21
REMARK 500 VAL C 259 78.81 -117.87
REMARK 500 PHE C 285 79.19 -114.07
REMARK 500 PHE C 302 76.60 -103.08
REMARK 500 ASP D 83 111.80 -34.17
REMARK 500 ASP D 117 -129.54 56.59
REMARK 500 ILE D 135 -66.21 -92.64
REMARK 500 ASN D 273 61.31 -152.80
REMARK 500 PHE D 285 72.44 -118.89
REMARK 500 PRO E 82 175.39 -52.08
REMARK 500 ASP E 83 102.26 -39.43
REMARK 500 ASP E 117 -125.64 54.75
REMARK 500 ILE E 135 -73.82 -85.83
REMARK 500 VAL E 259 75.21 -116.97
REMARK 500 ASN E 273 76.51 -151.94
REMARK 500 ARG F 74 119.29 -33.42
REMARK 500 PRO F 82 158.29 -47.91
REMARK 500 ASP F 83 106.87 -32.84
REMARK 500 LEU F 84 -5.39 -57.58
REMARK 500 ASP F 117 -133.53 62.91
REMARK 500 ILE F 135 -71.18 -84.70
REMARK 500 ASP F 141 62.85 37.88
REMARK 500 PHE F 302 40.90 -97.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 8K6 A 403
REMARK 610 8K6 B 402
REMARK 610 8K6 C 403
REMARK 610 8K6 D 404
REMARK 610 8K6 E 402
REMARK 610 8K6 F 403
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 191 O
REMARK 620 2 SER A 194 O 84.3
REMARK 620 3 ARG A 196 O 89.9 76.7
REMARK 620 4 HOH A 537 O 171.3 93.5 81.4
REMARK 620 5 HOH A 547 O 103.6 80.2 151.8 84.3
REMARK 620 6 HOH A 571 O 86.7 170.9 101.9 95.2 103.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 194 O
REMARK 620 2 ARG D 196 O 79.4
REMARK 620 3 HOH D 529 O 70.4 144.8
REMARK 620 N 1 2
DBREF 9C2G A -19 303 PDB 9C2G 9C2G -19 303
DBREF 9C2G B -19 303 PDB 9C2G 9C2G -19 303
DBREF 9C2G C -19 303 PDB 9C2G 9C2G -19 303
DBREF 9C2G D -19 303 PDB 9C2G 9C2G -19 303
DBREF 9C2G E -19 303 PDB 9C2G 9C2G -19 303
DBREF 9C2G F -19 303 PDB 9C2G 9C2G -19 303
SEQRES 1 A 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 323 LEU VAL PRO ARG GLY SER HIS MET THR THR ALA SER SER
SEQRES 3 A 323 PHE ALA THR PRO ALA VAL ARG ARG PRO GLU GLU PHE SER
SEQRES 4 A 323 HIS ASN GLU ILE GLN LEU SER THR GLY VAL LYS ILE HIS
SEQRES 5 A 323 TYR VAL ARG GLU GLY SER GLY PRO PRO LEU LEU LEU LEU
SEQRES 6 A 323 HIS GLY TRP PRO GLY PHE TRP TRP GLU TRP SER LYS VAL
SEQRES 7 A 323 VAL ALA PRO LEU ALA GLU HIS PHE ASP VAL ILE VAL PRO
SEQRES 8 A 323 ASP LEU ARG GLY PHE GLY ASP SER GLU LYS PRO ASP LEU
SEQRES 9 A 323 GLY ASP ILE SER GLN TYR THR LEU ASP HIS ALA THR ASP
SEQRES 10 A 323 ASP GLN ALA ALA LEU LEU ASP GLU LEU GLY ILE ASP GLU
SEQRES 11 A 323 ALA TYR VAL VAL GLY HIS ASP TYR ALA ALA ILE ILE VAL
SEQRES 12 A 323 HIS LYS PHE ILE ARG LYS PHE ARG ASN ARG VAL ILE LYS
SEQRES 13 A 323 ALA ALA ILE PHE ASP PRO ILE THR PRO ASP PHE GLY GLU
SEQRES 14 A 323 PHE TYR PHE GLY ILE PRO HIS VAL SER GLU SER TRP TYR
SEQRES 15 A 323 SER GLN PHE HIS GLN THR ASP MET SER VAL GLU LEU VAL
SEQRES 16 A 323 SER SER SER ARG THR ALA CYS LYS ILE TYR PHE THR HIS
SEQRES 17 A 323 PHE MET ASN HIS TRP SER TYR ARG ASP GLU LEU LEU THR
SEQRES 18 A 323 ASP ASP GLU MET GLU ILE TYR VAL ASP ASN PHE MET LYS
SEQRES 19 A 323 ALA GLY ASN ILE HIS GLY GLY PHE ASN TYR TYR ARG ALA
SEQRES 20 A 323 ASN LEU SER MET THR SER ALA PRO TRP ASN GLU LEU ASP
SEQRES 21 A 323 ASP GLU VAL THR ASP LEU PRO VAL THR ILE LEU TRP GLY
SEQRES 22 A 323 GLN GLY ASP THR VAL VAL PRO SER LEU LEU ALA ASP ARG
SEQRES 23 A 323 LEU PRO LYS TYR TYR SER ASN TYR THR LEU GLU ILE VAL
SEQRES 24 A 323 GLU ASP ALA GLY HIS PHE MET MET VAL GLU LYS PRO ASP
SEQRES 25 A 323 ILE VAL ILE GLU ARG LEU THR ALA ALA PHE LYS
SEQRES 1 B 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 323 LEU VAL PRO ARG GLY SER HIS MET THR THR ALA SER SER
SEQRES 3 B 323 PHE ALA THR PRO ALA VAL ARG ARG PRO GLU GLU PHE SER
SEQRES 4 B 323 HIS ASN GLU ILE GLN LEU SER THR GLY VAL LYS ILE HIS
SEQRES 5 B 323 TYR VAL ARG GLU GLY SER GLY PRO PRO LEU LEU LEU LEU
SEQRES 6 B 323 HIS GLY TRP PRO GLY PHE TRP TRP GLU TRP SER LYS VAL
SEQRES 7 B 323 VAL ALA PRO LEU ALA GLU HIS PHE ASP VAL ILE VAL PRO
SEQRES 8 B 323 ASP LEU ARG GLY PHE GLY ASP SER GLU LYS PRO ASP LEU
SEQRES 9 B 323 GLY ASP ILE SER GLN TYR THR LEU ASP HIS ALA THR ASP
SEQRES 10 B 323 ASP GLN ALA ALA LEU LEU ASP GLU LEU GLY ILE ASP GLU
SEQRES 11 B 323 ALA TYR VAL VAL GLY HIS ASP TYR ALA ALA ILE ILE VAL
SEQRES 12 B 323 HIS LYS PHE ILE ARG LYS PHE ARG ASN ARG VAL ILE LYS
SEQRES 13 B 323 ALA ALA ILE PHE ASP PRO ILE THR PRO ASP PHE GLY GLU
SEQRES 14 B 323 PHE TYR PHE GLY ILE PRO HIS VAL SER GLU SER TRP TYR
SEQRES 15 B 323 SER GLN PHE HIS GLN THR ASP MET SER VAL GLU LEU VAL
SEQRES 16 B 323 SER SER SER ARG THR ALA CYS LYS ILE TYR PHE THR HIS
SEQRES 17 B 323 PHE MET ASN HIS TRP SER TYR ARG ASP GLU LEU LEU THR
SEQRES 18 B 323 ASP ASP GLU MET GLU ILE TYR VAL ASP ASN PHE MET LYS
SEQRES 19 B 323 ALA GLY ASN ILE HIS GLY GLY PHE ASN TYR TYR ARG ALA
SEQRES 20 B 323 ASN LEU SER MET THR SER ALA PRO TRP ASN GLU LEU ASP
SEQRES 21 B 323 ASP GLU VAL THR ASP LEU PRO VAL THR ILE LEU TRP GLY
SEQRES 22 B 323 GLN GLY ASP THR VAL VAL PRO SER LEU LEU ALA ASP ARG
SEQRES 23 B 323 LEU PRO LYS TYR TYR SER ASN TYR THR LEU GLU ILE VAL
SEQRES 24 B 323 GLU ASP ALA GLY HIS PHE MET MET VAL GLU LYS PRO ASP
SEQRES 25 B 323 ILE VAL ILE GLU ARG LEU THR ALA ALA PHE LYS
SEQRES 1 C 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 323 LEU VAL PRO ARG GLY SER HIS MET THR THR ALA SER SER
SEQRES 3 C 323 PHE ALA THR PRO ALA VAL ARG ARG PRO GLU GLU PHE SER
SEQRES 4 C 323 HIS ASN GLU ILE GLN LEU SER THR GLY VAL LYS ILE HIS
SEQRES 5 C 323 TYR VAL ARG GLU GLY SER GLY PRO PRO LEU LEU LEU LEU
SEQRES 6 C 323 HIS GLY TRP PRO GLY PHE TRP TRP GLU TRP SER LYS VAL
SEQRES 7 C 323 VAL ALA PRO LEU ALA GLU HIS PHE ASP VAL ILE VAL PRO
SEQRES 8 C 323 ASP LEU ARG GLY PHE GLY ASP SER GLU LYS PRO ASP LEU
SEQRES 9 C 323 GLY ASP ILE SER GLN TYR THR LEU ASP HIS ALA THR ASP
SEQRES 10 C 323 ASP GLN ALA ALA LEU LEU ASP GLU LEU GLY ILE ASP GLU
SEQRES 11 C 323 ALA TYR VAL VAL GLY HIS ASP TYR ALA ALA ILE ILE VAL
SEQRES 12 C 323 HIS LYS PHE ILE ARG LYS PHE ARG ASN ARG VAL ILE LYS
SEQRES 13 C 323 ALA ALA ILE PHE ASP PRO ILE THR PRO ASP PHE GLY GLU
SEQRES 14 C 323 PHE TYR PHE GLY ILE PRO HIS VAL SER GLU SER TRP TYR
SEQRES 15 C 323 SER GLN PHE HIS GLN THR ASP MET SER VAL GLU LEU VAL
SEQRES 16 C 323 SER SER SER ARG THR ALA CYS LYS ILE TYR PHE THR HIS
SEQRES 17 C 323 PHE MET ASN HIS TRP SER TYR ARG ASP GLU LEU LEU THR
SEQRES 18 C 323 ASP ASP GLU MET GLU ILE TYR VAL ASP ASN PHE MET LYS
SEQRES 19 C 323 ALA GLY ASN ILE HIS GLY GLY PHE ASN TYR TYR ARG ALA
SEQRES 20 C 323 ASN LEU SER MET THR SER ALA PRO TRP ASN GLU LEU ASP
SEQRES 21 C 323 ASP GLU VAL THR ASP LEU PRO VAL THR ILE LEU TRP GLY
SEQRES 22 C 323 GLN GLY ASP THR VAL VAL PRO SER LEU LEU ALA ASP ARG
SEQRES 23 C 323 LEU PRO LYS TYR TYR SER ASN TYR THR LEU GLU ILE VAL
SEQRES 24 C 323 GLU ASP ALA GLY HIS PHE MET MET VAL GLU LYS PRO ASP
SEQRES 25 C 323 ILE VAL ILE GLU ARG LEU THR ALA ALA PHE LYS
SEQRES 1 D 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 323 LEU VAL PRO ARG GLY SER HIS MET THR THR ALA SER SER
SEQRES 3 D 323 PHE ALA THR PRO ALA VAL ARG ARG PRO GLU GLU PHE SER
SEQRES 4 D 323 HIS ASN GLU ILE GLN LEU SER THR GLY VAL LYS ILE HIS
SEQRES 5 D 323 TYR VAL ARG GLU GLY SER GLY PRO PRO LEU LEU LEU LEU
SEQRES 6 D 323 HIS GLY TRP PRO GLY PHE TRP TRP GLU TRP SER LYS VAL
SEQRES 7 D 323 VAL ALA PRO LEU ALA GLU HIS PHE ASP VAL ILE VAL PRO
SEQRES 8 D 323 ASP LEU ARG GLY PHE GLY ASP SER GLU LYS PRO ASP LEU
SEQRES 9 D 323 GLY ASP ILE SER GLN TYR THR LEU ASP HIS ALA THR ASP
SEQRES 10 D 323 ASP GLN ALA ALA LEU LEU ASP GLU LEU GLY ILE ASP GLU
SEQRES 11 D 323 ALA TYR VAL VAL GLY HIS ASP TYR ALA ALA ILE ILE VAL
SEQRES 12 D 323 HIS LYS PHE ILE ARG LYS PHE ARG ASN ARG VAL ILE LYS
SEQRES 13 D 323 ALA ALA ILE PHE ASP PRO ILE THR PRO ASP PHE GLY GLU
SEQRES 14 D 323 PHE TYR PHE GLY ILE PRO HIS VAL SER GLU SER TRP TYR
SEQRES 15 D 323 SER GLN PHE HIS GLN THR ASP MET SER VAL GLU LEU VAL
SEQRES 16 D 323 SER SER SER ARG THR ALA CYS LYS ILE TYR PHE THR HIS
SEQRES 17 D 323 PHE MET ASN HIS TRP SER TYR ARG ASP GLU LEU LEU THR
SEQRES 18 D 323 ASP ASP GLU MET GLU ILE TYR VAL ASP ASN PHE MET LYS
SEQRES 19 D 323 ALA GLY ASN ILE HIS GLY GLY PHE ASN TYR TYR ARG ALA
SEQRES 20 D 323 ASN LEU SER MET THR SER ALA PRO TRP ASN GLU LEU ASP
SEQRES 21 D 323 ASP GLU VAL THR ASP LEU PRO VAL THR ILE LEU TRP GLY
SEQRES 22 D 323 GLN GLY ASP THR VAL VAL PRO SER LEU LEU ALA ASP ARG
SEQRES 23 D 323 LEU PRO LYS TYR TYR SER ASN TYR THR LEU GLU ILE VAL
SEQRES 24 D 323 GLU ASP ALA GLY HIS PHE MET MET VAL GLU LYS PRO ASP
SEQRES 25 D 323 ILE VAL ILE GLU ARG LEU THR ALA ALA PHE LYS
SEQRES 1 E 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 323 LEU VAL PRO ARG GLY SER HIS MET THR THR ALA SER SER
SEQRES 3 E 323 PHE ALA THR PRO ALA VAL ARG ARG PRO GLU GLU PHE SER
SEQRES 4 E 323 HIS ASN GLU ILE GLN LEU SER THR GLY VAL LYS ILE HIS
SEQRES 5 E 323 TYR VAL ARG GLU GLY SER GLY PRO PRO LEU LEU LEU LEU
SEQRES 6 E 323 HIS GLY TRP PRO GLY PHE TRP TRP GLU TRP SER LYS VAL
SEQRES 7 E 323 VAL ALA PRO LEU ALA GLU HIS PHE ASP VAL ILE VAL PRO
SEQRES 8 E 323 ASP LEU ARG GLY PHE GLY ASP SER GLU LYS PRO ASP LEU
SEQRES 9 E 323 GLY ASP ILE SER GLN TYR THR LEU ASP HIS ALA THR ASP
SEQRES 10 E 323 ASP GLN ALA ALA LEU LEU ASP GLU LEU GLY ILE ASP GLU
SEQRES 11 E 323 ALA TYR VAL VAL GLY HIS ASP TYR ALA ALA ILE ILE VAL
SEQRES 12 E 323 HIS LYS PHE ILE ARG LYS PHE ARG ASN ARG VAL ILE LYS
SEQRES 13 E 323 ALA ALA ILE PHE ASP PRO ILE THR PRO ASP PHE GLY GLU
SEQRES 14 E 323 PHE TYR PHE GLY ILE PRO HIS VAL SER GLU SER TRP TYR
SEQRES 15 E 323 SER GLN PHE HIS GLN THR ASP MET SER VAL GLU LEU VAL
SEQRES 16 E 323 SER SER SER ARG THR ALA CYS LYS ILE TYR PHE THR HIS
SEQRES 17 E 323 PHE MET ASN HIS TRP SER TYR ARG ASP GLU LEU LEU THR
SEQRES 18 E 323 ASP ASP GLU MET GLU ILE TYR VAL ASP ASN PHE MET LYS
SEQRES 19 E 323 ALA GLY ASN ILE HIS GLY GLY PHE ASN TYR TYR ARG ALA
SEQRES 20 E 323 ASN LEU SER MET THR SER ALA PRO TRP ASN GLU LEU ASP
SEQRES 21 E 323 ASP GLU VAL THR ASP LEU PRO VAL THR ILE LEU TRP GLY
SEQRES 22 E 323 GLN GLY ASP THR VAL VAL PRO SER LEU LEU ALA ASP ARG
SEQRES 23 E 323 LEU PRO LYS TYR TYR SER ASN TYR THR LEU GLU ILE VAL
SEQRES 24 E 323 GLU ASP ALA GLY HIS PHE MET MET VAL GLU LYS PRO ASP
SEQRES 25 E 323 ILE VAL ILE GLU ARG LEU THR ALA ALA PHE LYS
SEQRES 1 F 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 323 LEU VAL PRO ARG GLY SER HIS MET THR THR ALA SER SER
SEQRES 3 F 323 PHE ALA THR PRO ALA VAL ARG ARG PRO GLU GLU PHE SER
SEQRES 4 F 323 HIS ASN GLU ILE GLN LEU SER THR GLY VAL LYS ILE HIS
SEQRES 5 F 323 TYR VAL ARG GLU GLY SER GLY PRO PRO LEU LEU LEU LEU
SEQRES 6 F 323 HIS GLY TRP PRO GLY PHE TRP TRP GLU TRP SER LYS VAL
SEQRES 7 F 323 VAL ALA PRO LEU ALA GLU HIS PHE ASP VAL ILE VAL PRO
SEQRES 8 F 323 ASP LEU ARG GLY PHE GLY ASP SER GLU LYS PRO ASP LEU
SEQRES 9 F 323 GLY ASP ILE SER GLN TYR THR LEU ASP HIS ALA THR ASP
SEQRES 10 F 323 ASP GLN ALA ALA LEU LEU ASP GLU LEU GLY ILE ASP GLU
SEQRES 11 F 323 ALA TYR VAL VAL GLY HIS ASP TYR ALA ALA ILE ILE VAL
SEQRES 12 F 323 HIS LYS PHE ILE ARG LYS PHE ARG ASN ARG VAL ILE LYS
SEQRES 13 F 323 ALA ALA ILE PHE ASP PRO ILE THR PRO ASP PHE GLY GLU
SEQRES 14 F 323 PHE TYR PHE GLY ILE PRO HIS VAL SER GLU SER TRP TYR
SEQRES 15 F 323 SER GLN PHE HIS GLN THR ASP MET SER VAL GLU LEU VAL
SEQRES 16 F 323 SER SER SER ARG THR ALA CYS LYS ILE TYR PHE THR HIS
SEQRES 17 F 323 PHE MET ASN HIS TRP SER TYR ARG ASP GLU LEU LEU THR
SEQRES 18 F 323 ASP ASP GLU MET GLU ILE TYR VAL ASP ASN PHE MET LYS
SEQRES 19 F 323 ALA GLY ASN ILE HIS GLY GLY PHE ASN TYR TYR ARG ALA
SEQRES 20 F 323 ASN LEU SER MET THR SER ALA PRO TRP ASN GLU LEU ASP
SEQRES 21 F 323 ASP GLU VAL THR ASP LEU PRO VAL THR ILE LEU TRP GLY
SEQRES 22 F 323 GLN GLY ASP THR VAL VAL PRO SER LEU LEU ALA ASP ARG
SEQRES 23 F 323 LEU PRO LYS TYR TYR SER ASN TYR THR LEU GLU ILE VAL
SEQRES 24 F 323 GLU ASP ALA GLY HIS PHE MET MET VAL GLU LYS PRO ASP
SEQRES 25 F 323 ILE VAL ILE GLU ARG LEU THR ALA ALA PHE LYS
HET GOL A 401 14
HET MG A 402 1
HET 8K6 A 403 9
HET GOL B 401 14
HET 8K6 B 402 19
HET GOL C 401 14
HET SO4 C 402 5
HET 8K6 C 403 28
HET GOL D 401 14
HET GOL D 402 14
HET MG D 403 1
HET 8K6 D 404 27
HET GOL E 401 14
HET 8K6 E 402 30
HET GOL F 401 14
HET SO4 F 402 5
HET 8K6 F 403 22
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETNAM 8K6 OCTADECANE
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN 8K6 N-OCTADECANE
FORMUL 7 GOL 7(C3 H8 O3)
FORMUL 8 MG 2(MG 2+)
FORMUL 9 8K6 6(C18 H38)
FORMUL 13 SO4 2(O4 S 2-)
FORMUL 24 HOH *276(H2 O)
HELIX 1 AA1 ARG A 14 PHE A 18 5 5
HELIX 2 AA2 PHE A 51 GLU A 54 5 4
HELIX 3 AA3 TRP A 55 ALA A 63 1 9
HELIX 4 AA4 ASP A 86 TYR A 90 5 5
HELIX 5 AA5 THR A 91 LEU A 106 1 16
HELIX 6 AA6 ASP A 117 PHE A 130 1 14
HELIX 7 AA7 ASP A 146 PHE A 152 1 7
HELIX 8 AA8 HIS A 156 HIS A 166 1 11
HELIX 9 AA9 THR A 168 SER A 176 1 9
HELIX 10 AB1 SER A 178 TRP A 193 1 16
HELIX 11 AB2 THR A 201 MET A 213 1 13
HELIX 12 AB3 GLY A 216 LEU A 229 1 14
HELIX 13 AB4 ASN A 237 GLU A 242 5 6
HELIX 14 AB5 PRO A 260 TYR A 270 5 11
HELIX 15 AB6 PHE A 285 LYS A 290 1 6
HELIX 16 AB7 LYS A 290 PHE A 302 1 13
HELIX 17 AB8 ARG B 14 PHE B 18 5 5
HELIX 18 AB9 PHE B 51 GLU B 54 5 4
HELIX 19 AC1 TRP B 55 ALA B 63 1 9
HELIX 20 AC2 ASP B 86 TYR B 90 5 5
HELIX 21 AC3 THR B 91 LEU B 106 1 16
HELIX 22 AC4 ASP B 117 PHE B 130 1 14
HELIX 23 AC5 ASP B 146 PHE B 152 1 7
HELIX 24 AC6 HIS B 156 HIS B 166 1 11
HELIX 25 AC7 THR B 168 SER B 176 1 9
HELIX 26 AC8 SER B 178 TRP B 193 1 16
HELIX 27 AC9 THR B 201 MET B 213 1 13
HELIX 28 AD1 GLY B 216 LEU B 229 1 14
HELIX 29 AD2 GLU B 238 GLU B 242 5 5
HELIX 30 AD3 PRO B 260 LEU B 267 5 8
HELIX 31 AD4 PHE B 285 LYS B 290 1 6
HELIX 32 AD5 LYS B 290 PHE B 302 1 13
HELIX 33 AD6 ARG C 14 PHE C 18 5 5
HELIX 34 AD7 PHE C 51 GLU C 54 5 4
HELIX 35 AD8 TRP C 55 GLU C 64 1 10
HELIX 36 AD9 ASP C 86 TYR C 90 5 5
HELIX 37 AE1 THR C 91 LEU C 106 1 16
HELIX 38 AE2 ASP C 117 PHE C 130 1 14
HELIX 39 AE3 ASP C 146 PHE C 152 1 7
HELIX 40 AE4 HIS C 156 HIS C 166 1 11
HELIX 41 AE5 THR C 168 SER C 176 1 9
HELIX 42 AE6 SER C 178 TRP C 193 1 16
HELIX 43 AE7 THR C 201 LYS C 214 1 14
HELIX 44 AE8 GLY C 216 LEU C 229 1 14
HELIX 45 AE9 ASN C 237 GLU C 242 5 6
HELIX 46 AF1 PRO C 260 TYR C 270 5 11
HELIX 47 AF2 PHE C 285 LYS C 290 1 6
HELIX 48 AF3 LYS C 290 PHE C 302 1 13
HELIX 49 AF4 ARG D 14 PHE D 18 5 5
HELIX 50 AF5 PHE D 51 GLU D 54 5 4
HELIX 51 AF6 TRP D 55 GLU D 64 1 10
HELIX 52 AF7 ASP D 86 TYR D 90 5 5
HELIX 53 AF8 THR D 91 LEU D 106 1 16
HELIX 54 AF9 ASP D 117 PHE D 130 1 14
HELIX 55 AG1 ASP D 146 PHE D 152 1 7
HELIX 56 AG2 HIS D 156 HIS D 166 1 11
HELIX 57 AG3 THR D 168 SER D 176 1 9
HELIX 58 AG4 SER D 178 TRP D 193 1 16
HELIX 59 AG5 THR D 201 LYS D 214 1 14
HELIX 60 AG6 GLY D 216 LEU D 229 1 14
HELIX 61 AG7 ASN D 237 GLU D 242 5 6
HELIX 62 AG8 PRO D 260 TYR D 270 5 11
HELIX 63 AG9 PHE D 285 LYS D 290 1 6
HELIX 64 AH1 LYS D 290 PHE D 302 1 13
HELIX 65 AH2 ARG E 14 PHE E 18 5 5
HELIX 66 AH3 PHE E 51 GLU E 54 5 4
HELIX 67 AH4 TRP E 55 ALA E 63 1 9
HELIX 68 AH5 ASP E 86 TYR E 90 5 5
HELIX 69 AH6 THR E 91 LEU E 106 1 16
HELIX 70 AH7 ASP E 117 PHE E 130 1 14
HELIX 71 AH8 ASP E 146 PHE E 152 1 7
HELIX 72 AH9 HIS E 156 HIS E 166 1 11
HELIX 73 AI1 THR E 168 SER E 176 1 9
HELIX 74 AI2 SER E 178 TRP E 193 1 16
HELIX 75 AI3 THR E 201 LYS E 214 1 14
HELIX 76 AI4 GLY E 216 LEU E 229 1 14
HELIX 77 AI5 ASN E 237 GLU E 242 5 6
HELIX 78 AI6 PRO E 260 TYR E 270 5 11
HELIX 79 AI7 PHE E 285 LYS E 290 1 6
HELIX 80 AI8 LYS E 290 PHE E 302 1 13
HELIX 81 AI9 ARG F 14 PHE F 18 5 5
HELIX 82 AJ1 PHE F 51 SER F 56 5 6
HELIX 83 AJ2 VAL F 58 ALA F 63 1 6
HELIX 84 AJ3 ASP F 86 TYR F 90 5 5
HELIX 85 AJ4 THR F 91 GLY F 107 1 17
HELIX 86 AJ5 ASP F 117 PHE F 130 1 14
HELIX 87 AJ6 PHE F 147 PHE F 152 1 6
HELIX 88 AJ7 HIS F 156 HIS F 166 1 11
HELIX 89 AJ8 ASP F 169 SER F 178 1 10
HELIX 90 AJ9 SER F 178 TRP F 193 1 16
HELIX 91 AK1 THR F 201 MET F 213 1 13
HELIX 92 AK2 GLY F 216 LEU F 229 1 14
HELIX 93 AK3 ASN F 237 GLU F 242 5 6
HELIX 94 AK4 PRO F 260 TYR F 270 5 11
HELIX 95 AK5 PHE F 285 LYS F 290 1 6
HELIX 96 AK6 LYS F 290 PHE F 302 1 13
SHEET 1 AA1 8 HIS A 20 GLN A 24 0
SHEET 2 AA1 8 LYS A 30 GLU A 36 -1 O ILE A 31 N ILE A 23
SHEET 3 AA1 8 ASP A 67 PRO A 71 -1 O VAL A 70 N VAL A 34
SHEET 4 AA1 8 PRO A 41 LEU A 45 1 N LEU A 42 O ILE A 69
SHEET 5 AA1 8 ALA A 111 HIS A 116 1 O TYR A 112 N LEU A 43
SHEET 6 AA1 8 VAL A 134 PHE A 140 1 O ILE A 135 N ALA A 111
SHEET 7 AA1 8 VAL A 248 GLY A 253 1 O THR A 249 N ILE A 139
SHEET 8 AA1 8 TYR A 274 VAL A 279 1 O VAL A 279 N TRP A 252
SHEET 1 AA216 HIS B 20 GLN B 24 0
SHEET 2 AA216 LYS B 30 GLU B 36 -1 O ILE B 31 N ILE B 23
SHEET 3 AA216 ASP B 67 PRO B 71 -1 O VAL B 70 N VAL B 34
SHEET 4 AA216 PRO B 41 LEU B 45 1 N LEU B 42 O ILE B 69
SHEET 5 AA216 ALA B 111 HIS B 116 1 O TYR B 112 N LEU B 43
SHEET 6 AA216 VAL B 134 PHE B 140 1 O ILE B 135 N ALA B 111
SHEET 7 AA216 VAL B 248 GLY B 253 1 O THR B 249 N ILE B 139
SHEET 8 AA216 ASN B 273 VAL B 279 1 O VAL B 279 N TRP B 252
SHEET 9 AA216 ASN E 273 VAL E 279 -1 O LEU E 276 N TYR B 274
SHEET 10 AA216 VAL E 248 GLY E 253 1 N ILE E 250 O THR E 275
SHEET 11 AA216 VAL E 134 PHE E 140 1 N ILE E 139 O THR E 249
SHEET 12 AA216 ALA E 111 HIS E 116 1 N VAL E 113 O ALA E 138
SHEET 13 AA216 PRO E 41 LEU E 45 1 N PRO E 41 O TYR E 112
SHEET 14 AA216 ASP E 67 PRO E 71 1 O ASP E 67 N LEU E 42
SHEET 15 AA216 LYS E 30 GLU E 36 -1 N VAL E 34 O VAL E 70
SHEET 16 AA216 HIS E 20 GLN E 24 -1 N ASN E 21 O TYR E 33
SHEET 1 AA3 8 HIS C 20 GLN C 24 0
SHEET 2 AA3 8 LYS C 30 GLY C 37 -1 O ILE C 31 N ILE C 23
SHEET 3 AA3 8 ASP C 67 PRO C 71 -1 O VAL C 70 N VAL C 34
SHEET 4 AA3 8 PRO C 41 LEU C 45 1 N LEU C 42 O ILE C 69
SHEET 5 AA3 8 ALA C 111 HIS C 116 1 O TYR C 112 N LEU C 43
SHEET 6 AA3 8 VAL C 134 PHE C 140 1 O ALA C 138 N VAL C 113
SHEET 7 AA3 8 VAL C 248 GLY C 253 1 O THR C 249 N ALA C 137
SHEET 8 AA3 8 TYR C 274 VAL C 279 1 O VAL C 279 N TRP C 252
SHEET 1 AA4 8 HIS D 20 GLN D 24 0
SHEET 2 AA4 8 LYS D 30 GLY D 37 -1 O ILE D 31 N ILE D 23
SHEET 3 AA4 8 ASP D 67 PRO D 71 -1 O VAL D 70 N VAL D 34
SHEET 4 AA4 8 PRO D 41 LEU D 45 1 N LEU D 42 O ILE D 69
SHEET 5 AA4 8 ALA D 111 HIS D 116 1 O TYR D 112 N LEU D 43
SHEET 6 AA4 8 VAL D 134 PHE D 140 1 O ALA D 138 N VAL D 113
SHEET 7 AA4 8 VAL D 248 GLY D 253 1 O THR D 249 N ALA D 137
SHEET 8 AA4 8 TYR D 274 VAL D 279 1 O VAL D 279 N TRP D 252
SHEET 1 AA5 8 HIS F 20 GLN F 24 0
SHEET 2 AA5 8 LYS F 30 GLY F 37 -1 O ILE F 31 N ILE F 23
SHEET 3 AA5 8 ASP F 67 PRO F 71 -1 O VAL F 68 N GLU F 36
SHEET 4 AA5 8 PRO F 41 LEU F 45 1 N LEU F 42 O ILE F 69
SHEET 5 AA5 8 ALA F 111 HIS F 116 1 O TYR F 112 N LEU F 43
SHEET 6 AA5 8 VAL F 134 PHE F 140 1 O ALA F 138 N VAL F 113
SHEET 7 AA5 8 VAL F 248 GLY F 253 1 O THR F 249 N ALA F 137
SHEET 8 AA5 8 TYR F 274 VAL F 279 1 O THR F 275 N ILE F 250
LINK O ASN A 191 MG MG A 402 1555 1555 2.48
LINK O SER A 194 MG MG A 402 1555 1555 2.45
LINK O ARG A 196 MG MG A 402 1555 1555 2.95
LINK MG MG A 402 O HOH A 537 1555 1555 2.41
LINK MG MG A 402 O HOH A 547 1555 1555 2.24
LINK MG MG A 402 O HOH A 571 1555 1555 2.47
LINK O SER D 194 MG MG D 403 1555 1555 2.77
LINK O ARG D 196 MG MG D 403 1555 1555 2.69
LINK MG MG D 403 O HOH D 529 1555 1555 2.65
CISPEP 1 TRP A 48 PRO A 49 0 -7.41
CISPEP 2 ILE A 154 PRO A 155 0 3.66
CISPEP 3 TRP B 48 PRO B 49 0 -6.12
CISPEP 4 ILE B 154 PRO B 155 0 7.00
CISPEP 5 TRP C 48 PRO C 49 0 -3.95
CISPEP 6 ILE C 154 PRO C 155 0 1.75
CISPEP 7 TRP D 48 PRO D 49 0 -8.34
CISPEP 8 ILE D 154 PRO D 155 0 -1.15
CISPEP 9 TRP E 48 PRO E 49 0 -9.14
CISPEP 10 ILE E 154 PRO E 155 0 2.06
CISPEP 11 TRP F 48 PRO F 49 0 -4.99
CISPEP 12 ILE F 154 PRO F 155 0 -0.45
CRYST1 48.417 181.005 221.720 90.00 90.00 90.00 P 21 21 21 24
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 0.020654 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005525 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004510 0.00000
TER 4604 LYS A 303
TER 9201 LYS B 303
TER 13803 LYS C 303
TER 18396 PHE D 302
TER 22844 LYS E 303
TER 27327 LYS F 303
MASTER 596 0 17 96 48 0 0 614485 6 255 150
END |