| content |
HEADER HYDROLASE 14-OCT-16 5TNK
TITLE CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING THE ADDUCTED 1,2-EPOXYOCTANE 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 5TNK 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. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 146702
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7340
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 19.6972 - 5.0981 1.00 4663 367 0.1544 0.1810
REMARK 3 2 5.0981 - 4.0581 1.00 4949 0 0.1257 0.0000
REMARK 3 3 4.0581 - 3.5486 1.00 4567 367 0.1414 0.1478
REMARK 3 4 3.5486 - 3.2257 1.00 4533 367 0.1414 0.1602
REMARK 3 5 3.2257 - 2.9953 1.00 4928 0 0.1547 0.0000
REMARK 3 6 2.9953 - 2.8193 1.00 4545 367 0.1578 0.1743
REMARK 3 7 2.8193 - 2.6784 1.00 4534 367 0.1479 0.1646
REMARK 3 8 2.6784 - 2.5621 1.00 4887 0 0.1539 0.0000
REMARK 3 9 2.5621 - 2.4636 1.00 4525 367 0.1570 0.1733
REMARK 3 10 2.4636 - 2.3788 1.00 4521 367 0.1525 0.1716
REMARK 3 11 2.3788 - 2.3045 1.00 4906 0 0.1479 0.0000
REMARK 3 12 2.3045 - 2.2387 1.00 4456 367 0.1527 0.1750
REMARK 3 13 2.2387 - 2.1799 1.00 4562 367 0.1509 0.1800
REMARK 3 14 2.1799 - 2.1268 1.00 4884 0 0.1511 0.0000
REMARK 3 15 2.1268 - 2.0785 1.00 4495 367 0.1483 0.1788
REMARK 3 16 2.0785 - 2.0343 1.00 4567 367 0.1522 0.1811
REMARK 3 17 2.0343 - 1.9936 1.00 4845 0 0.1557 0.0000
REMARK 3 18 1.9936 - 1.9560 1.00 4502 367 0.1534 0.1980
REMARK 3 19 1.9560 - 1.9211 1.00 4503 367 0.1514 0.1611
REMARK 3 20 1.9211 - 1.8886 1.00 4868 0 0.1570 0.0000
REMARK 3 21 1.8886 - 1.8582 1.00 4533 367 0.1649 0.2099
REMARK 3 22 1.8582 - 1.8296 1.00 4481 367 0.1643 0.1974
REMARK 3 23 1.8296 - 1.8027 1.00 4887 0 0.1619 0.0000
REMARK 3 24 1.8027 - 1.7773 1.00 4497 367 0.1566 0.1931
REMARK 3 25 1.7773 - 1.7533 1.00 4508 367 0.1605 0.1982
REMARK 3 26 1.7533 - 1.7306 1.00 4896 0 0.1654 0.0000
REMARK 3 27 1.7306 - 1.7089 1.00 4492 367 0.1674 0.1905
REMARK 3 28 1.7089 - 1.6884 1.00 4502 367 0.1679 0.2099
REMARK 3 29 1.6884 - 1.6687 1.00 4897 0 0.1797 0.0000
REMARK 3 30 1.6687 - 1.6500 1.00 4429 367 0.1840 0.2282
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.390
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 9831
REMARK 3 ANGLE : 0.810 13343
REMARK 3 CHIRALITY : 0.052 1366
REMARK 3 PLANARITY : 0.006 1753
REMARK 3 DIHEDRAL : 14.084 5779
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 25:325 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.1451 54.2060 27.3236
REMARK 3 T TENSOR
REMARK 3 T11: 0.0803 T22: 0.0934
REMARK 3 T33: 0.0621 T12: 0.0004
REMARK 3 T13: 0.0074 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 0.7445 L22: 0.6741
REMARK 3 L33: 0.6366 L12: 0.0460
REMARK 3 L13: 0.1405 L23: 0.0514
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: -0.1069 S13: -0.0783
REMARK 3 S21: 0.0575 S22: -0.0172 S23: 0.0489
REMARK 3 S31: 0.0809 S32: -0.0478 S33: 0.0073
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN B AND RESID 25:317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.2430 93.3854 15.6409
REMARK 3 T TENSOR
REMARK 3 T11: 0.0852 T22: 0.0784
REMARK 3 T33: 0.1075 T12: 0.0133
REMARK 3 T13: -0.0220 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.0535 L22: 1.1308
REMARK 3 L33: 0.5207 L12: -0.3790
REMARK 3 L13: -0.0140 L23: -0.0724
REMARK 3 S TENSOR
REMARK 3 S11: -0.0176 S12: 0.0137 S13: 0.1495
REMARK 3 S21: -0.0401 S22: 0.0132 S23: 0.0430
REMARK 3 S31: -0.0832 S32: -0.0279 S33: 0.0034
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN C AND RESID 26:317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 89.9521 86.2111 26.9233
REMARK 3 T TENSOR
REMARK 3 T11: 0.0797 T22: 0.0822
REMARK 3 T33: 0.1004 T12: 0.0046
REMARK 3 T13: 0.0028 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.6504 L22: 0.8481
REMARK 3 L33: 0.6594 L12: 0.0643
REMARK 3 L13: 0.0252 L23: 0.0492
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: -0.0528 S13: 0.1170
REMARK 3 S21: 0.0369 S22: -0.0209 S23: -0.0854
REMARK 3 S31: -0.0771 S32: 0.0357 S33: 0.0174
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN D AND RESID 25:325 )
REMARK 3 ORIGIN FOR THE GROUP (A): 98.8272 46.9979 15.7291
REMARK 3 T TENSOR
REMARK 3 T11: 0.0816 T22: 0.0837
REMARK 3 T33: 0.0600 T12: 0.0190
REMARK 3 T13: 0.0078 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.0012 L22: 0.9668
REMARK 3 L33: 0.4971 L12: -0.2923
REMARK 3 L13: -0.0661 L23: 0.1469
REMARK 3 S TENSOR
REMARK 3 S11: 0.0264 S12: 0.0409 S13: -0.0412
REMARK 3 S21: -0.0207 S22: -0.0136 S23: -0.1063
REMARK 3 S31: 0.0419 S32: 0.0156 S33: -0.0104
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 5TNK 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_1000221651.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-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) : 1.0781
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 MARCH 30, 2013
REMARK 200 DATA SCALING SOFTWARE : XDS JULY 4, 2012
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 146707
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 19.696
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.520
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.43
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.640
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 (%): 45.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
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 84.10350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.04650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.10350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.04650
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: 2820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20830 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: 2770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 A 745 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 778 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 816 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 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 465 HIS A 329
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 ALA C 25
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 HIS D 326
REMARK 465 HIS D 327
REMARK 465 HIS D 328
REMARK 465 HIS D 329
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 OE1 GLU C 189 O HOH C 501 2.02
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 A 730 O HOH D 704 2655 2.15
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 -130.49 60.86
REMARK 500 ALA A 154 148.48 178.97
REMARK 500 ASP A 184 -179.74 -69.01
REMARK 500 CYS A 303 54.21 -142.80
REMARK 500 THR B 99 -71.73 -90.91
REMARK 500 ASP B 129 -129.02 60.50
REMARK 500 ALA B 154 148.25 176.99
REMARK 500 TRP B 298 57.99 -92.25
REMARK 500 ASP C 129 -129.90 60.46
REMARK 500 ALA C 154 148.70 179.28
REMARK 500 CYS C 303 55.64 -142.43
REMARK 500 THR D 99 -68.06 -90.04
REMARK 500 ASP D 129 -130.13 57.86
REMARK 500 ALA D 154 149.28 177.81
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 817 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 818 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH C 806 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH D 816 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH D 817 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH D 818 DISTANCE = 6.88 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7F2 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7F2 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7F2 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7F2 D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TND 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: 5TNL RELATED DB: PDB
REMARK 900 RELATED ID: 5TNM RELATED DB: PDB
REMARK 900 RELATED ID: 5TNN RELATED DB: PDB
REMARK 900 RELATED ID: 5TNR RELATED DB: PDB
REMARK 900 RELATED ID: 5TNS RELATED DB: PDB
DBREF1 5TNK A 25 329 UNP A0A0M3KL26_PSEAB
DBREF2 5TNK A A0A0M3KL26 1 301
DBREF1 5TNK B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNK B A0A0M3KL26 1 301
DBREF1 5TNK C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNK C A0A0M3KL26 1 301
DBREF1 5TNK D 25 329 UNP A0A0M3KL26_PSEAB
DBREF2 5TNK D A0A0M3KL26 1 301
SEQADV 5TNK GLN A 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNK GLN B 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNK GLN C 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNK 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 7F2 A 401 9
HET 7F2 B 401 9
HET 7F2 C 401 9
HET 7F2 D 401 9
HETNAM 7F2 (2R)-OCTANE-1,2-DIOL
FORMUL 5 7F2 4(C8 H18 O2)
FORMUL 9 HOH *1227(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 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 SER B 215 LYS B 228 1 14
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 284 1 11
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 TRP C 176 ALA C 183 1 8
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 282 1 9
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 ALA D 284 1 11
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 ASP A 124 N LEU A 56
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 PHE B 34 VAL B 41 0
SHEET 2 AA2 8 VAL B 44 GLY B 52 -1 O TYR B 48 N ALA B 37
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 THR B 82
SHEET 5 AA2 8 PHE B 123 HIS B 128 1 O ASP B 124 N LEU B 56
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 ALA C 147 N PHE C 123
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 2 PHE C 167 THR C 168 0
SHEET 2 AA5 2 GLY C 171 GLU C 172 -1 O GLY C 171 N THR C 168
SHEET 1 AA6 8 PHE D 34 VAL D 41 0
SHEET 2 AA6 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
SHEET 3 AA6 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA6 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 AA6 8 PHE D 123 HIS D 128 1 O VAL D 126 N VAL D 60
SHEET 6 AA6 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA6 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA6 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA7 2 PHE D 167 THR D 168 0
SHEET 2 AA7 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 2.01
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 OD1 ASP A 129 CA A7F2 A 401 1555 1555 1.39
LINK OD1 ASP B 129 CA A7F2 B 401 1555 1555 1.39
LINK OD1 ASP C 129 CA A7F2 C 401 1555 1555 1.39
LINK OD1 ASP D 129 CA A7F2 D 401 1555 1555 1.40
SITE 1 AC1 9 GLN A 153 LEU A 174 HIS A 177 PHE A 178
SITE 2 AC1 9 HIS A 207 TYR A 239 MET A 272 HIS A 297
SITE 3 AC1 9 HOH A 516
SITE 1 AC2 7 VAL B 175 HIS B 177 PHE B 178 HIS B 207
SITE 2 AC2 7 TYR B 239 GLY B 270 HIS B 297
SITE 1 AC3 7 GLN C 153 HIS C 177 PHE C 178 HIS C 207
SITE 2 AC3 7 TYR C 239 GLY C 270 HIS C 297
SITE 1 AC4 6 HIS D 177 PHE D 178 TYR D 239 GLY D 270
SITE 2 AC4 6 MET D 272 HIS D 297
CRYST1 168.207 84.093 89.246 90.00 100.39 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 0.005945 0.000000 0.001090 0.00000
SCALE2 0.000000 0.011892 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011392 0.00000
TER 2412 HIS A 325
TER 4755 ARG B 317
TER 7128 ARG C 317
TER 9502 HIS D 325
MASTER 441 0 4 63 38 0 9 610680 4 48 96
END |