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HEADER HYDROLASE 06-FEB-12 4DLN
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE D129S
TITLE 2 MUTATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CIF (UNP RESIDUES 25-319);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
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;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMQ70
KEYWDS ALPHA BETA HYDROLASE, EPOXIDE HYDROLASE, SECRETED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.BAHL,J.F.AMACHER,D.R.MADDEN
REVDAT 1 07-AUG-13 4DLN 0
JRNL AUTH C.D.BAHL,D.R.MADDEN
JRNL TITL CIF EPOXIDE HYDROLASE ENZYME ACTIVITY IS REQUIRED FOR CFTR
JRNL TITL 2 INHIBITORY ACTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 173079
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 8686
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 46.1078 - 4.8145 0.99 5543 440 0.1619 0.1558
REMARK 3 2 4.8145 - 3.8220 0.99 5892 0 0.1310 10000000.0000
REMARK 3 3 3.8220 - 3.3390 0.99 5462 441 0.1408 0.1430
REMARK 3 4 3.3390 - 3.0338 0.99 5424 440 0.1549 0.1604
REMARK 3 5 3.0338 - 2.8164 0.99 5884 0 0.1641 10000000.0000
REMARK 3 6 2.8164 - 2.6504 0.99 5414 438 0.1516 0.1667
REMARK 3 7 2.6504 - 2.5176 0.99 5386 438 0.1569 0.1596
REMARK 3 8 2.5176 - 2.4080 0.99 5764 0 0.1574 10000000.0000
REMARK 3 9 2.4080 - 2.3153 0.99 5413 436 0.1577 0.1896
REMARK 3 10 2.3153 - 2.2355 0.99 5328 435 0.1527 0.1806
REMARK 3 11 2.2355 - 2.1656 0.99 5823 0 0.1518 10000000.0000
REMARK 3 12 2.1656 - 2.1037 0.98 5356 431 0.1478 0.1671
REMARK 3 13 2.1037 - 2.0483 0.98 5296 435 0.1478 0.1687
REMARK 3 14 2.0483 - 1.9983 0.98 5797 0 0.1493 10000000.0000
REMARK 3 15 1.9983 - 1.9529 0.98 5320 433 0.1512 0.1841
REMARK 3 16 1.9529 - 1.9113 0.98 5316 431 0.1490 0.1685
REMARK 3 17 1.9113 - 1.8731 0.98 5786 0 0.1518 10000000.0000
REMARK 3 18 1.8731 - 1.8377 0.97 5287 432 0.1539 0.1757
REMARK 3 19 1.8377 - 1.8049 0.97 5249 431 0.1529 0.1801
REMARK 3 20 1.8049 - 1.7743 0.98 5713 0 0.1476 10000000.0000
REMARK 3 21 1.7743 - 1.7457 0.97 5278 431 0.1562 0.1831
REMARK 3 22 1.7457 - 1.7188 0.98 5310 434 0.1576 0.1981
REMARK 3 23 1.7188 - 1.6936 0.97 5766 0 0.1568 10000000.0000
REMARK 3 24 1.6936 - 1.6697 0.97 5224 430 0.1527 0.1848
REMARK 3 25 1.6697 - 1.6471 0.97 5210 433 0.1554 0.1845
REMARK 3 26 1.6471 - 1.6257 0.97 5721 0 0.1590 10000000.0000
REMARK 3 27 1.6257 - 1.6054 0.97 5294 434 0.1631 0.1953
REMARK 3 28 1.6054 - 1.5861 0.97 5198 435 0.1641 0.1925
REMARK 3 29 1.5861 - 1.5676 0.97 5661 0 0.1666 10000000.0000
REMARK 3 30 1.5676 - 1.5500 0.97 5278 428 0.1715 0.2035
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 : 0.37
REMARK 3 B_SOL : 39.77
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.480
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) : -0.71390
REMARK 3 B22 (A**2) : -0.93050
REMARK 3 B33 (A**2) : 1.64440
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.35040
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 : 0.006 9860
REMARK 3 ANGLE : 1.083 13394
REMARK 3 CHIRALITY : 0.078 1378
REMARK 3 PLANARITY : 0.005 1763
REMARK 3 DIHEDRAL : 12.935 3600
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6846 41.0545 27.1069
REMARK 3 T TENSOR
REMARK 3 T11: 0.0268 T22: 0.0236
REMARK 3 T33: 0.0367 T12: 0.0076
REMARK 3 T13: 0.0044 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.2843 L22: 0.5652
REMARK 3 L33: 0.4103 L12: 0.0643
REMARK 3 L13: 0.0402 L23: -0.0109
REMARK 3 S TENSOR
REMARK 3 S11: 0.0128 S12: -0.0129 S13: 0.0476
REMARK 3 S21: 0.0267 S22: -0.0270 S23: -0.0474
REMARK 3 S31: -0.0494 S32: 0.0103 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain B and resid 25:322)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8079 1.1684 15.6506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0315 T22: 0.0335
REMARK 3 T33: 0.0192 T12: 0.0200
REMARK 3 T13: 0.0068 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.5684 L22: 0.6036
REMARK 3 L33: 0.3225 L12: -0.1584
REMARK 3 L13: -0.0109 L23: 0.1408
REMARK 3 S TENSOR
REMARK 3 S11: 0.0189 S12: 0.0174 S13: -0.0242
REMARK 3 S21: -0.0197 S22: 0.0072 S23: -0.0873
REMARK 3 S31: 0.0228 S32: 0.0074 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain C and resid 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9648 7.9968 27.2913
REMARK 3 T TENSOR
REMARK 3 T11: 0.0267 T22: 0.0424
REMARK 3 T33: 0.0163 T12: 0.0028
REMARK 3 T13: 0.0052 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.3412 L22: 0.3789
REMARK 3 L33: 0.4404 L12: 0.0400
REMARK 3 L13: 0.0874 L23: 0.0958
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: -0.0552 S13: -0.0346
REMARK 3 S21: 0.0310 S22: -0.0274 S23: 0.0221
REMARK 3 S31: 0.0547 S32: -0.0487 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain D and resid 25:320)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9669 47.6447 15.6348
REMARK 3 T TENSOR
REMARK 3 T11: 0.0338 T22: 0.0282
REMARK 3 T33: 0.0515 T12: 0.0172
REMARK 3 T13: -0.0196 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.7111 L22: 0.6212
REMARK 3 L33: 0.2502 L12: -0.2658
REMARK 3 L13: -0.0423 L23: -0.0825
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.0072 S13: 0.1072
REMARK 3 S21: -0.0321 S22: 0.0094 S23: 0.0125
REMARK 3 S31: -0.0355 S32: -0.0013 S33: 0.0000
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 4DLN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-09
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) : 0.9782
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL CUT MONOCHROMATOR
REMARK 200 OPTICS : TOROIDAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS-PACKAGE
REMARK 200 DATA SCALING SOFTWARE : XDS-PACKAGE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 173094
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 46.087
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28400
REMARK 200 FOR SHELL : 4.900
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: CHAIN A OF PDB ENTRY 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 8000, 0.125M CALCIUM CHLORIDE,
REMARK 280 0.1M SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 84.08700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.97650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.08700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.97650
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: 2740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20870 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: 2730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 676 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 678 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 319 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG B 319 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG C 319 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG D 319 CB CG CD NE CZ NH1 NH2
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 SER A 129 -136.79 59.09
REMARK 500 ALA A 154 147.67 177.26
REMARK 500 CYS A 303 55.31 -141.30
REMARK 500 THR B 99 -66.23 -90.84
REMARK 500 SER B 129 -136.59 57.91
REMARK 500 ALA B 154 146.87 178.21
REMARK 500 CYS B 303 53.73 -142.29
REMARK 500 SER C 129 -137.28 60.52
REMARK 500 ALA C 154 147.79 176.14
REMARK 500 CYS C 303 56.18 -142.36
REMARK 500 SER D 129 -136.99 58.99
REMARK 500 ALA D 154 146.48 178.42
REMARK 500 CYS D 303 54.44 -140.36
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4DLN A 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DLN B 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DLN C 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DLN D 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
SEQADV 4DLN SER A 129 UNP Q02P97 ASP 129 ENGINEERED MUTATION
SEQADV 4DLN HIS A 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS A 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS A 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS A 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS A 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS A 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN SER B 129 UNP Q02P97 ASP 129 ENGINEERED MUTATION
SEQADV 4DLN HIS B 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS B 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS B 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS B 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS B 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS B 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN SER C 129 UNP Q02P97 ASP 129 ENGINEERED MUTATION
SEQADV 4DLN HIS C 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS C 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS C 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS C 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS C 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS C 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN SER D 129 UNP Q02P97 ASP 129 ENGINEERED MUTATION
SEQADV 4DLN HIS D 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS D 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS D 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS D 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN HIS D 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DLN 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 SER 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 SER 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 SER 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 SER 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 *1224(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 SER 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 ALA A 282 1 9
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 SER 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 282 1 9
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 LEU C 73 ALA C 78 1 6
HELIX 35 35 SER C 102 SER C 118 1 17
HELIX 36 36 SER 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 ASN C 210 PHE C 214 5 5
HELIX 43 43 SER C 215 ALA C 227 1 13
HELIX 44 44 LYS C 228 ALA C 241 1 14
HELIX 45 45 ALA C 241 ALA C 253 1 13
HELIX 46 46 THR C 274 ALA C 282 1 9
HELIX 47 47 TRP C 298 CYS C 303 1 6
HELIX 48 48 CYS C 303 SER C 316 1 14
HELIX 49 49 THR D 66 HIS D 71 5 6
HELIX 50 50 GLN D 72 ALA D 78 1 7
HELIX 51 51 SER D 102 SER D 118 1 17
HELIX 52 52 SER D 129 ASN D 134 1 6
HELIX 53 53 THR D 135 ASN D 142 1 8
HELIX 54 54 ASP D 158 PHE D 164 5 7
HELIX 55 55 TRP D 176 ALA D 183 1 8
HELIX 56 56 ARG D 186 ALA D 193 1 8
HELIX 57 57 LYS D 195 HIS D 207 1 13
HELIX 58 58 ASN D 210 PHE D 214 5 5
HELIX 59 59 SER D 215 LYS D 228 1 14
HELIX 60 60 LYS D 228 ALA D 241 1 14
HELIX 61 61 ALA D 241 ALA D 253 1 13
HELIX 62 62 THR D 274 ALA D 282 1 9
HELIX 63 63 TRP D 298 CYS D 303 1 6
HELIX 64 64 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 VAL A 57 O THR A 82
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 GLU C 35 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 VAL C 57 O THR C 82
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 TYR C 151
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 PHE D 34 VAL D 41 0
SHEET 2 G 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
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 VAL D 126 N VAL D 60
SHEET 6 G 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
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 2.01
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 2.00
CRYST1 168.174 83.953 89.169 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 0.005946 0.000000 0.001090 0.00000
SCALE2 0.000000 0.011911 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011402 0.00000
TER 2408 HIS A 321
TER 4795 HIS B 322
TER 7193 HIS C 321
TER 9555 HIS D 320
MASTER 368 0 0 64 40 0 0 610708 4 8 96
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