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HEADER HYDROLASE 14-OCT-16 5TNP
TITLE CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING THE ADDUCTED STYRENE OXIDE HYDROLYSIS INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN UCBPP-PA14);
SOURCE 3 ORGANISM_TAXID: 208963;
SOURCE 4 STRAIN: UCBPP-PA14;
SOURCE 5 GENE: PA14_26090;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10
KEYWDS EPOXIDE HYDROLASE, HYDROXYALKYL-ENZYME INTERMEDIATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.HVORECNY,D.R.MADDEN
REVDAT 1 11-OCT-17 5TNP 0
JRNL AUTH K.L.HVORECNY,C.D.BAHL,S.KITAMURA,K.S.S.LEE,B.D.HAMMOCK,
JRNL AUTH 2 C.MORISSEAU,D.R.MADDEN
JRNL TITL ACTIVE-SITE FLEXIBILITY AND SUBSTRATE SPECIFICITY IN A
JRNL TITL 2 BACTERIAL VIRULENCE FACTOR: CRYSTALLOGRAPHIC SNAPSHOTS OF AN
JRNL TITL 3 EPOXIDE HYDROLASE.
JRNL REF STRUCTURE V. 25 697 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28392259
JRNL DOI 10.1016/J.STR.2017.03.002
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 104010
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5220
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 19.8238 - 5.7039 0.99 3317 261 0.1621 0.2072
REMARK 3 2 5.7039 - 4.5453 1.00 3513 0 0.1434 0.0000
REMARK 3 3 4.5453 - 3.9761 1.00 3230 261 0.1387 0.1615
REMARK 3 4 3.9761 - 3.6149 1.00 3206 261 0.1525 0.1761
REMARK 3 5 3.6149 - 3.3571 1.00 3478 0 0.1494 0.0000
REMARK 3 6 3.3571 - 3.1600 1.00 3248 261 0.1662 0.1944
REMARK 3 7 3.1600 - 3.0024 1.00 3171 261 0.1742 0.2160
REMARK 3 8 3.0024 - 2.8721 1.00 3503 0 0.1813 0.0000
REMARK 3 9 2.8721 - 2.7618 1.00 3188 261 0.1749 0.2264
REMARK 3 10 2.7618 - 2.6667 0.99 3210 261 0.1700 0.2094
REMARK 3 11 2.6667 - 2.5835 1.00 3443 0 0.1746 0.0000
REMARK 3 12 2.5835 - 2.5098 1.00 3218 261 0.1678 0.2127
REMARK 3 13 2.5098 - 2.4439 1.00 3227 261 0.1750 0.2334
REMARK 3 14 2.4439 - 2.3844 1.00 3448 0 0.1732 0.0000
REMARK 3 15 2.3844 - 2.3302 1.00 3195 261 0.1712 0.2255
REMARK 3 16 2.3302 - 2.2807 1.00 3205 261 0.1655 0.2174
REMARK 3 17 2.2807 - 2.2352 1.00 3435 0 0.1691 0.0000
REMARK 3 18 2.2352 - 2.1930 1.00 3203 261 0.1711 0.2166
REMARK 3 19 2.1930 - 2.1539 1.00 3212 261 0.1712 0.2144
REMARK 3 20 2.1539 - 2.1174 1.00 3465 0 0.1686 0.0000
REMARK 3 21 2.1174 - 2.0833 1.00 3164 261 0.1731 0.2404
REMARK 3 22 2.0833 - 2.0513 0.99 3181 261 0.1778 0.2313
REMARK 3 23 2.0513 - 2.0212 1.00 3476 0 0.1767 0.0000
REMARK 3 24 2.0212 - 1.9927 1.00 3181 261 0.1833 0.2321
REMARK 3 25 1.9927 - 1.9658 1.00 3204 261 0.1904 0.2348
REMARK 3 26 1.9658 - 1.9403 1.00 3456 0 0.1912 0.0000
REMARK 3 27 1.9403 - 1.9161 1.00 3166 261 0.1937 0.2410
REMARK 3 28 1.9161 - 1.8930 1.00 3230 261 0.2079 0.2666
REMARK 3 29 1.8930 - 1.8710 1.00 3399 0 0.2356 0.0000
REMARK 3 30 1.8710 - 1.8500 0.99 3218 261 0.2585 0.2834
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 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) : 20.360
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 : 0.006 9910
REMARK 3 ANGLE : 0.798 13484
REMARK 3 CHIRALITY : 0.050 1382
REMARK 3 PLANARITY : 0.006 1777
REMARK 3 DIHEDRAL : 15.677 5812
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0817 -31.7278 27.0638
REMARK 3 T TENSOR
REMARK 3 T11: 0.1525 T22: 0.1585
REMARK 3 T33: 0.1422 T12: 0.0067
REMARK 3 T13: 0.0075 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 1.0146 L22: 1.0939
REMARK 3 L33: 0.7388 L12: 0.0368
REMARK 3 L13: 0.1202 L23: -0.0986
REMARK 3 S TENSOR
REMARK 3 S11: 0.0190 S12: -0.0821 S13: -0.1076
REMARK 3 S21: 0.0893 S22: -0.0203 S23: 0.0472
REMARK 3 S31: 0.0763 S32: -0.0214 S33: 0.0038
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.7310 7.1104 15.6553
REMARK 3 T TENSOR
REMARK 3 T11: 0.1202 T22: 0.1370
REMARK 3 T33: 0.1703 T12: 0.0188
REMARK 3 T13: -0.0190 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 1.0720 L22: 1.6176
REMARK 3 L33: 0.5980 L12: -0.3621
REMARK 3 L13: -0.0382 L23: -0.2412
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: 0.0162 S13: 0.1397
REMARK 3 S21: -0.0508 S22: 0.0213 S23: 0.0630
REMARK 3 S31: -0.0719 S32: -0.0274 S33: -0.0136
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0037 0.0257 27.0019
REMARK 3 T TENSOR
REMARK 3 T11: 0.1539 T22: 0.1587
REMARK 3 T33: 0.1838 T12: 0.0056
REMARK 3 T13: 0.0038 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.8677 L22: 1.1892
REMARK 3 L33: 0.7110 L12: 0.0263
REMARK 3 L13: 0.0561 L23: 0.0934
REMARK 3 S TENSOR
REMARK 3 S11: -0.0003 S12: -0.0456 S13: 0.1623
REMARK 3 S21: 0.0675 S22: -0.0225 S23: -0.0833
REMARK 3 S31: -0.0895 S32: 0.0181 S33: 0.0230
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7600 -38.8663 15.7861
REMARK 3 T TENSOR
REMARK 3 T11: 0.1396 T22: 0.1499
REMARK 3 T33: 0.1337 T12: 0.0216
REMARK 3 T13: 0.0113 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.0416 L22: 1.3905
REMARK 3 L33: 0.5210 L12: -0.3333
REMARK 3 L13: -0.0642 L23: 0.1640
REMARK 3 S TENSOR
REMARK 3 S11: 0.0161 S12: 0.0387 S13: -0.0636
REMARK 3 S21: -0.0185 S22: -0.0035 S23: -0.1136
REMARK 3 S31: 0.0561 S32: 0.0270 S33: -0.0113
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 5TNP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000221415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.181
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS OCT 15, 2015
REMARK 200 DATA SCALING SOFTWARE : XDS OCT 15, 2015
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104019
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 19.823
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.2800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.68
REMARK 200 R MERGE FOR SHELL (I) : 0.51700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.6.0
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PH5 CALCIUM CHLORIDE
REMARK 280 PEG 8000, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 84.00750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.00650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.00750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.00650
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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: 2760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH D 519 LIES ON A SPECIAL POSITION.
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 318
REMARK 465 ARG A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 GLY B 318
REMARK 465 ARG B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 GLY C 318
REMARK 465 ARG C 319
REMARK 465 HIS C 320
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 GLY D 318
REMARK 465 ARG D 319
REMARK 465 HIS D 320
REMARK 465 HIS D 321
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
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 NH2 ARG B 148 O ARG B 317 2.15
REMARK 500 NH1 ARG B 197 OD1 ASP B 220 2.16
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 129 -129.71 58.79
REMARK 500 ASP A 129 -130.60 60.41
REMARK 500 ALA A 154 150.49 179.62
REMARK 500 THR B 99 -62.58 -98.26
REMARK 500 ASP B 129 -127.09 59.37
REMARK 500 ASP B 129 -127.23 59.65
REMARK 500 ALA B 154 148.30 175.71
REMARK 500 THR C 99 -68.69 -90.47
REMARK 500 ASP C 129 -128.43 59.18
REMARK 500 ASP C 129 -128.91 60.09
REMARK 500 THR D 99 -66.70 -100.69
REMARK 500 ASP D 129 -126.87 58.33
REMARK 500 ASP D 129 -127.08 58.73
REMARK 500 ALA D 154 149.88 179.38
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 699 DISTANCE = 7.47 ANGSTROMS
REMARK 525 HOH C 699 DISTANCE = 9.33 ANGSTROMS
REMARK 525 HOH C 700 DISTANCE = 10.07 ANGSTROMS
REMARK 525 HOH D 694 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH D 695 DISTANCE = 6.82 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FEH REPRESENTS BOUND FORM OF STYRENE OXIDE. C1 ATOM OF FEH 327 (OR
REMARK 600 C3 ATOM OF FEH 326) COVALENTLY BOUND TO OD1 ATOM OF RESIDUES 129
REMARK 600 (ASP) OF POLYMER.
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 FEH A 401
REMARK 610 FEH B 401
REMARK 610 FEH C 401
REMARK 610 FEH D 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FEH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FEH A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FEH B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FEH B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FEH C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FEH C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FEH D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FEH D 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 WILD TYPE VERSION OF THE CURRENT SUBMISSION
REMARK 900 RELATED ID: 4DMC RELATED DB: PDB
REMARK 900 APO VERSION OF SAME PROTEIN AS CURRENT SUBMISSION (CIF WITH E153Q
REMARK 900 MUTATION)
REMARK 900 RELATED ID: 5TND RELATED DB: PDB
REMARK 900 RELATED ID: 5TNE RELATED DB: PDB
REMARK 900 RELATED ID: 5TNF RELATED DB: PDB
REMARK 900 RELATED ID: 5TNG RELATED DB: PDB
REMARK 900 RELATED ID: 5TNH RELATED DB: PDB
REMARK 900 RELATED ID: 5TNI RELATED DB: PDB
REMARK 900 RELATED ID: 5TNJ RELATED DB: PDB
REMARK 900 RELATED ID: 5TNK RELATED DB: PDB
REMARK 900 RELATED ID: 5TNL RELATED DB: PDB
REMARK 900 RELATED ID: 5TNM RELATED DB: PDB
REMARK 900 RELATED ID: 5TNN RELATED DB: PDB
REMARK 900 RELATED ID: 5TNQ RELATED DB: PDB
REMARK 900 RELATED ID: 5TNR RELATED DB: PDB
REMARK 900 RELATED ID: 5TNS RELATED DB: PDB
DBREF1 5TNP A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNP A A0A0M3KL26 1 301
DBREF1 5TNP B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNP B A0A0M3KL26 1 301
DBREF1 5TNP C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNP C A0A0M3KL26 1 301
DBREF1 5TNP D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNP D A0A0M3KL26 1 301
SEQADV 5TNP GLN A 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNP GLN B 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNP GLN C 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNP GLN D 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQRES 1 A 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 A 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 A 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 A 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 A 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 A 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 A 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 A 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 A 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 A 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA
SEQRES 11 A 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 A 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 A 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 A 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 A 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 A 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 A 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 A 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 A 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 A 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 A 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 A 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 A 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 A 301 HIS HIS
SEQRES 1 B 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 B 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 B 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 B 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 B 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 B 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 B 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 B 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 B 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 B 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA
SEQRES 11 B 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 B 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 B 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 B 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 B 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 B 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 B 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 B 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 B 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 B 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 B 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 B 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 B 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 B 301 HIS HIS
SEQRES 1 C 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 C 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 C 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 C 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 C 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 C 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 C 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 C 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 C 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 C 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA
SEQRES 11 C 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 C 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 C 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 C 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 C 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 C 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 C 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 C 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 C 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 C 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 C 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 C 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 C 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 C 301 HIS HIS
SEQRES 1 D 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 D 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 D 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 D 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 D 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 D 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 D 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 D 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 D 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 D 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA
SEQRES 11 D 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 D 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 D 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 D 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 D 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 D 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 D 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 D 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 D 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 D 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 D 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 D 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 D 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 D 301 HIS HIS
HET FEH A 401 9
HET FEH A 402 9
HET FEH B 401 9
HET FEH B 402 9
HET FEH C 401 9
HET FEH C 402 9
HET FEH D 401 9
HET FEH D 402 9
HETNAM FEH (1R)-1-PHENYLETHANE-1,2-DIOL
FORMUL 5 FEH 8(C8 H10 O2)
FORMUL 13 HOH *778(H2 O)
HELIX 1 AA1 THR A 66 HIS A 71 5 6
HELIX 2 AA2 LEU A 73 ALA A 78 1 6
HELIX 3 AA3 SER A 102 SER A 118 1 17
HELIX 4 AA4 ASP A 129 ASN A 134 1 6
HELIX 5 AA5 THR A 135 ASN A 142 1 8
HELIX 6 AA6 ASP A 158 PHE A 164 5 7
HELIX 7 AA7 TRP A 176 ALA A 183 1 8
HELIX 8 AA8 ARG A 186 ALA A 193 1 8
HELIX 9 AA9 LYS A 195 HIS A 207 1 13
HELIX 10 AB1 ASN A 210 PHE A 214 5 5
HELIX 11 AB2 SER A 215 ALA A 227 1 13
HELIX 12 AB3 LYS A 228 ALA A 241 1 14
HELIX 13 AB4 ALA A 241 ALA A 253 1 13
HELIX 14 AB5 THR A 274 ALA A 284 1 11
HELIX 15 AB6 TRP A 298 CYS A 303 1 6
HELIX 16 AB7 CYS A 303 ARG A 317 1 15
HELIX 17 AB8 THR B 66 HIS B 71 5 6
HELIX 18 AB9 GLN B 72 ALA B 78 1 7
HELIX 19 AC1 SER B 102 SER B 118 1 17
HELIX 20 AC2 ASP B 129 ASN B 134 1 6
HELIX 21 AC3 THR B 135 ASN B 142 1 8
HELIX 22 AC4 ASP B 158 PHE B 164 5 7
HELIX 23 AC5 TRP B 176 ALA B 183 1 8
HELIX 24 AC6 ARG B 186 ALA B 193 1 8
HELIX 25 AC7 LYS B 195 HIS B 207 1 13
HELIX 26 AC8 SER B 215 ALA B 227 1 13
HELIX 27 AC9 LYS B 228 ALA B 241 1 14
HELIX 28 AD1 ALA B 241 ALA B 253 1 13
HELIX 29 AD2 THR B 274 ALA B 282 1 9
HELIX 30 AD3 TRP B 298 CYS B 303 1 6
HELIX 31 AD4 CYS B 303 ARG B 317 1 15
HELIX 32 AD5 THR C 66 HIS C 71 5 6
HELIX 33 AD6 LEU C 73 ALA C 78 1 6
HELIX 34 AD7 SER C 102 SER C 118 1 17
HELIX 35 AD8 ASP C 129 ASN C 134 1 6
HELIX 36 AD9 THR C 135 ASN C 142 1 8
HELIX 37 AE1 ASP C 158 PHE C 164 5 7
HELIX 38 AE2 VAL C 175 ALA C 183 1 9
HELIX 39 AE3 ARG C 186 ALA C 193 1 8
HELIX 40 AE4 LYS C 195 HIS C 207 1 13
HELIX 41 AE5 ASN C 210 PHE C 214 5 5
HELIX 42 AE6 SER C 215 ALA C 227 1 13
HELIX 43 AE7 LYS C 228 ALA C 241 1 14
HELIX 44 AE8 ALA C 241 ALA C 253 1 13
HELIX 45 AE9 THR C 274 ALA C 284 1 11
HELIX 46 AF1 TRP C 298 CYS C 303 1 6
HELIX 47 AF2 CYS C 303 SER C 316 1 14
HELIX 48 AF3 THR D 66 HIS D 71 5 6
HELIX 49 AF4 GLN D 72 ALA D 78 1 7
HELIX 50 AF5 SER D 102 SER D 118 1 17
HELIX 51 AF6 ASP D 129 ASN D 134 1 6
HELIX 52 AF7 THR D 135 ASN D 142 1 8
HELIX 53 AF8 ASP D 158 PHE D 164 5 7
HELIX 54 AF9 TRP D 176 ALA D 183 1 8
HELIX 55 AG1 ARG D 186 ALA D 193 1 8
HELIX 56 AG2 LYS D 195 HIS D 207 1 13
HELIX 57 AG3 ASN D 210 PHE D 214 5 5
HELIX 58 AG4 SER D 215 ALA D 227 1 13
HELIX 59 AG5 LYS D 228 ALA D 241 1 14
HELIX 60 AG6 ALA D 241 ALA D 253 1 13
HELIX 61 AG7 THR D 274 LYS D 281 1 8
HELIX 62 AG8 TRP D 298 CYS D 303 1 6
HELIX 63 AG9 CYS D 303 ARG D 317 1 15
SHEET 1 AA1 8 GLU A 35 VAL A 41 0
SHEET 2 AA1 8 VAL A 44 GLY A 52 -1 O VAL A 44 N VAL A 41
SHEET 3 AA1 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 AA1 8 LEU A 56 VAL A 60 1 N VAL A 57 O THR A 82
SHEET 5 AA1 8 PHE A 123 HIS A 128 1 O VAL A 126 N VAL A 60
SHEET 6 AA1 8 ILE A 146 MET A 152 1 O ALA A 147 N PHE A 123
SHEET 7 AA1 8 THR A 261 GLY A 266 1 O MET A 262 N TYR A 151
SHEET 8 AA1 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 AA2 2 PHE A 167 THR A 168 0
SHEET 2 AA2 2 GLY A 171 GLU A 172 -1 O GLY A 171 N THR A 168
SHEET 1 AA3 8 GLU B 35 VAL B 41 0
SHEET 2 AA3 8 VAL B 44 GLY B 52 -1 O VAL B 44 N VAL B 41
SHEET 3 AA3 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 AA3 8 LEU B 56 VAL B 60 1 N VAL B 57 O THR B 82
SHEET 5 AA3 8 PHE B 123 HIS B 128 1 O ASP B 124 N LEU B 56
SHEET 6 AA3 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 AA3 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 AA3 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 AA4 2 PHE B 167 THR B 168 0
SHEET 2 AA4 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SHEET 1 AA5 8 GLU C 35 VAL C 41 0
SHEET 2 AA5 8 VAL C 44 GLY C 52 -1 O VAL C 44 N VAL C 41
SHEET 3 AA5 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA5 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 AA5 8 PHE C 123 HIS C 128 1 O VAL C 126 N VAL C 60
SHEET 6 AA5 8 ILE C 146 MET C 152 1 O ALA C 147 N PHE C 123
SHEET 7 AA5 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 AA5 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA6 2 PHE C 167 THR C 168 0
SHEET 2 AA6 2 GLY C 171 GLU C 172 -1 O GLY C 171 N THR C 168
SHEET 1 AA7 8 GLU D 35 VAL D 41 0
SHEET 2 AA7 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
SHEET 3 AA7 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA7 8 LEU D 56 VAL D 60 1 N VAL D 57 O ILE D 84
SHEET 5 AA7 8 PHE D 123 HIS D 128 1 O VAL D 126 N VAL D 60
SHEET 6 AA7 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA7 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA7 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA8 2 PHE D 167 THR D 168 0
SHEET 2 AA8 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SSBOND 1 CYS A 295 CYS A 303 1555 1555 2.01
SSBOND 2 CYS B 295 CYS B 303 1555 1555 2.00
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.01
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.00
LINK OD1AASP A 129 C1 AFEH A 401 1555 1555 1.40
LINK OD1BASP A 129 C3 BFEH A 402 1555 1555 1.38
LINK OD1AASP B 129 C1 AFEH B 401 1555 1555 1.40
LINK OD1BASP B 129 C3 BFEH B 402 1555 1555 1.38
LINK OD1AASP C 129 C1 AFEH C 401 1555 1555 1.40
LINK OD1BASP C 129 C3 BFEH C 402 1555 1555 1.38
LINK OD1AASP D 129 C1 AFEH D 401 1555 1555 1.40
LINK OD1BASP D 129 C3 BFEH D 402 1555 1555 1.39
SITE 1 AC1 5 ILE A 130 HIS A 207 TYR A 239 HIS A 297
SITE 2 AC1 5 FEH A 402
SITE 1 AC2 6 VAL A 175 HIS A 177 TYR A 239 MET A 272
SITE 2 AC2 6 HIS A 297 FEH A 401
SITE 1 AC3 4 HIS B 207 TYR B 239 HIS B 297 FEH B 402
SITE 1 AC4 7 VAL B 175 HIS B 177 PHE B 178 TYR B 239
SITE 2 AC4 7 MET B 272 HIS B 297 FEH B 401
SITE 1 AC5 4 HIS C 207 TYR C 239 HIS C 297 FEH C 402
SITE 1 AC6 7 VAL C 175 HIS C 177 PHE C 178 TYR C 239
SITE 2 AC6 7 MET C 272 HIS C 297 FEH C 401
SITE 1 AC7 5 HIS D 177 HIS D 207 TYR D 239 HIS D 297
SITE 2 AC7 5 FEH D 402
SITE 1 AC8 6 VAL D 175 HIS D 177 PHE D 178 TYR D 239
SITE 2 AC8 6 HIS D 297 FEH D 401
CRYST1 168.015 84.013 89.459 90.00 100.31 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005952 0.000000 0.001082 0.00000
SCALE2 0.000000 0.011903 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011362 0.00000
TER 2410 ARG A 317
TER 4758 ARG B 317
TER 7166 ARG C 317
TER 9525 ARG D 317
MASTER 469 0 8 63 40 0 14 610202 4 88 96
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