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HEADER HYDROLASE 14-OCT-16 5TNQ
TITLE CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING THE ADDUCTED (R)-STYRENE OXIDE HYDROLYSIS INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 3 CHAIN: C, D, A, B;
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 5TNQ 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. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 194339
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 9700
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 19.8080 - 4.6414 1.00 6143 485 0.1533 0.1526
REMARK 3 2 4.6414 - 3.6918 1.00 6561 0 0.1362 0.0000
REMARK 3 3 3.6918 - 3.2275 1.00 6012 485 0.1474 0.1719
REMARK 3 4 3.2275 - 2.9334 1.00 6043 485 0.1609 0.1852
REMARK 3 5 2.9334 - 2.7237 1.00 6509 0 0.1632 0.0000
REMARK 3 6 2.7237 - 2.5635 1.00 6026 485 0.1651 0.1742
REMARK 3 7 2.5635 - 2.4353 1.00 6015 485 0.1636 0.1792
REMARK 3 8 2.4353 - 2.3295 1.00 6459 0 0.1591 0.0000
REMARK 3 9 2.3295 - 2.2399 1.00 5981 485 0.1617 0.1879
REMARK 3 10 2.2399 - 2.1627 1.00 6032 485 0.1601 0.1917
REMARK 3 11 2.1627 - 2.0952 1.00 6464 0 0.1576 0.0000
REMARK 3 12 2.0952 - 2.0354 1.00 5996 485 0.1610 0.1719
REMARK 3 13 2.0354 - 1.9818 1.00 5970 485 0.1586 0.1926
REMARK 3 14 1.9818 - 1.9335 1.00 6440 0 0.1652 0.0000
REMARK 3 15 1.9335 - 1.8896 1.00 5980 485 0.1632 0.1877
REMARK 3 16 1.8896 - 1.8494 1.00 5994 485 0.1731 0.2044
REMARK 3 17 1.8494 - 1.8125 1.00 6469 0 0.1702 0.0000
REMARK 3 18 1.8125 - 1.7783 1.00 5978 485 0.1710 0.2098
REMARK 3 19 1.7783 - 1.7465 1.00 5915 485 0.1678 0.1871
REMARK 3 20 1.7465 - 1.7169 1.00 6482 0 0.1697 0.0000
REMARK 3 21 1.7169 - 1.6893 1.00 6009 485 0.1714 0.1862
REMARK 3 22 1.6893 - 1.6633 1.00 5984 485 0.1685 0.1908
REMARK 3 23 1.6633 - 1.6388 1.00 6472 0 0.1741 0.0000
REMARK 3 24 1.6388 - 1.6158 1.00 5909 485 0.1887 0.2140
REMARK 3 25 1.6158 - 1.5939 1.00 5953 485 0.1916 0.2334
REMARK 3 26 1.5939 - 1.5732 1.00 6484 0 0.1972 0.0000
REMARK 3 27 1.5732 - 1.5536 1.00 5950 485 0.2073 0.2318
REMARK 3 28 1.5536 - 1.5349 1.00 6000 485 0.2135 0.2353
REMARK 3 29 1.5349 - 1.5170 1.00 6416 0 0.2212 0.0000
REMARK 3 30 1.5170 - 1.5000 1.00 5993 485 0.2307 0.2429
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.880
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 9883
REMARK 3 ANGLE : 0.838 13453
REMARK 3 CHIRALITY : 0.052 1389
REMARK 3 PLANARITY : 0.006 1774
REMARK 3 DIHEDRAL : 14.589 5838
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN C AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7004 -0.0967 26.9011
REMARK 3 T TENSOR
REMARK 3 T11: 0.1037 T22: 0.1013
REMARK 3 T33: 0.1130 T12: 0.0147
REMARK 3 T13: -0.0011 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.8160 L22: 1.1256
REMARK 3 L33: 0.7469 L12: -0.0048
REMARK 3 L13: -0.0162 L23: 0.0879
REMARK 3 S TENSOR
REMARK 3 S11: -0.0050 S12: -0.0648 S13: 0.1270
REMARK 3 S21: 0.0835 S22: -0.0100 S23: -0.0934
REMARK 3 S31: -0.0857 S32: 0.0219 S33: 0.0141
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN D AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5396 -38.9698 15.6863
REMARK 3 T TENSOR
REMARK 3 T11: 0.0873 T22: 0.0965
REMARK 3 T33: 0.0779 T12: 0.0215
REMARK 3 T13: 0.0107 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.0548 L22: 1.3588
REMARK 3 L33: 0.6218 L12: -0.3614
REMARK 3 L13: -0.0524 L23: 0.2482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0298 S12: 0.0290 S13: -0.0394
REMARK 3 S21: -0.0366 S22: -0.0026 S23: -0.1334
REMARK 3 S31: 0.0497 S32: 0.0171 S33: -0.0206
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0925 -31.8136 27.1034
REMARK 3 T TENSOR
REMARK 3 T11: 0.1022 T22: 0.1120
REMARK 3 T33: 0.0741 T12: 0.0133
REMARK 3 T13: 0.0090 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.8881 L22: 0.9087
REMARK 3 L33: 0.7043 L12: -0.0049
REMARK 3 L13: 0.0778 L23: -0.0206
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: -0.1205 S13: -0.1045
REMARK 3 S21: 0.0980 S22: 0.0036 S23: 0.0496
REMARK 3 S31: 0.0881 S32: -0.0314 S33: 0.0091
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.8791 6.9821 15.4447
REMARK 3 T TENSOR
REMARK 3 T11: 0.0824 T22: 0.0951
REMARK 3 T33: 0.1305 T12: 0.0144
REMARK 3 T13: -0.0229 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 1.0951 L22: 1.4595
REMARK 3 L33: 0.6481 L12: -0.4458
REMARK 3 L13: -0.0044 L23: -0.1629
REMARK 3 S TENSOR
REMARK 3 S11: -0.0154 S12: 0.0121 S13: 0.1621
REMARK 3 S21: -0.0497 S22: 0.0113 S23: 0.0353
REMARK 3 S31: -0.0797 S32: -0.0184 S33: 0.0055
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 5TNQ 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_1000221468.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-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) : 0.979
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 : 194347
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 19.806
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.67
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.490
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 (%): 45.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
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 84.08650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.98950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.08650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.98950
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: 3520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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: 3530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 700 O HOH B 705 1.91
REMARK 500 O HOH A 611 O HOH A 696 1.92
REMARK 500 O HOH A 607 O HOH A 736 2.03
REMARK 500 O HOH D 755 O HOH D 772 2.07
REMARK 500 O HOH C 761 O HOH C 775 2.07
REMARK 500 O HOH C 696 O HOH C 757 2.07
REMARK 500 O HOH D 732 O HOH D 767 2.08
REMARK 500 O HOH D 571 O HOH D 647 2.09
REMARK 500 NH1 ARG B 197 OD1 ASP B 220 2.09
REMARK 500 O HOH C 728 O HOH C 764 2.10
REMARK 500 O HOH B 542 O HOH B 733 2.12
REMARK 500 O HOH A 527 O HOH A 741 2.15
REMARK 500 NE2 GLN D 170 O HOH D 501 2.17
REMARK 500 OE2 GLU C 172 O HOH C 501 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 708 O HOH C 761 2556 2.18
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 C 129 -128.13 60.91
REMARK 500 ALA C 154 149.56 175.23
REMARK 500 CYS C 303 56.60 -141.91
REMARK 500 THR D 99 -63.82 -96.13
REMARK 500 ASP D 129 -130.09 58.81
REMARK 500 ALA D 154 149.53 173.80
REMARK 500 ASP A 129 -127.86 61.02
REMARK 500 ALA A 154 149.86 172.87
REMARK 500 CYS A 303 54.23 -142.68
REMARK 500 THR B 99 -72.05 -91.13
REMARK 500 ASP B 129 -130.43 61.53
REMARK 500 ALA B 154 149.72 172.69
REMARK 500 ASP B 185 19.08 59.06
REMARK 500 TRP B 298 59.43 -90.10
REMARK 500 CYS B 303 54.21 -140.10
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 C 811 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH C 812 DISTANCE = 6.50 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FEH IS BOUND FORM OF (R)-STYRENE OXIDE VIA ITS C8 ATOM CONVALENTLY
REMARK 600 LINKED TO OD1 ATOM OF ASP RESIDUE 129 OF CIF.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FEH C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide FEH A 401 and ASP A
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide FEH B 401 and ASP B
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide FEH D 401 and ASP D
REMARK 800 129
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: 5TNP RELATED DB: PDB
REMARK 900 RELATED ID: 5TNR RELATED DB: PDB
REMARK 900 RELATED ID: 5TNS RELATED DB: PDB
DBREF1 5TNQ C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNQ C A0A0M3KL26 1 301
DBREF1 5TNQ D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNQ D A0A0M3KL26 1 301
DBREF1 5TNQ A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNQ A A0A0M3KL26 1 301
DBREF1 5TNQ B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNQ B A0A0M3KL26 1 301
SEQADV 5TNQ GLN C 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNQ GLN D 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNQ GLN A 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNQ GLN B 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
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
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
HET FEH C 401 9
HET FEH D 401 9
HET FEH A 401 9
HET FEH B 401 9
HETNAM FEH (1R)-1-PHENYLETHANE-1,2-DIOL
FORMUL 5 FEH 4(C8 H10 O2)
FORMUL 9 HOH *1156(H2 O)
HELIX 1 AA1 THR C 66 HIS C 71 5 6
HELIX 2 AA2 GLN C 72 ALA C 78 1 7
HELIX 3 AA3 SER C 102 SER C 118 1 17
HELIX 4 AA4 ASP C 129 ASN C 134 1 6
HELIX 5 AA5 THR C 135 ASN C 142 1 8
HELIX 6 AA6 ASP C 158 PHE C 164 5 7
HELIX 7 AA7 TRP C 176 ALA C 183 1 8
HELIX 8 AA8 ARG C 186 ALA C 193 1 8
HELIX 9 AA9 LYS C 195 HIS C 207 1 13
HELIX 10 AB1 ASN C 210 PHE C 214 5 5
HELIX 11 AB2 SER C 215 ALA C 227 1 13
HELIX 12 AB3 LYS C 228 ALA C 241 1 14
HELIX 13 AB4 ALA C 241 ALA C 253 1 13
HELIX 14 AB5 THR C 274 ALA C 284 1 11
HELIX 15 AB6 TRP C 298 CYS C 303 1 6
HELIX 16 AB7 CYS C 303 ARG C 317 1 15
HELIX 17 AB8 THR D 66 HIS D 71 5 6
HELIX 18 AB9 GLN D 72 ALA D 78 1 7
HELIX 19 AC1 SER D 102 SER D 118 1 17
HELIX 20 AC2 ASP D 129 ASN D 134 1 6
HELIX 21 AC3 THR D 135 ASN D 142 1 8
HELIX 22 AC4 ASP D 158 PHE D 164 5 7
HELIX 23 AC5 TRP D 176 ALA D 183 1 8
HELIX 24 AC6 ARG D 186 ALA D 193 1 8
HELIX 25 AC7 LYS D 195 HIS D 207 1 13
HELIX 26 AC8 ASN D 210 PHE D 214 5 5
HELIX 27 AC9 SER D 215 ALA D 227 1 13
HELIX 28 AD1 LYS D 228 ALA D 241 1 14
HELIX 29 AD2 ALA D 241 ALA D 253 1 13
HELIX 30 AD3 THR D 274 ALA D 282 1 9
HELIX 31 AD4 TRP D 298 CYS D 303 1 6
HELIX 32 AD5 CYS D 303 ARG D 317 1 15
HELIX 33 AD6 THR A 66 HIS A 71 5 6
HELIX 34 AD7 LEU A 73 ALA A 78 1 6
HELIX 35 AD8 SER A 102 SER A 118 1 17
HELIX 36 AD9 ASP A 129 ASN A 134 1 6
HELIX 37 AE1 THR A 135 ASN A 142 1 8
HELIX 38 AE2 ASP A 158 PHE A 164 5 7
HELIX 39 AE3 TRP A 176 ALA A 183 1 8
HELIX 40 AE4 ARG A 186 ALA A 193 1 8
HELIX 41 AE5 LYS A 195 HIS A 207 1 13
HELIX 42 AE6 ASN A 210 PHE A 214 5 5
HELIX 43 AE7 SER A 215 ALA A 227 1 13
HELIX 44 AE8 LYS A 228 ALA A 241 1 14
HELIX 45 AE9 ALA A 241 ALA A 253 1 13
HELIX 46 AF1 THR A 274 ALA A 284 1 11
HELIX 47 AF2 TRP A 298 CYS A 303 1 6
HELIX 48 AF3 CYS A 303 SER A 316 1 14
HELIX 49 AF4 THR B 66 HIS B 71 5 6
HELIX 50 AF5 GLN B 72 ALA B 78 1 7
HELIX 51 AF6 SER B 102 SER B 118 1 17
HELIX 52 AF7 ASP B 129 ASN B 134 1 6
HELIX 53 AF8 THR B 135 ASN B 142 1 8
HELIX 54 AF9 ASP B 158 PHE B 164 5 7
HELIX 55 AG1 TRP B 176 ALA B 183 1 8
HELIX 56 AG2 ARG B 186 ALA B 193 1 8
HELIX 57 AG3 LYS B 195 HIS B 207 1 13
HELIX 58 AG4 SER B 215 LYS B 228 1 14
HELIX 59 AG5 LYS B 228 ALA B 241 1 14
HELIX 60 AG6 ALA B 241 ALA B 253 1 13
HELIX 61 AG7 THR B 274 ALA B 284 1 11
HELIX 62 AG8 TRP B 298 CYS B 303 1 6
HELIX 63 AG9 CYS B 303 ARG B 317 1 15
SHEET 1 AA1 8 GLU C 35 VAL C 41 0
SHEET 2 AA1 8 VAL C 44 GLY C 52 -1 O VAL C 44 N VAL C 41
SHEET 3 AA1 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA1 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 AA1 8 PHE C 123 HIS C 128 1 O VAL C 126 N VAL C 60
SHEET 6 AA1 8 ILE C 146 MET C 152 1 O VAL C 150 N ALA C 127
SHEET 7 AA1 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 AA1 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA2 8 GLU D 35 VAL D 41 0
SHEET 2 AA2 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
SHEET 3 AA2 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA2 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 AA2 8 PHE D 123 HIS D 128 1 O ASP D 124 N LEU D 56
SHEET 6 AA2 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA2 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA2 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA3 2 PHE D 167 THR D 168 0
SHEET 2 AA3 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SHEET 1 AA4 8 GLU A 35 VAL A 41 0
SHEET 2 AA4 8 VAL A 44 GLY A 52 -1 O VAL A 44 N VAL A 41
SHEET 3 AA4 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 AA4 8 LEU A 56 VAL A 60 1 N VAL A 57 O THR A 82
SHEET 5 AA4 8 PHE A 123 HIS A 128 1 O VAL A 126 N VAL A 60
SHEET 6 AA4 8 ILE A 146 MET A 152 1 O VAL A 150 N LEU A 125
SHEET 7 AA4 8 THR A 261 GLY A 266 1 O MET A 262 N TYR A 151
SHEET 8 AA4 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 AA5 8 PHE B 34 VAL B 41 0
SHEET 2 AA5 8 VAL B 44 GLY B 52 -1 O LYS B 50 N GLU B 35
SHEET 3 AA5 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 AA5 8 LEU B 56 VAL B 60 1 N VAL B 57 O THR B 82
SHEET 5 AA5 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 AA5 8 ILE B 146 MET B 152 1 O ALA B 147 N PHE B 123
SHEET 7 AA5 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 AA5 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 AA6 2 PHE B 167 THR B 168 0
SHEET 2 AA6 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SSBOND 1 CYS C 295 CYS C 303 1555 1555 2.01
SSBOND 2 CYS D 295 CYS D 303 1555 1555 1.96
SSBOND 3 CYS A 295 CYS A 303 1555 1555 2.02
SSBOND 4 CYS B 295 CYS B 303 1555 1555 2.00
LINK OD1 ASP C 129 C3 FEH C 401 1555 1555 1.39
LINK OD1 ASP D 129 C3 FEH D 401 1555 1555 1.39
LINK OD1 ASP A 129 C3 FEH A 401 1555 1555 1.39
LINK OD1 ASP B 129 C3 FEH B 401 1555 1555 1.38
SITE 1 AC1 6 ASP C 129 HIS C 177 PHE C 178 HIS C 207
SITE 2 AC1 6 TYR C 239 HIS C 297
SITE 1 AC2 16 GLY A 62 PHE A 63 HIS A 128 ILE A 130
SITE 2 AC2 16 GLY A 131 ILE A 132 MET A 152 GLN A 153
SITE 3 AC2 16 ALA A 154 HIS A 177 PHE A 178 TYR A 239
SITE 4 AC2 16 MET A 272 HIS A 297 HOH A 512 HOH A 652
SITE 1 AC3 15 GLY B 62 PHE B 63 HIS B 128 ILE B 130
SITE 2 AC3 15 GLY B 131 ILE B 132 MET B 152 GLN B 153
SITE 3 AC3 15 ALA B 154 HIS B 177 PHE B 178 HIS B 207
SITE 4 AC3 15 TYR B 239 HIS B 297 HOH B 645
SITE 1 AC4 14 GLY D 62 PHE D 63 HIS D 128 ILE D 130
SITE 2 AC4 14 GLY D 131 ILE D 132 MET D 152 GLN D 153
SITE 3 AC4 14 ALA D 154 HIS D 177 PHE D 178 TYR D 239
SITE 4 AC4 14 HIS D 297 HOH D 663
CRYST1 168.173 83.979 89.169 90.00 100.55 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 0.005946 0.000000 0.001108 0.00000
SCALE2 0.000000 0.011908 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011408 0.00000
TER 2408 ARG C 317
TER 4764 ARG D 317
TER 7169 ARG A 317
TER 9536 ARG B 317
MASTER 466 0 4 63 36 0 14 610544 4 48 96
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