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HEADER HYDROLASE 14-OCT-16 5TNJ
TITLE CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING THE ADDUCTED 4-VINYL-1-CYCLOHEXENE 1,2-EPOXIDE
TITLE 3 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 5TNJ 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 (1.11_2567: ???)
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 145781
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7288
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 19.9067 - 5.0990 1.00 4635 365 0.1467 0.1716
REMARK 3 2 5.0990 - 4.0585 1.00 4920 0 0.1209 0.0000
REMARK 3 3 4.0585 - 3.5488 1.00 4564 365 0.1371 0.1524
REMARK 3 4 3.5488 - 3.2258 1.00 4496 365 0.1374 0.1691
REMARK 3 5 3.2258 - 2.9954 1.00 4885 0 0.1519 0.0000
REMARK 3 6 2.9954 - 2.8193 1.00 4524 365 0.1542 0.1833
REMARK 3 7 2.8193 - 2.6785 1.00 4517 365 0.1461 0.1684
REMARK 3 8 2.6785 - 2.5621 1.00 4856 0 0.1517 0.0000
REMARK 3 9 2.5621 - 2.4637 1.00 4485 365 0.1507 0.1757
REMARK 3 10 2.4637 - 2.3788 1.00 4514 365 0.1522 0.1571
REMARK 3 11 2.3788 - 2.3045 1.00 4883 0 0.1411 0.0000
REMARK 3 12 2.3045 - 2.2388 1.00 4452 364 0.1426 0.1622
REMARK 3 13 2.2388 - 2.1799 1.00 4505 365 0.1407 0.1655
REMARK 3 14 2.1799 - 2.1268 1.00 4859 0 0.1437 0.0000
REMARK 3 15 2.1268 - 2.0785 1.00 4472 365 0.1411 0.1671
REMARK 3 16 2.0785 - 2.0343 1.00 4492 365 0.1445 0.1833
REMARK 3 17 2.0343 - 1.9936 1.00 4868 0 0.1473 0.0000
REMARK 3 18 1.9936 - 1.9560 1.00 4490 365 0.1460 0.1894
REMARK 3 19 1.9560 - 1.9211 1.00 4482 365 0.1430 0.1727
REMARK 3 20 1.9211 - 1.8886 1.00 4841 0 0.1449 0.0000
REMARK 3 21 1.8886 - 1.8582 1.00 4480 365 0.1583 0.1854
REMARK 3 22 1.8582 - 1.8296 1.00 4498 365 0.1568 0.1963
REMARK 3 23 1.8296 - 1.8027 1.00 4841 0 0.1510 0.0000
REMARK 3 24 1.8027 - 1.7773 1.00 4423 365 0.1435 0.1768
REMARK 3 25 1.7773 - 1.7533 1.00 4550 365 0.1508 0.1948
REMARK 3 26 1.7533 - 1.7306 1.00 4850 0 0.1572 0.0000
REMARK 3 27 1.7306 - 1.7089 1.00 4458 365 0.1583 0.2012
REMARK 3 28 1.7089 - 1.6884 1.00 4488 365 0.1593 0.1903
REMARK 3 29 1.6884 - 1.6687 0.99 4827 0 0.1585 0.0000
REMARK 3 30 1.6687 - 1.6500 0.97 4338 354 0.1695 0.1966
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) : 15.280
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 9958
REMARK 3 ANGLE : 0.832 13562
REMARK 3 CHIRALITY : 0.053 1403
REMARK 3 PLANARITY : 0.006 1776
REMARK 3 DIHEDRAL : 14.448 5851
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): 62.0891 54.5222 27.2305
REMARK 3 T TENSOR
REMARK 3 T11: 0.0900 T22: 0.0957
REMARK 3 T33: 0.0735 T12: 0.0036
REMARK 3 T13: 0.0086 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.6826 L22: 0.6573
REMARK 3 L33: 0.7288 L12: 0.0152
REMARK 3 L13: 0.1043 L23: -0.0053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: -0.0773 S13: -0.0704
REMARK 3 S21: 0.0572 S22: -0.0235 S23: 0.0416
REMARK 3 S31: 0.0929 S32: -0.0362 S33: 0.0189
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.1991 93.3040 15.4789
REMARK 3 T TENSOR
REMARK 3 T11: 0.0907 T22: 0.0890
REMARK 3 T33: 0.1169 T12: 0.0181
REMARK 3 T13: -0.0214 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.9967 L22: 1.1473
REMARK 3 L33: 0.5641 L12: -0.2632
REMARK 3 L13: 0.0304 L23: -0.1530
REMARK 3 S TENSOR
REMARK 3 S11: -0.0186 S12: 0.0084 S13: 0.1388
REMARK 3 S21: -0.0467 S22: 0.0112 S23: 0.0751
REMARK 3 S31: -0.0846 S32: -0.0302 S33: 0.0058
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 89.8855 86.1221 27.1154
REMARK 3 T TENSOR
REMARK 3 T11: 0.0941 T22: 0.0908
REMARK 3 T33: 0.1207 T12: 0.0062
REMARK 3 T13: 0.0012 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.6878 L22: 0.8998
REMARK 3 L33: 0.7533 L12: -0.0133
REMARK 3 L13: 0.0598 L23: 0.0700
REMARK 3 S TENSOR
REMARK 3 S11: 0.0061 S12: -0.0213 S13: 0.1229
REMARK 3 S21: 0.0452 S22: -0.0377 S23: -0.0928
REMARK 3 S31: -0.0981 S32: 0.0291 S33: 0.0300
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 98.8637 47.5476 15.7693
REMARK 3 T TENSOR
REMARK 3 T11: 0.0907 T22: 0.1000
REMARK 3 T33: 0.0727 T12: 0.0257
REMARK 3 T13: 0.0070 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.0253 L22: 0.9252
REMARK 3 L33: 0.5391 L12: -0.2216
REMARK 3 L13: -0.0876 L23: 0.1553
REMARK 3 S TENSOR
REMARK 3 S11: 0.0221 S12: 0.0559 S13: -0.0457
REMARK 3 S21: -0.0107 S22: -0.0152 S23: -0.1065
REMARK 3 S31: 0.0486 S32: 0.0123 S33: -0.0053
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 5TNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000221154.
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 : 145788
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 19.905
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.490
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.0200
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) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.99
REMARK 200 R MERGE FOR SHELL (I) : 0.35500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.080
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 (%): 45.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
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 84.17550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.71800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.17550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.71800
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: 20650 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: 20750 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 761 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 766 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 790 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 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 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 O HOH D 708 O HOH D 722 2.18
REMARK 500 NH1 ARG B 197 OD1 ASP B 220 2.19
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 -129.70 61.81
REMARK 500 ALA A 154 146.07 -179.42
REMARK 500 THR B 99 -69.53 -95.05
REMARK 500 ASP B 129 -130.26 59.55
REMARK 500 ALA B 154 147.58 -179.41
REMARK 500 ASP B 185 19.30 59.28
REMARK 500 ASP C 129 -129.21 61.31
REMARK 500 ALA C 154 146.87 -177.90
REMARK 500 CYS C 303 55.62 -140.85
REMARK 500 THR D 99 -67.06 -93.37
REMARK 500 ASP D 129 -129.10 57.33
REMARK 500 ALA D 154 148.09 179.78
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 D 790 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH D 791 DISTANCE = 6.28 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 LIGAND AVH ((1R,2R,4R)-4-ETHENYLCYCLOHEXANE-1,2-DIOL) OR 8MD ((1S,
REMARK 600 2S,4S)-4-ETHENYLCYCLOHEXANE-1,2-DIOL ) COVALENTLY LINKED TO THE
REMARK 600 PROTEIN CIF-E153Q, VIA ITS C1 ATOM TO OD1 ON ASP129 OF THE PROTEIN
REMARK 600 CHAIN A; IN CHAIN B, C AND D, LIGAND BVH ((1R,2R,4S)-4-
REMARK 600 ETHENYLCYCLOHEXANE-1,2-DIOL) OR DVH ((1S,2S,4R)-4-
REMARK 600 ETHENYLCYCLOHEXANE-1,2-DIOL) COVALENTLY LINKED TO THE PROTEIN CIF-
REMARK 600 E153Q, VIA ITS C6 ATOM TO OD1 ON ASP129 OF THE PROTEIN.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AVH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8MD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BVH 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 BVH B 401 and ASP B
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DVH B 402 and ASP B
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DVH B 402 and ASP B
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BVH C 401 and ASP C
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BVH C 401 and ASP C
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DVH C 402 and ASP C
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DVH C 402 and ASP C
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BVH D 401 and ASP D
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BVH D 401 and ASP D
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DVH D 402 and ASP D
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DVH D 402 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: 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: 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 5TNJ A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNJ A A0A0M3KL26 1 301
DBREF1 5TNJ B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNJ B A0A0M3KL26 1 301
DBREF1 5TNJ C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNJ C A0A0M3KL26 1 301
DBREF1 5TNJ D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNJ D A0A0M3KL26 1 301
SEQADV 5TNJ GLN A 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNJ GLN B 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNJ GLN C 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNJ 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 AVH A 401 9
HET 8MD A 402 9
HET BVH B 401 9
HET DVH B 402 9
HET BVH C 401 9
HET DVH C 402 9
HET BVH D 401 9
HET DVH D 402 9
HETNAM AVH (1R,2R,4R)-4-ETHENYLCYCLOHEXANE-1,2-DIOL
HETNAM 8MD (1S,2S,4S)-4-ETHENYLCYCLOHEXANE-1,2-DIOL
HETNAM BVH (1R,2R,4S)-4-ETHENYLCYCLOHEXANE-1,2-DIOL
HETNAM DVH (1S,2S,4R)-4-ETHENYLCYCLOHEXANE-1,2-DIOL
FORMUL 5 AVH C8 H14 O2
FORMUL 6 8MD C8 H14 O2
FORMUL 7 BVH 3(C8 H14 O2)
FORMUL 8 DVH 3(C8 H14 O2)
FORMUL 13 HOH *1138(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 LYS A 281 1 8
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 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 ALA D 282 1 9
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 VAL A 150 N LEU A 125
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 PHE B 34 VAL B 41 0
SHEET 2 AA3 8 VAL B 44 GLY B 52 -1 O LEU B 46 N ARG B 39
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 VAL B 126 N VAL B 60
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 ASP C 124 N LEU C 56
SHEET 6 AA5 8 ILE C 146 MET C 152 1 O VAL C 150 N LEU C 125
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 8 GLU D 35 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 ASP D 124 N LEU D 56
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 2.00
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.00
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.01
LINK OD1 ASP A 129 C1 AAVH A 401 1555 1555 1.40
LINK OD1 ASP A 129 C1 B8MD A 402 1555 1555 1.43
LINK OD1 ASP B 129 C6 ABVH B 401 1555 1555 1.50
LINK OD1 ASP B 129 C6 BDVH B 402 1555 1555 1.43
LINK OD1 ASP C 129 C6 ABVH C 401 1555 1555 1.51
LINK OD1 ASP C 129 C6 BDVH C 402 1555 1555 1.44
LINK OD1 ASP D 129 C6 ABVH D 401 1555 1555 1.50
LINK OD1 ASP D 129 C6 BDVH D 402 1555 1555 1.44
SITE 1 AC1 8 ASP A 129 VAL A 175 HIS A 177 PHE A 178
SITE 2 AC1 8 TYR A 239 MET A 272 HIS A 297 8MD A 402
SITE 1 AC2 6 ASP A 129 HIS A 177 TYR A 239 HIS A 297
SITE 2 AC2 6 AVH A 401 HOH A 510
SITE 1 AC3 15 PHE B 63 HIS B 128 ILE B 130 GLY B 131
SITE 2 AC3 15 ILE B 132 MET B 152 GLN B 153 ALA B 154
SITE 3 AC3 15 LEU B 174 HIS B 177 PHE B 178 TYR B 239
SITE 4 AC3 15 HIS B 297 DVH B 402 HOH B 637
SITE 1 AC4 15 PHE B 63 HIS B 128 ILE B 130 GLY B 131
SITE 2 AC4 15 ILE B 132 MET B 152 GLN B 153 ALA B 154
SITE 3 AC4 15 LEU B 174 HIS B 177 PHE B 178 TYR B 239
SITE 4 AC4 15 HIS B 297 DVH B 402 HOH B 637
SITE 1 AC5 16 PHE B 63 HIS B 128 ILE B 130 GLY B 131
SITE 2 AC5 16 ILE B 132 MET B 152 GLN B 153 ALA B 154
SITE 3 AC5 16 PRO B 155 VAL B 175 HIS B 177 TYR B 239
SITE 4 AC5 16 MET B 272 HIS B 297 BVH B 401 HOH B 637
SITE 1 AC6 16 PHE B 63 HIS B 128 ILE B 130 GLY B 131
SITE 2 AC6 16 ILE B 132 MET B 152 GLN B 153 ALA B 154
SITE 3 AC6 16 PRO B 155 VAL B 175 HIS B 177 TYR B 239
SITE 4 AC6 16 MET B 272 HIS B 297 BVH B 401 HOH B 637
SITE 1 AC7 17 PHE C 63 HIS C 128 ILE C 130 GLY C 131
SITE 2 AC7 17 ILE C 132 MET C 152 GLN C 153 ALA C 154
SITE 3 AC7 17 LEU C 174 VAL C 175 HIS C 177 PHE C 178
SITE 4 AC7 17 TYR C 239 HIS C 297 DVH C 402 HOH C 518
SITE 5 AC7 17 HOH C 650
SITE 1 AC8 17 PHE C 63 HIS C 128 ILE C 130 GLY C 131
SITE 2 AC8 17 ILE C 132 MET C 152 GLN C 153 ALA C 154
SITE 3 AC8 17 LEU C 174 VAL C 175 HIS C 177 PHE C 178
SITE 4 AC8 17 TYR C 239 HIS C 297 DVH C 402 HOH C 518
SITE 5 AC8 17 HOH C 650
SITE 1 AC9 16 PHE C 63 HIS C 128 ILE C 130 GLY C 131
SITE 2 AC9 16 ILE C 132 MET C 152 GLN C 153 ALA C 154
SITE 3 AC9 16 PRO C 155 VAL C 175 HIS C 177 TYR C 239
SITE 4 AC9 16 MET C 272 HIS C 297 BVH C 401 HOH C 650
SITE 1 AD1 16 PHE C 63 HIS C 128 ILE C 130 GLY C 131
SITE 2 AD1 16 ILE C 132 MET C 152 GLN C 153 ALA C 154
SITE 3 AD1 16 PRO C 155 VAL C 175 HIS C 177 TYR C 239
SITE 4 AD1 16 MET C 272 HIS C 297 BVH C 401 HOH C 650
SITE 1 AD2 15 PHE D 63 HIS D 128 ILE D 130 GLY D 131
SITE 2 AD2 15 ILE D 132 MET D 152 GLN D 153 ALA D 154
SITE 3 AD2 15 LEU D 174 HIS D 177 PHE D 178 TYR D 239
SITE 4 AD2 15 HIS D 297 DVH D 402 HOH D 644
SITE 1 AD3 15 PHE D 63 HIS D 128 ILE D 130 GLY D 131
SITE 2 AD3 15 ILE D 132 MET D 152 GLN D 153 ALA D 154
SITE 3 AD3 15 LEU D 174 HIS D 177 PHE D 178 TYR D 239
SITE 4 AD3 15 HIS D 297 DVH D 402 HOH D 644
SITE 1 AD4 16 PHE D 63 HIS D 128 ILE D 130 GLY D 131
SITE 2 AD4 16 ILE D 132 MET D 152 GLN D 153 ALA D 154
SITE 3 AD4 16 PRO D 155 VAL D 175 HIS D 177 TYR D 239
SITE 4 AD4 16 MET D 272 HIS D 297 BVH D 401 HOH D 644
SITE 1 AD5 16 PHE D 63 HIS D 128 ILE D 130 GLY D 131
SITE 2 AD5 16 ILE D 132 MET D 152 GLN D 153 ALA D 154
SITE 3 AD5 16 PRO D 155 VAL D 175 HIS D 177 TYR D 239
SITE 4 AD5 16 MET D 272 HIS D 297 BVH D 401 HOH D 644
CRYST1 168.351 83.436 89.377 90.00 100.45 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 0.005940 0.000000 0.001096 0.00000
SCALE2 0.000000 0.011985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011378 0.00000
TER 2403 GLY A 318
TER 4780 ARG B 317
TER 7194 ARG C 317
TER 9565 GLY D 318
MASTER 493 0 8 63 38 0 54 610570 4 84 96
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