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HEADER HYDROLASE 08-FEB-12 4DNO
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE E153Q
TITLE 2 MUTATION ADDUCTED WITH THE 1,2-EPOXYHEXANE 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 1,2-EPOXYHEXANE HYDROLYSIS INTERMEDIATE, SECRETED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.BAHL,Y.R.PATANKAR,D.R.MADDEN
REVDAT 1 07-AUG-13 4DNO 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. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 88434
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4411
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 46.0207 - 6.0547 0.99 2819 221 0.2335 0.2648
REMARK 3 2 6.0547 - 4.8074 1.00 3001 0 0.1631 10000000.0000
REMARK 3 3 4.8074 - 4.2002 1.00 2746 220 0.1375 0.1743
REMARK 3 4 4.2002 - 3.8164 1.00 2730 221 0.1506 0.1893
REMARK 3 5 3.8164 - 3.5429 1.00 3001 0 0.1666 10000000.0000
REMARK 3 6 3.5429 - 3.3341 1.00 2727 221 0.1730 0.2145
REMARK 3 7 3.3341 - 3.1672 1.00 2744 221 0.1750 0.2087
REMARK 3 8 3.1672 - 3.0293 1.00 2920 0 0.1779 10000000.0000
REMARK 3 9 3.0293 - 2.9127 1.00 2757 221 0.1803 0.2303
REMARK 3 10 2.9127 - 2.8122 1.00 2728 221 0.1745 0.2425
REMARK 3 11 2.8122 - 2.7243 1.00 2946 0 0.1708 10000000.0000
REMARK 3 12 2.7243 - 2.6465 1.00 2742 221 0.1682 0.2215
REMARK 3 13 2.6465 - 2.5768 1.00 2717 221 0.1735 0.2624
REMARK 3 14 2.5768 - 2.5139 1.00 2961 0 0.1716 10000000.0000
REMARK 3 15 2.5139 - 2.4568 1.00 2710 221 0.1730 0.2225
REMARK 3 16 2.4568 - 2.4045 1.00 2686 221 0.1707 0.2344
REMARK 3 17 2.4045 - 2.3564 1.00 2972 0 0.1741 10000000.0000
REMARK 3 18 2.3564 - 2.3119 1.00 2733 221 0.1605 0.2218
REMARK 3 19 2.3119 - 2.2707 1.00 2720 221 0.1704 0.2583
REMARK 3 20 2.2707 - 2.2322 1.00 2898 0 0.1716 10000000.0000
REMARK 3 21 2.2322 - 2.1962 1.00 2744 221 0.1608 0.2081
REMARK 3 22 2.1962 - 2.1624 1.00 2754 220 0.1626 0.2146
REMARK 3 23 2.1624 - 2.1306 1.00 2886 0 0.1672 10000000.0000
REMARK 3 24 2.1306 - 2.1006 1.00 2748 221 0.1734 0.2365
REMARK 3 25 2.1006 - 2.0722 1.00 2706 219 0.1837 0.2441
REMARK 3 26 2.0722 - 2.0453 1.00 2907 0 0.1935 10000000.0000
REMARK 3 27 2.0453 - 2.0197 1.00 2763 220 0.1893 0.2762
REMARK 3 28 2.0197 - 1.9954 1.00 2678 221 0.2015 0.2664
REMARK 3 29 1.9954 - 1.9722 0.99 2919 0 0.2099 10000000.0000
REMARK 3 30 1.9722 - 1.9500 0.98 2660 217 0.2171 0.3001
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 : 47.37
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.240
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) : -5.92250
REMARK 3 B22 (A**2) : -2.92370
REMARK 3 B33 (A**2) : 8.84620
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.20550
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 9819
REMARK 3 ANGLE : 1.006 13314
REMARK 3 CHIRALITY : 0.073 1364
REMARK 3 PLANARITY : 0.005 1752
REMARK 3 DIHEDRAL : 14.148 3568
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): 22.0382 12.4459 -27.3134
REMARK 3 T TENSOR
REMARK 3 T11: 0.0562 T22: 0.0577
REMARK 3 T33: 0.0563 T12: -0.0036
REMARK 3 T13: 0.0004 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.2441 L22: 0.2767
REMARK 3 L33: 0.2581 L12: 0.0265
REMARK 3 L13: 0.0491 L23: -0.0047
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: 0.0132 S13: -0.0502
REMARK 3 S21: 0.0048 S22: -0.0084 S23: -0.0526
REMARK 3 S31: 0.0519 S32: 0.0056 S33: 0.0048
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain B and resid 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8479 51.4147 -15.6035
REMARK 3 T TENSOR
REMARK 3 T11: 0.0605 T22: 0.0564
REMARK 3 T33: 0.1136 T12: -0.0257
REMARK 3 T13: -0.0145 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.0829 L22: 0.0589
REMARK 3 L33: 0.0479 L12: 0.0239
REMARK 3 L13: 0.0139 L23: 0.0138
REMARK 3 S TENSOR
REMARK 3 S11: -0.0320 S12: -0.0133 S13: 0.0848
REMARK 3 S21: 0.0205 S22: 0.0350 S23: -0.0546
REMARK 3 S31: -0.0380 S32: 0.0009 S33: 0.0110
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain C and resid 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7191 44.5884 -27.2337
REMARK 3 T TENSOR
REMARK 3 T11: 0.0657 T22: 0.0666
REMARK 3 T33: 0.1018 T12: -0.0017
REMARK 3 T13: 0.0110 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.1594 L22: 0.1460
REMARK 3 L33: 0.2432 L12: 0.0370
REMARK 3 L13: -0.0402 L23: 0.0284
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: -0.0118 S13: 0.1009
REMARK 3 S21: 0.0005 S22: -0.0262 S23: 0.0522
REMARK 3 S31: -0.0558 S32: -0.0162 S33: 0.0012
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain D and resid 25:318)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5599 5.5379 -15.7611
REMARK 3 T TENSOR
REMARK 3 T11: 0.0705 T22: 0.0689
REMARK 3 T33: 0.0625 T12: -0.0252
REMARK 3 T13: 0.0101 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.1937 L22: 0.2458
REMARK 3 L33: 0.1609 L12: 0.0754
REMARK 3 L13: -0.0278 L23: -0.0785
REMARK 3 S TENSOR
REMARK 3 S11: 0.0108 S12: -0.0257 S13: -0.0022
REMARK 3 S21: 0.0225 S22: 0.0098 S23: 0.0725
REMARK 3 S31: 0.0279 S32: 0.0232 S33: -0.0037
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 4DNO 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 RCSB070555.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-11
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) : 1.2006
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 : 88446
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 46.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09900
REMARK 200 FOR THE DATA SET : 11.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.39400
REMARK 200 FOR SHELL : 3.530
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 (%): 45.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 0.125M CALCIUM CHLORIDE,
REMARK 280 0.1M SODIUM ACETATE, 0.01M 1,2-EPOXYHEXANE, 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 84.04000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.83150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.04000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.83150
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: 3520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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: 3500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 D 637 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 617 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 734 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 700 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 704 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 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 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: 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 -128.85 60.06
REMARK 500 ALA A 154 147.83 175.84
REMARK 500 CYS A 303 54.24 -142.77
REMARK 500 THR B 99 -63.61 -91.20
REMARK 500 ASP B 129 -131.00 60.19
REMARK 500 ALA B 154 146.14 171.99
REMARK 500 CYS B 303 54.64 -143.58
REMARK 500 THR C 99 -70.72 -80.38
REMARK 500 ASP C 129 -127.25 58.48
REMARK 500 ALA C 154 148.64 176.18
REMARK 500 THR D 99 -61.41 -92.05
REMARK 500 ASP D 129 -128.03 62.16
REMARK 500 ALA D 154 145.62 171.51
REMARK 500 CYS D 303 50.04 -141.56
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 HE2 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HE2 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HE2 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HE2 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: 4DNF RELATED DB: PDB
DBREF 4DNO A 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DNO B 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DNO C 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DNO D 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
SEQADV 4DNO GLN A 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DNO HIS A 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS A 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS A 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS A 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS A 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS A 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO GLN B 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DNO HIS B 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS B 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS B 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS B 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS B 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS B 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO GLN C 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DNO HIS C 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS C 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS C 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS C 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS C 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS C 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO GLN D 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DNO HIS D 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS D 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS D 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS D 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO HIS D 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DNO 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 HE2 A 401 7
HET HE2 B 401 7
HET HE2 C 401 7
HET HE2 D 401 7
HETNAM HE2 HEXAN-1-OL
FORMUL 5 HE2 4(C6 H14 O)
FORMUL 9 HOH *995(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 SER B 215 LYS B 228 1 14
HELIX 27 27 LYS B 228 ALA B 241 1 14
HELIX 28 28 ALA B 241 ALA B 253 1 13
HELIX 29 29 THR B 274 ALA B 284 1 11
HELIX 30 30 TRP B 298 CYS B 303 1 6
HELIX 31 31 CYS B 303 SER B 316 1 14
HELIX 32 32 THR C 66 HIS C 71 5 6
HELIX 33 33 LEU C 73 ALA C 78 1 6
HELIX 34 34 SER C 102 SER C 118 1 17
HELIX 35 35 ASP C 129 ASN C 134 1 6
HELIX 36 36 THR C 135 ASN C 142 1 8
HELIX 37 37 ASP C 158 PHE C 164 5 7
HELIX 38 38 TRP C 176 ALA C 183 1 8
HELIX 39 39 ARG C 186 ALA C 193 1 8
HELIX 40 40 LYS C 195 HIS C 207 1 13
HELIX 41 41 ASN C 210 PHE C 214 5 5
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 LYS C 281 1 8
HELIX 46 46 TRP C 298 CYS C 303 1 6
HELIX 47 47 CYS C 303 SER C 316 1 14
HELIX 48 48 THR D 66 HIS D 71 5 6
HELIX 49 49 GLN D 72 ALA D 78 1 7
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 ALA D 282 1 9
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 VAL A 57 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 8 GLU B 35 VAL B 41 0
SHEET 2 B 8 VAL B 44 GLY B 52 -1 O VAL B 44 N VAL B 41
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 LEU B 125
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 LEU C 46 N ARG C 39
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 ILE C 84
SHEET 5 D 8 PHE C 123 HIS C 128 1 O VAL C 126 N VAL C 60
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 GLU D 35 VAL D 41 0
SHEET 2 E 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
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 LEU D 59 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 ALA D 127
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 2.01
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.02
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.00
LINK OD2 ASP A 129 CAF HE2 A 401 1555 1555 1.41
LINK OD2 ASP B 129 CAF HE2 B 401 1555 1555 1.41
LINK OD2 ASP C 129 CAF HE2 C 401 1555 1555 1.41
LINK OD2 ASP D 129 CAF HE2 D 401 1555 1555 1.42
SITE 1 AC1 6 ASP A 129 HIS A 177 PHE A 178 HIS A 207
SITE 2 AC1 6 TYR A 239 HIS A 297
SITE 1 AC2 7 ASP B 129 LEU B 174 HIS B 177 PHE B 178
SITE 2 AC2 7 HIS B 207 TYR B 239 HIS B 297
SITE 1 AC3 7 ASP C 129 HIS C 177 PHE C 178 HIS C 207
SITE 2 AC3 7 TYR C 239 GLY C 270 HIS C 297
SITE 1 AC4 5 ASP D 129 HIS D 177 PHE D 178 TYR D 239
SITE 2 AC4 5 HIS D 297
CRYST1 168.080 83.663 89.248 90.00 100.52 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 0.005950 0.000000 0.001105 0.00000
SCALE2 0.000000 0.011953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011396 0.00000
TER 2407 HIS A 321
TER 4750 ARG B 317
TER 7157 HIS C 321
TER 9500 GLY D 318
MASTER 397 0 4 63 36 0 8 610449 4 40 96
END |