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HEADER HYDROLASE 14-OCT-16 5TNI
TITLE CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING THE ADDUCTED S-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 5TNI 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. 1.80 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 112236
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5639
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 19.9525 - 5.5539 1.00 3546 282 0.1516 0.1835
REMARK 3 2 5.5539 - 4.4241 1.00 3803 0 0.1270 0.0000
REMARK 3 3 4.4241 - 3.8695 1.00 3503 282 0.1260 0.1326
REMARK 3 4 3.8695 - 3.5178 1.00 3477 282 0.1345 0.1428
REMARK 3 5 3.5178 - 3.2668 1.00 3755 0 0.1305 0.0000
REMARK 3 6 3.2668 - 3.0749 1.00 3472 282 0.1421 0.1613
REMARK 3 7 3.0749 - 2.9214 1.00 3470 282 0.1514 0.1770
REMARK 3 8 2.9214 - 2.7946 1.00 3740 0 0.1497 0.0000
REMARK 3 9 2.7946 - 2.6873 1.00 3453 282 0.1440 0.1958
REMARK 3 10 2.6873 - 2.5948 1.00 3474 282 0.1489 0.1729
REMARK 3 11 2.5948 - 2.5138 1.00 3765 0 0.1463 0.0000
REMARK 3 12 2.5138 - 2.4421 1.00 3440 282 0.1469 0.1807
REMARK 3 13 2.4421 - 2.3779 1.00 3455 282 0.1451 0.1831
REMARK 3 14 2.3779 - 2.3200 1.00 3703 0 0.1402 0.0000
REMARK 3 15 2.3200 - 2.2673 1.00 3483 282 0.1406 0.1767
REMARK 3 16 2.2673 - 2.2191 1.00 3426 282 0.1426 0.1849
REMARK 3 17 2.2191 - 2.1748 1.00 3727 0 0.1413 0.0000
REMARK 3 18 2.1748 - 2.1338 1.00 3463 282 0.1423 0.1832
REMARK 3 19 2.1338 - 2.0957 1.00 3433 282 0.1429 0.1937
REMARK 3 20 2.0957 - 2.0602 1.00 3758 0 0.1503 0.0000
REMARK 3 21 2.0602 - 2.0270 1.00 3449 282 0.1471 0.1977
REMARK 3 22 2.0270 - 1.9959 1.00 3400 282 0.1499 0.1848
REMARK 3 23 1.9959 - 1.9665 1.00 3752 0 0.1458 0.0000
REMARK 3 24 1.9665 - 1.9389 1.00 3413 282 0.1397 0.1848
REMARK 3 25 1.9389 - 1.9127 1.00 3411 282 0.1451 0.1756
REMARK 3 26 1.9127 - 1.8879 1.00 3796 0 0.1575 0.0000
REMARK 3 27 1.8879 - 1.8643 1.00 3403 282 0.1707 0.2284
REMARK 3 28 1.8643 - 1.8418 1.00 3494 282 0.1817 0.2229
REMARK 3 29 1.8418 - 1.8204 1.00 3643 0 0.1766 0.0000
REMARK 3 30 1.8204 - 1.8000 1.00 3490 281 0.1871 0.2319
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.750
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 9940
REMARK 3 ANGLE : 0.814 13514
REMARK 3 CHIRALITY : 0.053 1382
REMARK 3 PLANARITY : 0.006 1783
REMARK 3 DIHEDRAL : 12.519 5852
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 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.9738 54.3102 27.2767
REMARK 3 T TENSOR
REMARK 3 T11: 0.0936 T22: 0.1049
REMARK 3 T33: 0.0727 T12: 0.0033
REMARK 3 T13: 0.0063 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.6855 L22: 0.7687
REMARK 3 L33: 0.7194 L12: 0.1020
REMARK 3 L13: 0.0910 L23: 0.0339
REMARK 3 S TENSOR
REMARK 3 S11: 0.0117 S12: -0.0807 S13: -0.0850
REMARK 3 S21: 0.0608 S22: -0.0128 S23: 0.0185
REMARK 3 S31: 0.0896 S32: -0.0406 S33: 0.0083
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.1515 93.2190 15.4797
REMARK 3 T TENSOR
REMARK 3 T11: 0.0918 T22: 0.0932
REMARK 3 T33: 0.1178 T12: 0.0139
REMARK 3 T13: -0.0215 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.9146 L22: 0.9962
REMARK 3 L33: 0.4493 L12: -0.2440
REMARK 3 L13: -0.0342 L23: -0.0913
REMARK 3 S TENSOR
REMARK 3 S11: -0.0226 S12: 0.0128 S13: 0.1337
REMARK 3 S21: -0.0401 S22: 0.0173 S23: 0.0658
REMARK 3 S31: -0.0676 S32: -0.0265 S33: 0.0058
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESID 25:320)
REMARK 3 ORIGIN FOR THE GROUP (A): 89.7622 86.4108 27.0617
REMARK 3 T TENSOR
REMARK 3 T11: 0.0905 T22: 0.0944
REMARK 3 T33: 0.1069 T12: 0.0053
REMARK 3 T13: 0.0059 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.6277 L22: 0.9382
REMARK 3 L33: 0.7390 L12: 0.0368
REMARK 3 L13: 0.0153 L23: 0.0447
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: -0.0278 S13: 0.1207
REMARK 3 S21: 0.0483 S22: -0.0211 S23: -0.0675
REMARK 3 S31: -0.0875 S32: 0.0255 S33: 0.0187
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESID 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 98.6905 47.1245 15.6954
REMARK 3 T TENSOR
REMARK 3 T11: 0.0946 T22: 0.0975
REMARK 3 T33: 0.0745 T12: 0.0211
REMARK 3 T13: 0.0071 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.8698 L22: 0.9253
REMARK 3 L33: 0.5210 L12: -0.1795
REMARK 3 L13: -0.0231 L23: 0.1344
REMARK 3 S TENSOR
REMARK 3 S11: 0.0261 S12: 0.0437 S13: -0.0528
REMARK 3 S21: -0.0189 S22: -0.0106 S23: -0.1150
REMARK 3 S31: 0.0533 S32: 0.0255 S33: -0.0156
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 5TNI 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_1000221221.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-13
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 : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS SEPT 26, 2012
REMARK 200 DATA SCALING SOFTWARE : XDS JULY 4, 2012
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112243
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 19.951
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.590
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.57
REMARK 200 R MERGE FOR SHELL (I) : 0.40800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.610
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.10_2155
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
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 83.92150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.83850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 83.92150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.83850
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: 2760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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: 2750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 C 737 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 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 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 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 O HOH D 624 O HOH D 685 2.14
REMARK 500 O HOH A 572 O HOH A 701 2.15
REMARK 500 OE2 GLU C 189 O HOH C 501 2.18
REMARK 500 O HOH D 722 O HOH D 725 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 A 129 -129.87 59.73
REMARK 500 GLN A 153 61.63 60.06
REMARK 500 ALA A 154 147.87 173.86
REMARK 500 GLN A 170 -97.91 -100.44
REMARK 500 GLU A 172 130.70 -38.31
REMARK 500 ASP A 184 -174.30 -68.03
REMARK 500 CYS A 303 58.09 -141.43
REMARK 500 THR B 99 -63.95 -94.14
REMARK 500 ASP B 129 -128.82 56.47
REMARK 500 ALA B 154 147.02 174.05
REMARK 500 CYS B 303 54.92 -141.93
REMARK 500 ASP C 129 -129.23 60.29
REMARK 500 ALA C 154 150.10 175.82
REMARK 500 CYS C 303 56.87 -140.90
REMARK 500 ARG C 319 93.57 -172.86
REMARK 500 THR D 99 -62.25 -93.76
REMARK 500 ASP D 129 -129.49 57.57
REMARK 500 GLN D 153 60.38 61.36
REMARK 500 ALA D 154 149.60 175.17
REMARK 500 CYS D 303 55.23 -142.97
REMARK 500 ARG D 319 165.71 65.30
REMARK 500 HIS D 320 -167.83 -176.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FEH IS BOUND FORM OF (S)-STYRENE OXIDE, ITS CA 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 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
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: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide FEH C 401 and ASP C
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: 5TNQ RELATED DB: PDB
REMARK 900 RELATED ID: 5TNR RELATED DB: PDB
REMARK 900 RELATED ID: 5TNS RELATED DB: PDB
DBREF1 5TNI A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNI A A0A0M3KL26 1 301
DBREF1 5TNI B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNI B A0A0M3KL26 1 301
DBREF1 5TNI C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNI C A0A0M3KL26 1 301
DBREF1 5TNI D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNI D A0A0M3KL26 1 301
SEQADV 5TNI GLN A 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNI GLN B 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNI GLN C 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNI 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 B 401 9
HET FEH C 401 9
HET FEH D 401 9
HETNAM FEH (1R)-1-PHENYLETHANE-1,2-DIOL
FORMUL 5 FEH 4(C8 H10 O2)
FORMUL 9 HOH *1023(H2 O)
HELIX 1 AA1 THR A 66 HIS A 71 5 6
HELIX 2 AA2 GLN A 72 ALA A 78 1 7
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 282 1 9
HELIX 15 AB6 TRP A 298 CYS A 303 1 6
HELIX 16 AB7 CYS A 303 SER A 316 1 14
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 ASN B 210 PHE B 214 5 5
HELIX 27 AC9 SER B 215 LYS B 228 1 14
HELIX 28 AD1 LYS B 228 ALA B 241 1 14
HELIX 29 AD2 ALA B 241 ALA B 253 1 13
HELIX 30 AD3 THR B 274 ALA B 282 1 9
HELIX 31 AD4 TRP B 298 CYS B 303 1 6
HELIX 32 AD5 CYS B 303 ARG B 317 1 15
HELIX 33 AD6 THR C 66 HIS C 71 5 6
HELIX 34 AD7 GLN C 72 ALA C 78 1 7
HELIX 35 AD8 SER C 102 SER C 118 1 17
HELIX 36 AD9 ASP C 129 ASN C 134 1 6
HELIX 37 AE1 THR C 135 ASN C 142 1 8
HELIX 38 AE2 ASP C 158 PHE C 164 5 7
HELIX 39 AE3 TRP C 176 ALA C 183 1 8
HELIX 40 AE4 ARG C 186 ALA C 193 1 8
HELIX 41 AE5 LYS C 195 HIS C 207 1 13
HELIX 42 AE6 ASN C 210 PHE C 214 5 5
HELIX 43 AE7 SER C 215 ALA C 227 1 13
HELIX 44 AE8 LYS C 228 ALA C 241 1 14
HELIX 45 AE9 ALA C 241 ALA C 253 1 13
HELIX 46 AF1 THR C 274 ALA C 282 1 9
HELIX 47 AF2 TRP C 298 CYS C 303 1 6
HELIX 48 AF3 CYS C 303 SER C 316 1 14
HELIX 49 AF4 THR D 66 HIS D 71 5 6
HELIX 50 AF5 GLN D 72 ALA D 78 1 7
HELIX 51 AF6 SER D 102 SER D 118 1 17
HELIX 52 AF7 ASP D 129 ASN D 134 1 6
HELIX 53 AF8 THR D 135 ASN D 142 1 8
HELIX 54 AF9 ASP D 158 PHE D 164 5 7
HELIX 55 AG1 TRP D 176 ALA D 183 1 8
HELIX 56 AG2 ARG D 186 ALA D 193 1 8
HELIX 57 AG3 LYS D 195 HIS D 207 1 13
HELIX 58 AG4 ASN D 210 PHE D 214 5 5
HELIX 59 AG5 SER D 215 ALA D 227 1 13
HELIX 60 AG6 LYS D 228 ALA D 241 1 14
HELIX 61 AG7 ALA D 241 ALA D 253 1 13
HELIX 62 AG8 THR D 274 ALA D 282 1 9
HELIX 63 AG9 TRP D 298 CYS D 303 1 6
HELIX 64 AH1 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 LYS A 50 N GLU A 35
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 8 GLU B 35 VAL B 41 0
SHEET 2 AA2 8 VAL B 44 GLY B 52 -1 O LEU B 46 N ARG B 39
SHEET 3 AA2 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 AA2 8 LEU B 56 VAL B 60 1 N VAL B 57 O ILE B 84
SHEET 5 AA2 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 AA2 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 AA2 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 AA2 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 AA3 2 PHE B 167 THR B 168 0
SHEET 2 AA3 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SHEET 1 AA4 8 GLU C 35 VAL C 41 0
SHEET 2 AA4 8 VAL C 44 GLY C 52 -1 O VAL C 44 N VAL C 41
SHEET 3 AA4 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA4 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 AA4 8 PHE C 123 HIS C 128 1 O VAL C 126 N VAL C 60
SHEET 6 AA4 8 ILE C 146 MET C 152 1 O VAL C 150 N LEU C 125
SHEET 7 AA4 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 AA4 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA5 8 GLU D 35 VAL D 41 0
SHEET 2 AA5 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
SHEET 3 AA5 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA5 8 LEU D 56 VAL D 60 1 N VAL D 57 O ILE D 84
SHEET 5 AA5 8 PHE D 123 HIS D 128 1 O ASP D 124 N LEU D 56
SHEET 6 AA5 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA5 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA5 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA6 2 PHE D 167 THR D 168 0
SHEET 2 AA6 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 2.00
SSBOND 2 CYS B 295 CYS B 303 1555 1555 1.98
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.00
SSBOND 4 CYS D 295 CYS D 303 1555 1555 1.97
LINK OD1 ASP A 129 C1 FEH A 401 1555 1555 1.39
LINK OD1 ASP B 129 C1 FEH B 401 1555 1555 1.39
LINK OD1 ASP C 129 C1 FEH C 401 1555 1555 1.39
LINK OD1 ASP D 129 C1 FEH D 401 1555 1555 1.39
SITE 1 AC1 6 ASP A 129 HIS A 177 PHE A 178 HIS A 207
SITE 2 AC1 6 TYR A 239 HIS A 297
SITE 1 AC2 14 PHE B 63 HIS B 128 ILE B 130 GLY B 131
SITE 2 AC2 14 ILE B 132 MET B 152 GLN B 153 ALA B 154
SITE 3 AC2 14 HIS B 177 PHE B 178 HIS B 207 TYR B 239
SITE 4 AC2 14 HIS B 297 HOH B 651
SITE 1 AC3 14 PHE C 63 HIS C 128 ILE C 130 GLY C 131
SITE 2 AC3 14 ILE C 132 MET C 152 GLN C 153 ALA C 154
SITE 3 AC3 14 HIS C 177 PHE C 178 HIS C 207 TYR C 239
SITE 4 AC3 14 HIS C 297 HOH C 645
SITE 1 AC4 14 PHE D 63 HIS D 128 ILE D 130 GLY D 131
SITE 2 AC4 14 ILE D 132 MET D 152 GLN D 153 ALA D 154
SITE 3 AC4 14 HIS D 177 PHE D 178 HIS D 207 TYR D 239
SITE 4 AC4 14 HIS D 297 HOH D 665
CRYST1 167.843 83.677 89.133 90.00 100.37 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 0.005958 0.000000 0.001090 0.00000
SCALE2 0.000000 0.011951 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011405 0.00000
TER 2435 HIS A 321
TER 4804 ARG B 317
TER 7216 HIS C 320
TER 9595 HIS D 321
MASTER 428 0 4 64 36 0 14 610506 4 48 96
END |