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HEADER HYDROLASE 22-OCT-09 3KD2
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR (CIF);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA UCBPP-PA14;
SOURCE 3 ORGANISM_TAXID: 208963;
SOURCE 4 STRAIN: PA14;
SOURCE 5 GENE: PA14_26090;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDPM73
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.BAHL,D.R.MADDEN
REVDAT 1 26-JAN-10 3KD2 0
JRNL AUTH C.D.BAHL,C.MORISSEAU,J.M.BOMBERGER,B.A.STANTON,
JRNL AUTH 2 B.D.HAMMOCK,G.A.O'TOOLE,D.R.MADDEN
JRNL TITL CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF
JRNL TITL 2 REVEALS NOVEL ACTIVE-SITE FEATURES OF AN EPOXIDE
JRNL TITL 3 HYDROLASE VIRULENCE FACTOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.D.BAHL,D.P.MACEACHRAN,G.A.O'TOOLE,D.R.MADDEN
REMARK 1 TITL PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X-RAY
REMARK 1 TITL 2 DIFFRACTION ANALYSIS OF CIF, A VIRULENCE FACTOR
REMARK 1 TITL 3 SECRETED BY PSEUDOMONAS AERUGINOSA
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 112388
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5733
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 29.5570 - 5.5800 0.99 3612 230 0.1730 0.1660
REMARK 3 2 5.5800 - 4.4340 1.00 3589 219 0.1390 0.1210
REMARK 3 3 4.4340 - 3.8750 1.00 3618 167 0.1350 0.1740
REMARK 3 4 3.8750 - 3.5210 1.00 3567 195 0.1500 0.1590
REMARK 3 5 3.5210 - 3.2690 1.00 3537 234 0.1500 0.1700
REMARK 3 6 3.2690 - 3.0760 1.00 3529 240 0.1640 0.2040
REMARK 3 7 3.0760 - 2.9220 1.00 3755 0 0.1790 0.0000
REMARK 3 8 2.9220 - 2.7950 1.00 3469 274 0.1680 0.1780
REMARK 3 9 2.7950 - 2.6880 1.00 3411 332 0.1660 0.1750
REMARK 3 10 2.6880 - 2.5950 1.00 3779 0 0.1670 0.0000
REMARK 3 11 2.5950 - 2.5140 1.00 3376 383 0.1640 0.1730
REMARK 3 12 2.5140 - 2.4420 1.00 3730 0 0.1650 0.0000
REMARK 3 13 2.4420 - 2.3780 1.00 3325 417 0.1670 0.1920
REMARK 3 14 2.3780 - 2.3200 1.00 3729 0 0.1650 0.0000
REMARK 3 15 2.3200 - 2.2670 1.00 3224 502 0.1620 0.1790
REMARK 3 16 2.2670 - 2.2190 0.99 3720 0 0.1650 0.0000
REMARK 3 17 2.2190 - 2.1750 1.00 3760 0 0.1680 0.0000
REMARK 3 18 2.1750 - 2.1340 1.00 3212 526 0.1650 0.1810
REMARK 3 19 2.1340 - 2.0950 1.00 3755 0 0.1620 0.0000
REMARK 3 20 2.0950 - 2.0600 1.00 3292 423 0.1670 0.1860
REMARK 3 21 2.0600 - 2.0270 1.00 3555 166 0.1690 0.1950
REMARK 3 22 2.0270 - 1.9960 1.00 3708 0 0.1750 0.0000
REMARK 3 23 1.9960 - 1.9660 1.00 3564 191 0.1740 0.2020
REMARK 3 24 1.9660 - 1.9390 1.00 3287 471 0.1740 0.2040
REMARK 3 25 1.9390 - 1.9120 1.00 3689 0 0.1800 0.0000
REMARK 3 26 1.9120 - 1.8880 1.00 3765 0 0.1870 0.0000
REMARK 3 27 1.8880 - 1.8640 1.00 2954 762 0.1860 0.2220
REMARK 3 28 1.8640 - 1.8420 1.00 3727 0 0.1840 0.0000
REMARK 3 29 1.8420 - 1.8200 1.00 3723 0 0.1910 0.0000
REMARK 3 30 1.8200 - 1.8000 0.99 3694 1 0.2040 0.0000
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 : 0.39
REMARK 3 B_SOL : 37.69
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.004 9737
REMARK 3 ANGLE : 0.825 13229
REMARK 3 CHIRALITY : 0.060 1362
REMARK 3 PLANARITY : 0.004 1745
REMARK 3 DIHEDRAL : 16.933 3515
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1140 53.9999 27.0274
REMARK 3 T TENSOR
REMARK 3 T11: 0.0031 T22: 0.0318
REMARK 3 T33: 0.0614 T12: 0.0077
REMARK 3 T13: 0.0067 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: -0.0439 L22: 0.1654
REMARK 3 L33: 0.0100 L12: 0.0169
REMARK 3 L13: 0.0009 L23: -0.0085
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: -0.0152 S13: -0.0176
REMARK 3 S21: 0.0214 S22: -0.0206 S23: 0.0466
REMARK 3 S31: 0.0315 S32: -0.0237 S33: -0.0030
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5617 47.3891 15.5425
REMARK 3 T TENSOR
REMARK 3 T11: -0.0886 T22: -0.0339
REMARK 3 T33: 0.0708 T12: 0.1056
REMARK 3 T13: 0.0286 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: -0.0290 L22: 0.1720
REMARK 3 L33: -0.0010 L12: 0.0176
REMARK 3 L13: 0.0021 L23: -0.0021
REMARK 3 S TENSOR
REMARK 3 S11: 0.0199 S12: -0.0129 S13: -0.0285
REMARK 3 S21: 0.0069 S22: 0.0151 S23: -0.0861
REMARK 3 S31: 0.0165 S32: -0.0056 S33: 0.0013
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9559 9.3223 15.4493
REMARK 3 T TENSOR
REMARK 3 T11: -0.0935 T22: -0.0407
REMARK 3 T33: 0.1153 T12: 0.0979
REMARK 3 T13: -0.0278 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: -0.0361 L22: 0.1704
REMARK 3 L33: -0.0015 L12: 0.0121
REMARK 3 L13: -0.0075 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0167 S12: -0.0099 S13: 0.0515
REMARK 3 S21: -0.0209 S22: 0.0143 S23: 0.0618
REMARK 3 S31: -0.0098 S32: -0.0121 S33: 0.0010
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9791 2.8498 26.8201
REMARK 3 T TENSOR
REMARK 3 T11: 0.0049 T22: 0.0141
REMARK 3 T33: 0.0899 T12: 0.0147
REMARK 3 T13: 0.0028 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: -0.0485 L22: 0.1611
REMARK 3 L33: 0.0075 L12: 0.0190
REMARK 3 L13: -0.0047 L23: 0.0036
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: 0.0054 S13: 0.0183
REMARK 3 S21: 0.0190 S22: -0.0227 S23: -0.0601
REMARK 3 S31: -0.0253 S32: 0.0144 S33: 0.0030
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 3KD2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-09.
REMARK 100 THE RCSB ID CODE IS RCSB055839.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
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) : 0.9787
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : TOROIDAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112393
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.4900
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) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.160
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 0.125M CALCIUM
REMARK 280 CHLORIDE, 0.1M SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 84.09050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.94350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.09050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.94350
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: 2730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 2720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 318
REMARK 465 ARG A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 GLY B 318
REMARK 465 ARG B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 GLY C 318
REMARK 465 ARG C 319
REMARK 465 HIS C 320
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 GLY D 318
REMARK 465 ARG D 319
REMARK 465 HIS D 320
REMARK 465 HIS D 321
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: 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 -130.54 60.59
REMARK 500 ALA A 154 145.04 173.78
REMARK 500 CYS A 303 58.02 -142.89
REMARK 500 THR B 99 -62.87 -93.41
REMARK 500 ASP B 129 -134.43 58.03
REMARK 500 ALA B 154 142.83 174.27
REMARK 500 CYS B 303 57.53 -144.64
REMARK 500 THR C 99 -62.53 -91.60
REMARK 500 ASP C 129 -132.90 58.17
REMARK 500 ALA C 154 143.27 174.73
REMARK 500 PRO C 157 109.60 -59.33
REMARK 500 CYS C 303 56.42 -140.79
REMARK 500 ASP D 129 -132.34 60.19
REMARK 500 GLU D 153 60.12 61.18
REMARK 500 ALA D 154 148.29 173.53
REMARK 500 CYS D 303 57.18 -141.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KDA RELATED DB: PDB
DBREF 3KD2 A 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 3KD2 B 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 3KD2 C 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 3KD2 D 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
SEQADV 3KD2 HIS A 320 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS A 321 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS A 322 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS A 323 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS A 324 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS A 325 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS B 320 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS B 321 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS B 322 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS B 323 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS B 324 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS B 325 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS C 320 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS C 321 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS C 322 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS C 323 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS C 324 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS C 325 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS D 320 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS D 321 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS D 322 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS D 323 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS D 324 UNP Q02P97 EXPRESSION TAG
SEQADV 3KD2 HIS D 325 UNP Q02P97 EXPRESSION TAG
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 GLU 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 GLU 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 GLU 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 GLU 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
FORMUL 5 HOH *877(H2 O)
HELIX 1 1 THR A 66 HIS A 71 5 6
HELIX 2 2 GLN A 72 ALA A 78 1 7
HELIX 3 3 SER A 102 SER A 118 1 17
HELIX 4 4 ASP A 129 ASN A 134 1 6
HELIX 5 5 THR A 135 ASN A 142 1 8
HELIX 6 6 ASP A 158 PHE A 164 5 7
HELIX 7 7 TRP A 176 ALA A 183 1 8
HELIX 8 8 ARG A 186 ALA A 193 1 8
HELIX 9 9 LYS A 195 HIS A 207 1 13
HELIX 10 10 ASN A 210 PHE A 214 5 5
HELIX 11 11 SER A 215 ALA A 227 1 13
HELIX 12 12 LYS A 228 ALA A 241 1 14
HELIX 13 13 ALA A 241 ALA A 253 1 13
HELIX 14 14 THR A 274 LYS A 281 1 8
HELIX 15 15 TRP A 298 CYS A 303 1 6
HELIX 16 16 CYS A 303 SER A 316 1 14
HELIX 17 17 THR B 66 HIS B 71 5 6
HELIX 18 18 GLN B 72 ALA B 78 1 7
HELIX 19 19 SER B 102 SER B 118 1 17
HELIX 20 20 ASP B 129 ASN B 134 1 6
HELIX 21 21 THR B 135 ASN B 142 1 8
HELIX 22 22 ASP B 158 PHE B 164 5 7
HELIX 23 23 TRP B 176 ALA B 183 1 8
HELIX 24 24 ARG B 186 ALA B 193 1 8
HELIX 25 25 LYS B 195 HIS B 207 1 13
HELIX 26 26 ASN B 210 PHE B 214 5 5
HELIX 27 27 SER B 215 ALA B 227 1 13
HELIX 28 28 LYS B 228 ALA B 241 1 14
HELIX 29 29 ALA B 241 ALA B 253 1 13
HELIX 30 30 THR B 274 ALA B 284 1 11
HELIX 31 31 TRP B 298 CYS B 303 1 6
HELIX 32 32 CYS B 303 ARG B 317 1 15
HELIX 33 33 THR C 66 HIS C 71 5 6
HELIX 34 34 GLN C 72 ALA C 78 1 7
HELIX 35 35 SER C 102 SER C 118 1 17
HELIX 36 36 ASP C 129 ASN C 134 1 6
HELIX 37 37 THR C 135 ASN C 142 1 8
HELIX 38 38 ASP C 158 PHE C 164 5 7
HELIX 39 39 TRP C 176 ALA C 183 1 8
HELIX 40 40 ARG C 186 ALA C 193 1 8
HELIX 41 41 LYS C 195 HIS C 207 1 13
HELIX 42 42 SER C 215 ALA C 227 1 13
HELIX 43 43 LYS C 228 ALA C 241 1 14
HELIX 44 44 ALA C 241 ALA C 253 1 13
HELIX 45 45 THR C 274 ALA C 282 1 9
HELIX 46 46 TRP C 298 CYS C 303 1 6
HELIX 47 47 CYS C 303 ARG C 317 1 15
HELIX 48 48 THR D 66 HIS D 71 5 6
HELIX 49 49 LEU D 73 ALA D 78 1 6
HELIX 50 50 SER D 102 SER D 118 1 17
HELIX 51 51 ASP D 129 ASN D 134 1 6
HELIX 52 52 THR D 135 ASN D 142 1 8
HELIX 53 53 ASP D 158 PHE D 164 5 7
HELIX 54 54 TRP D 176 ALA D 183 1 8
HELIX 55 55 ARG D 186 ALA D 193 1 8
HELIX 56 56 LYS D 195 HIS D 207 1 13
HELIX 57 57 ASN D 210 PHE D 214 5 5
HELIX 58 58 SER D 215 ALA D 227 1 13
HELIX 59 59 LYS D 228 ALA D 241 1 14
HELIX 60 60 ALA D 241 ALA D 253 1 13
HELIX 61 61 THR D 274 LYS D 281 1 8
HELIX 62 62 TRP D 298 CYS D 303 1 6
HELIX 63 63 CYS D 303 ARG D 317 1 15
SHEET 1 A 8 GLU A 35 VAL A 41 0
SHEET 2 A 8 VAL A 44 GLY A 52 -1 O VAL A 44 N VAL A 41
SHEET 3 A 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 A 8 LEU A 56 VAL A 60 1 N LEU A 59 O ILE A 84
SHEET 5 A 8 PHE A 123 HIS A 128 1 O VAL A 126 N VAL A 60
SHEET 6 A 8 ILE A 146 MET A 152 1 O VAL A 150 N LEU A 125
SHEET 7 A 8 THR A 261 GLY A 266 1 O MET A 262 N TYR A 151
SHEET 8 A 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 B 2 PHE A 167 THR A 168 0
SHEET 2 B 2 GLY A 171 GLU A 172 -1 O GLY A 171 N THR A 168
SHEET 1 C 8 GLU B 35 VAL B 41 0
SHEET 2 C 8 VAL B 44 GLY B 52 -1 O LEU B 46 N ARG B 39
SHEET 3 C 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 C 8 LEU B 56 VAL B 60 1 N LEU B 59 O ILE B 84
SHEET 5 C 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 C 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 C 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 C 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 D 2 PHE B 167 THR B 168 0
SHEET 2 D 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SHEET 1 E 8 PHE C 34 VAL C 41 0
SHEET 2 E 8 VAL C 44 GLY C 52 -1 O VAL C 44 N VAL C 41
SHEET 3 E 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 E 8 LEU C 56 VAL C 60 1 N LEU C 59 O ILE C 84
SHEET 5 E 8 PHE C 123 HIS C 128 1 O ASP C 124 N LEU C 56
SHEET 6 E 8 ILE C 146 MET C 152 1 O VAL C 150 N LEU C 125
SHEET 7 E 8 THR C 261 GLY C 266 1 O MET C 262 N LEU C 149
SHEET 8 E 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 F 2 PHE C 167 THR C 168 0
SHEET 2 F 2 GLY C 171 GLU C 172 -1 O GLY C 171 N THR C 168
SHEET 1 G 8 GLU D 35 VAL D 41 0
SHEET 2 G 8 VAL D 44 GLY D 52 -1 O VAL D 44 N VAL D 41
SHEET 3 G 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 G 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 G 8 PHE D 123 HIS D 128 1 O ASP D 124 N LEU D 56
SHEET 6 G 8 ILE D 146 MET D 152 1 O VAL D 150 N ALA D 127
SHEET 7 G 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 G 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 H 2 PHE D 167 THR D 168 0
SHEET 2 H 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 2.02
SSBOND 2 CYS B 295 CYS B 303 1555 1555 1.98
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.02
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.02
CRYST1 168.181 83.887 88.977 90.00 100.50 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005946 0.000000 0.001102 0.00000
SCALE2 0.000000 0.011921 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011430 0.00000
END |