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HEADER HYDROLASE 08-FEB-12 4DNF
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE E153Q
TITLE 2 MUTATION ADDUCTED WITH THE EPIBROMOHYDRIN HYDROLYSIS INTERMEDIATE
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, COVALENTLY ADDUCTED WITH THE
KEYWDS 2 EPIBROMOHYDRIN HYDROLYSIS INTERMEDIATE, SECRETED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.BAHL,D.R.MADDEN
REVDAT 1 07-AUG-13 4DNF 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. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
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) : 38.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 112809
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 5797
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 38.5497 - 5.5875 0.98 3589 237 0.2069 0.2114
REMARK 3 2 5.5875 - 4.4371 0.99 3589 220 0.1649 0.1762
REMARK 3 3 4.4371 - 3.8768 0.99 3639 143 0.1690 0.1741
REMARK 3 4 3.8768 - 3.5226 0.99 3579 185 0.1756 0.1978
REMARK 3 5 3.5226 - 3.2703 0.99 3581 222 0.1831 0.2028
REMARK 3 6 3.2703 - 3.0775 0.99 3507 248 0.1984 0.2441
REMARK 3 7 3.0775 - 2.9235 0.99 3444 312 0.2015 0.2281
REMARK 3 8 2.9235 - 2.7963 0.99 3732 0 0.1924 10000000.0000
REMARK 3 9 2.7963 - 2.6886 0.99 3442 335 0.1877 0.2330
REMARK 3 10 2.6886 - 2.5959 0.99 3772 0 0.1876 10000000.0000
REMARK 3 11 2.5959 - 2.5147 0.99 3366 395 0.1826 0.2255
REMARK 3 12 2.5147 - 2.4429 0.99 3759 0 0.1847 10000000.0000
REMARK 3 13 2.4429 - 2.3786 0.99 3287 446 0.1849 0.2327
REMARK 3 14 2.3786 - 2.3205 0.99 3772 0 0.1858 10000000.0000
REMARK 3 15 2.3205 - 2.2678 0.99 3263 468 0.1783 0.2062
REMARK 3 16 2.2678 - 2.2195 0.99 3756 0 0.1673 10000000.0000
REMARK 3 17 2.2195 - 2.1751 1.00 3310 460 0.1791 0.2366
REMARK 3 18 2.1751 - 2.1341 1.00 3612 116 0.1808 0.2494
REMARK 3 19 2.1341 - 2.0960 1.00 3756 0 0.1859 10000000.0000
REMARK 3 20 2.0960 - 2.0605 1.00 3155 609 0.1749 0.2195
REMARK 3 21 2.0605 - 2.0272 0.99 3751 0 0.1749 10000000.0000
REMARK 3 22 2.0272 - 1.9960 1.00 3708 0 0.1771 10000000.0000
REMARK 3 23 1.9960 - 1.9667 1.00 3128 658 0.1863 0.2390
REMARK 3 24 1.9667 - 1.9390 1.00 3761 0 0.1856 10000000.0000
REMARK 3 25 1.9390 - 1.9128 1.00 3720 0 0.1866 10000000.0000
REMARK 3 26 1.9128 - 1.8879 1.00 3715 0 0.1956 10000000.0000
REMARK 3 27 1.8879 - 1.8643 1.00 3037 742 0.1911 0.2561
REMARK 3 28 1.8643 - 1.8419 1.00 3756 0 0.1932 10000000.0000
REMARK 3 29 1.8419 - 1.8205 1.00 3785 0 0.1999 10000000.0000
REMARK 3 30 1.8205 - 1.8000 1.00 3741 1 0.2071 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 : 0.40
REMARK 3 B_SOL : 39.97
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.600
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) : -2.81190
REMARK 3 B22 (A**2) : -2.89790
REMARK 3 B33 (A**2) : 3.62990
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.14930
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 9833
REMARK 3 ANGLE : 1.012 13349
REMARK 3 CHIRALITY : 0.074 1374
REMARK 3 PLANARITY : 0.005 1754
REMARK 3 DIHEDRAL : 16.606 3545
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 25:320)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9675 11.9494 27.2513
REMARK 3 T TENSOR
REMARK 3 T11: 0.0036 T22: 0.0060
REMARK 3 T33: -0.0872 T12: 0.0035
REMARK 3 T13: -0.0256 T23: 0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 0.3023 L22: 0.1899
REMARK 3 L33: 0.2584 L12: 0.0239
REMARK 3 L13: 0.1686 L23: -0.0434
REMARK 3 S TENSOR
REMARK 3 S11: -0.0176 S12: -0.0217 S13: -0.1462
REMARK 3 S21: 0.0491 S22: -0.0730 S23: 0.1627
REMARK 3 S31: 0.0854 S32: -0.0391 S33: -0.0533
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain B and resid 25:320)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.8609 51.5598 15.7372
REMARK 3 T TENSOR
REMARK 3 T11: 0.0229 T22: 0.0167
REMARK 3 T33: 0.0345 T12: 0.0215
REMARK 3 T13: -0.0168 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.3965 L22: 0.3956
REMARK 3 L33: 0.1659 L12: -0.2745
REMARK 3 L13: 0.0162 L23: -0.1684
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: 0.0234 S13: 0.0707
REMARK 3 S21: -0.0477 S22: 0.0117 S23: 0.0584
REMARK 3 S31: -0.0395 S32: -0.0133 S33: 0.0272
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain C and resid 25:320)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8775 44.6913 27.2357
REMARK 3 T TENSOR
REMARK 3 T11: 0.0060 T22: 0.0025
REMARK 3 T33: -0.0142 T12: 0.0014
REMARK 3 T13: 0.0050 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 0.3429 L22: 0.2740
REMARK 3 L33: 0.2941 L12: 0.0743
REMARK 3 L13: -0.0833 L23: 0.0480
REMARK 3 S TENSOR
REMARK 3 S11: 0.0099 S12: -0.0164 S13: 0.1381
REMARK 3 S21: 0.0053 S22: -0.0413 S23: -0.1040
REMARK 3 S31: -0.0497 S32: 0.0502 S33: -0.0377
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain D and resid 25:320)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7976 5.0678 15.7568
REMARK 3 T TENSOR
REMARK 3 T11: 0.0273 T22: 0.0294
REMARK 3 T33: -0.0033 T12: 0.0184
REMARK 3 T13: 0.0115 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.3125 L22: 0.3494
REMARK 3 L33: 0.1182 L12: -0.2177
REMARK 3 L13: -0.0051 L23: 0.1359
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0235 S13: -0.0135
REMARK 3 S21: -0.0249 S22: 0.0034 S23: -0.0703
REMARK 3 S31: 0.0151 S32: 0.0052 S33: -0.0094
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 4DNF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070546.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-08
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) : 0.8984
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-PACKAGE
REMARK 200 DATA SCALING SOFTWARE : XDS-PACKAGE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112816
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 FOR THE DATA SET : 11.8700
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) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27800
REMARK 200 FOR SHELL : 4.770
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 (%): 45.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 0.125M CALCIUM CHLORIDE,
REMARK 280 0.1M SODIUM ACETATE, 0.01M EPIBROMOHYDRIN, VAPOR DIFFUSION,
REMARK 280 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 84.07350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.97950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.07350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.97950
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: 2770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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: 20870 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 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 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 HIS D 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 ASP A 129 -133.56 61.92
REMARK 500 ASN A 142 51.48 -140.50
REMARK 500 ALA A 154 147.81 -179.80
REMARK 500 CYS A 303 54.21 -144.58
REMARK 500 THR B 99 -67.01 -96.49
REMARK 500 ASP B 129 -132.14 61.09
REMARK 500 ALA B 154 147.54 179.98
REMARK 500 CYS B 303 55.92 -141.84
REMARK 500 THR C 99 -70.26 -84.77
REMARK 500 ASP C 129 -132.39 62.11
REMARK 500 ALA C 154 146.79 179.44
REMARK 500 ASP C 184 176.75 -59.14
REMARK 500 CYS C 303 57.32 -141.83
REMARK 500 THR D 99 -68.52 -95.14
REMARK 500 ASP D 129 -129.19 58.78
REMARK 500 ALA D 154 141.50 172.96
REMARK 500 CYS D 303 56.37 -142.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EBH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EBH B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EBH C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EBH D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 SAME PROTEIN, BUT WITH THE WILD TYPE SEQUENCE
REMARK 900 RELATED ID: 3KDA RELATED DB: PDB
REMARK 900 RELATED ID: 3PI6 RELATED DB: PDB
REMARK 900 RELATED ID: 4DLN RELATED DB: PDB
REMARK 900 RELATED ID: 4DM7 RELATED DB: PDB
REMARK 900 RELATED ID: 4DMC RELATED DB: PDB
REMARK 900 RELATED ID: 4DMF RELATED DB: PDB
REMARK 900 RELATED ID: 4DMH RELATED DB: PDB
REMARK 900 RELATED ID: 4DMK RELATED DB: PDB
REMARK 900 RELATED ID: 4DNO RELATED DB: PDB
DBREF 4DNF A 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DNF B 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DNF C 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DNF D 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
SEQADV 4DNF GLN A 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DNF HIS A 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS A 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS A 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS A 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS A 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS A 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF GLN B 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DNF HIS B 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS B 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS B 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS B 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS B 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS B 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF GLN C 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DNF HIS C 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS C 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS C 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS C 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS C 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS C 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF GLN D 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DNF HIS D 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS D 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS D 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS D 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF HIS D 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNF 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 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 EBH A 401 5
HET EBH B 401 5
HET EBH C 401 5
HET EBH D 401 5
HETNAM EBH (2S)-1-BROMOPROPAN-2-OL
FORMUL 5 EBH 4(C3 H7 BR O)
FORMUL 9 HOH *829(H2 O)
HELIX 1 1 THR A 66 HIS A 71 5 6
HELIX 2 2 LEU A 73 ALA A 78 1 6
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 VAL A 175 ALA A 183 1 9
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 284 1 11
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 VAL B 175 ALA B 183 1 9
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 LYS B 228 1 14
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 SER B 316 1 14
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 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 VAL C 175 ALA C 183 1 9
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 LYS C 281 1 8
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 ASP 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 VAL D 175 ALA D 183 1 9
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 ALA D 227 1 13
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 ASP A 124 N MET A 58
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 LEU A 149
SHEET 8 A 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 B 8 PHE B 34 VAL B 41 0
SHEET 2 B 8 VAL B 44 GLY B 52 -1 O LYS B 50 N GLU B 35
SHEET 3 B 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 B 8 LEU B 56 VAL B 60 1 N VAL B 57 O ILE B 84
SHEET 5 B 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 B 8 ILE B 146 MET B 152 1 O VAL B 150 N ALA B 127
SHEET 7 B 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 B 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 C 2 PHE B 167 THR B 168 0
SHEET 2 C 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SHEET 1 D 8 GLU C 35 VAL C 41 0
SHEET 2 D 8 VAL C 44 GLY C 52 -1 O VAL C 44 N VAL C 41
SHEET 3 D 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 D 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 D 8 PHE C 123 HIS C 128 1 O ASP C 124 N MET C 58
SHEET 6 D 8 ILE C 146 MET C 152 1 O VAL C 150 N LEU C 125
SHEET 7 D 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 D 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 E 8 PHE D 34 VAL D 41 0
SHEET 2 E 8 VAL D 44 GLY D 52 -1 O VAL D 44 N VAL D 41
SHEET 3 E 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 E 8 LEU D 56 VAL D 60 1 N VAL D 57 O ILE D 84
SHEET 5 E 8 PHE D 123 HIS D 128 1 O VAL D 126 N VAL D 60
SHEET 6 E 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 E 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 E 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 F 2 PHE D 167 THR D 168 0
SHEET 2 F 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 2.00
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.01
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.01
LINK OD2 ASP A 129 C02 EBH A 401 1555 1555 1.38
LINK OD2 ASP B 129 C02 EBH B 401 1555 1555 1.38
LINK OD2 ASP C 129 C02 EBH C 401 1555 1555 1.38
LINK OD2 ASP D 129 C02 EBH D 401 1555 1555 1.38
SITE 1 AC1 5 ASP A 129 HIS A 177 PHE A 178 TYR A 239
SITE 2 AC1 5 HIS A 297
SITE 1 AC2 6 ASP B 129 ALA B 154 HIS B 177 PHE B 178
SITE 2 AC2 6 TYR B 239 HIS B 297
SITE 1 AC3 5 ASP C 129 HIS C 177 PHE C 178 TYR C 239
SITE 2 AC3 5 HIS C 297
SITE 1 AC4 5 ASP D 129 HIS D 177 PHE D 178 TYR D 239
SITE 2 AC4 5 HIS D 297
CRYST1 168.147 83.959 89.536 90.00 100.31 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 0.005947 0.000000 0.001081 0.00000
SCALE2 0.000000 0.011911 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011352 0.00000
TER 2396 HIS A 320
TER 4763 HIS B 320
TER 7141 HIS C 320
TER 9513 HIS D 320
MASTER 397 0 4 64 36 0 8 610301 4 32 96
END |