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HEADER HYDROLASE 07-FEB-12 4DM7
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE E153D
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,D.R.MADDEN
REVDAT 1 07-AUG-13 4DM7 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. 1.36 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) : 1.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 258287
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12908
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 43.6845 - 4.2246 0.99 8235 650 0.2178 0.1939
REMARK 3 2 4.2246 - 3.3536 1.00 8789 0 0.1971 10000000.0000
REMARK 3 3 3.3536 - 2.9298 1.00 8125 652 0.2079 0.2127
REMARK 3 4 2.9298 - 2.6619 1.00 8085 654 0.2050 0.2122
REMARK 3 5 2.6619 - 2.4712 1.00 8697 0 0.2024 10000000.0000
REMARK 3 6 2.4712 - 2.3255 1.00 8080 654 0.1998 0.2155
REMARK 3 7 2.3255 - 2.2090 1.00 8058 653 0.1916 0.2145
REMARK 3 8 2.2090 - 2.1129 1.00 8677 0 0.1970 10000000.0000
REMARK 3 9 2.1129 - 2.0315 0.99 8036 644 0.1927 0.2078
REMARK 3 10 2.0315 - 1.9614 1.00 8020 653 0.1939 0.2067
REMARK 3 11 1.9614 - 1.9001 0.99 8657 0 0.1941 10000000.0000
REMARK 3 12 1.9001 - 1.8458 0.99 7941 649 0.1950 0.2124
REMARK 3 13 1.8458 - 1.7972 0.99 8005 649 0.1870 0.2080
REMARK 3 14 1.7972 - 1.7533 0.99 8619 0 0.1947 10000000.0000
REMARK 3 15 1.7533 - 1.7135 0.99 7927 642 0.1961 0.2181
REMARK 3 16 1.7135 - 1.6770 0.99 7969 651 0.1924 0.2199
REMARK 3 17 1.6770 - 1.6435 0.99 8599 0 0.1939 10000000.0000
REMARK 3 18 1.6435 - 1.6125 0.99 7933 643 0.1966 0.2197
REMARK 3 19 1.6125 - 1.5837 0.98 7903 648 0.2003 0.2358
REMARK 3 20 1.5837 - 1.5568 0.98 8543 0 0.2056 10000000.0000
REMARK 3 21 1.5568 - 1.5317 0.98 7895 637 0.2041 0.2361
REMARK 3 22 1.5317 - 1.5081 0.98 7948 640 0.2077 0.2409
REMARK 3 23 1.5081 - 1.4859 0.98 8468 0 0.2151 10000000.0000
REMARK 3 24 1.4859 - 1.4650 0.98 7878 641 0.2168 0.2362
REMARK 3 25 1.4650 - 1.4452 0.98 7864 640 0.2094 0.2294
REMARK 3 26 1.4452 - 1.4264 0.98 8470 0 0.2209 10000000.0000
REMARK 3 27 1.4264 - 1.4086 0.98 7858 640 0.2257 0.2414
REMARK 3 28 1.4086 - 1.3916 0.97 7822 635 0.2274 0.2465
REMARK 3 29 1.3916 - 1.3755 0.97 8532 0 0.2342 10000000.0000
REMARK 3 30 1.3755 - 1.3600 0.97 7746 633 0.2389 0.2653
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 : 39.75
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.520
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) : -2.28330
REMARK 3 B22 (A**2) : -0.60760
REMARK 3 B33 (A**2) : 2.89090
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.05090
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 9751
REMARK 3 ANGLE : 1.062 13244
REMARK 3 CHIRALITY : 0.076 1366
REMARK 3 PLANARITY : 0.005 1743
REMARK 3 DIHEDRAL : 12.336 3556
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): -5.8453 -37.2415 -27.0427
REMARK 3 T TENSOR
REMARK 3 T11: 0.0393 T22: 0.0401
REMARK 3 T33: 0.0409 T12: -0.0023
REMARK 3 T13: 0.0033 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.3876 L22: 0.3429
REMARK 3 L33: 0.2827 L12: -0.0420
REMARK 3 L13: 0.0055 L23: -0.0228
REMARK 3 S TENSOR
REMARK 3 S11: 0.0218 S12: 0.0285 S13: 0.0601
REMARK 3 S21: -0.0158 S22: -0.0198 S23: 0.0340
REMARK 3 S31: -0.0307 S32: -0.0072 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain B and resid 25:318)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6969 -76.6236 -15.6315
REMARK 3 T TENSOR
REMARK 3 T11: 0.0424 T22: 0.0387
REMARK 3 T33: 0.0338 T12: -0.0192
REMARK 3 T13: 0.0058 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 0.5260 L22: 0.4355
REMARK 3 L33: 0.2731 L12: 0.1978
REMARK 3 L13: -0.0331 L23: -0.1099
REMARK 3 S TENSOR
REMARK 3 S11: 0.0091 S12: -0.0212 S13: -0.0210
REMARK 3 S21: 0.0223 S22: 0.0061 S23: 0.0713
REMARK 3 S31: 0.0417 S32: -0.0168 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain C and resid 25:320)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0442 -70.1291 -27.2248
REMARK 3 T TENSOR
REMARK 3 T11: 0.0387 T22: 0.0372
REMARK 3 T33: 0.0309 T12: -0.0027
REMARK 3 T13: 0.0005 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.3861 L22: 0.2589
REMARK 3 L33: 0.3158 L12: -0.0220
REMARK 3 L13: 0.0490 L23: 0.0262
REMARK 3 S TENSOR
REMARK 3 S11: 0.0239 S12: 0.0373 S13: -0.0546
REMARK 3 S21: -0.0091 S22: -0.0180 S23: -0.0226
REMARK 3 S31: 0.0375 S32: 0.0103 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain D and resid 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8881 -30.6836 -15.6301
REMARK 3 T TENSOR
REMARK 3 T11: 0.0426 T22: 0.0400
REMARK 3 T33: 0.0516 T12: -0.0191
REMARK 3 T13: -0.0093 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.4761 L22: 0.4791
REMARK 3 L33: 0.3000 L12: 0.2120
REMARK 3 L13: 0.0538 L23: 0.0894
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: -0.0246 S13: 0.0576
REMARK 3 S21: 0.0393 S22: 0.0012 S23: -0.0436
REMARK 3 S31: -0.0413 S32: 0.0172 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 4DM7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070504.
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 : 258302
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.360
REMARK 200 RESOLUTION RANGE LOW (A) : 44.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07500
REMARK 200 FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45400
REMARK 200 FOR SHELL : 3.700
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 (%): 45.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% 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 84.17650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.06900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.17650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.06900
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: 2750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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: 20860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 587 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 656 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 626 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 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
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 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 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 C 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 -129.82 61.12
REMARK 500 ALA A 154 148.13 178.01
REMARK 500 CYS A 303 57.79 -142.54
REMARK 500 THR B 99 -67.25 -93.94
REMARK 500 ASP B 129 -133.25 57.62
REMARK 500 ALA B 154 151.35 179.99
REMARK 500 CYS B 303 56.51 -144.61
REMARK 500 ASP C 129 -129.97 62.17
REMARK 500 ALA C 154 149.81 -179.57
REMARK 500 CYS C 303 56.87 -143.33
REMARK 500 THR D 99 -66.88 -95.91
REMARK 500 ASP D 129 -133.10 58.16
REMARK 500 ASP D 185 19.68 58.46
REMARK 500 CYS D 303 52.69 -144.74
REMARK 500
REMARK 500 REMARK: NULL
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: 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: 4DNF RELATED DB: PDB
REMARK 900 RELATED ID: 4DMO RELATED DB: PDB
DBREF 4DM7 A 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DM7 B 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DM7 C 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
DBREF 4DM7 D 25 319 UNP Q02P97 Q02P97_PSEAB 25 319
SEQADV 4DM7 ASP A 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DM7 HIS A 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS A 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS A 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS A 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS A 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS A 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 ASP B 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DM7 HIS B 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS B 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS B 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS B 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS B 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS B 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 ASP C 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DM7 HIS C 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS C 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS C 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS C 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS C 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS C 325 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 ASP D 153 UNP Q02P97 GLU 153 ENGINEERED MUTATION
SEQADV 4DM7 HIS D 320 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS D 321 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS D 322 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS D 323 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 HIS D 324 UNP Q02P97 EXPRESSION TAG
SEQADV 4DM7 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 ASP 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 ASP 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 ASP 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 ASP 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 *987(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 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 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 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 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 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 SER D 316 1 14
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 ALA A 127
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 PHE B 34 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 VAL B 57 O THR B 82
SHEET 5 C 8 PHE B 123 HIS B 128 1 O VAL B 126 N MET B 58
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 LYS C 50 N GLU C 35
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 LYS D 50 N GLU D 35
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 2.01
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.02
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.00
CRYST1 168.353 84.138 89.166 90.00 100.48 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005940 0.000000 0.001099 0.00000
SCALE2 0.000000 0.011885 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011405 0.00000
TER 2375 HIS A 320
TER 4738 GLY B 318
TER 7114 HIS C 320
TER 9455 ARG D 317
MASTER 390 0 0 64 40 0 0 610389 4 8 96
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