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HEADER DE NOVO PROTEIN 21-JAN-16 5HQ3
TITLE HUMAN ACETYLCHOLINESTERASE DESIGN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DESIGN OF HUMAN ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DESIGN OF HUMAN ACETYLCHOLINESTERASE;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DESIGN, DE NOVO PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GOLDENZWEIG,M.GOLDSMITH,S.E.HILL,O.GERTMAN,P.LAURINO,Y.ASHANI,
AUTHOR 2 O.DYM,S.ALBECK,T.UNGER,J.PRILUSKY,R.L.LIEBERMAN,A.AHARONI,I.SILMAN,
AUTHOR 3 J.L.SUSSMAN,D.S.TAWFIK,S.J.FLEISHMAN
REVDAT 1 27-JUL-16 5HQ3 0
JRNL AUTH A.GOLDENZWEIG,M.GOLDSMITH,S.E.HILL,O.GERTMAN,P.LAURINO,
JRNL AUTH 2 Y.ASHANI,O.DYM,T.UNGER,S.ALBECK,J.PRILUSKY,R.L.LIEBERMAN,
JRNL AUTH 3 A.AHARONI,I.SILMAN,J.L.SUSSMAN,D.S.TAWFIK,S.J.FLEISHMAN
JRNL TITL AUTOMATED STRUCTURE- AND SEQUENCE-BASED DESIGN OF PROTEINS
JRNL TITL 2 FOR HIGH BACTERIAL EXPRESSION AND STABILITY
JRNL REF MOL.CELL 2016
JRNL REFN ISSN 1097-2765
JRNL DOI 10.1016/J.MOLCEL.2016.06.012
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 48279
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2498
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3484
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8313
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.399
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.279
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.209
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.988
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8626 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7946 ; 0.009 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11785 ; 1.713 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18228 ; 1.005 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1055 ; 6.980 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 410 ;33.186 ;22.756
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1232 ;16.203 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 77 ;19.719 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1230 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9868 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2105 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4226 ; 2.999 ; 3.935
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4225 ; 2.974 ; 3.934
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5273 ; 4.580 ; 5.891
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5274 ; 4.581 ; 5.892
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4400 ; 3.285 ; 4.221
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4401 ; 3.285 ; 4.221
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6511 ; 5.063 ; 6.217
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9579 ; 6.701 ;31.399
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9577 ; 6.702 ;31.397
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5HQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217525.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95372
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50786
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 98.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : 0.10700
REMARK 200 FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 9.90
REMARK 200 R MERGE FOR SHELL (I) : 0.57600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 6000 0.1M MGCL2 0.1M MES PH=6,
REMARK 280 PH 6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 197.65250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 44.76700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 44.76700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 296.47875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 44.76700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 44.76700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 98.82625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 44.76700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.76700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 296.47875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 44.76700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.76700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 98.82625
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 197.65250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 3460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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 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 MET A 0
REMARK 465 GLU A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
REMARK 465 GLU A 4
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 ASP A 494
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 ALA A 497
REMARK 465 THR A 543
REMARK 465 ASP A 544
REMARK 465 THR A 545
REMARK 465 LEU A 546
REMARK 465 ASP A 547
REMARK 465 MET B 0
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLU B 4
REMARK 465 ASP B 5
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 ARG B 493
REMARK 465 ASP B 494
REMARK 465 PRO B 495
REMARK 465 LYS B 496
REMARK 465 ALA B 497
REMARK 465 ASP B 544
REMARK 465 THR B 545
REMARK 465 LEU B 546
REMARK 465 ASP B 547
REMARK 465 GLU B 548
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 109 CE NZ
REMARK 470 GLN A 291 CG CD OE1 NE2
REMARK 470 GLU A 292 CD OE1 OE2
REMARK 470 LYS A 322 CD CE NZ
REMARK 470 GLU A 357 CG CD OE1 OE2
REMARK 470 ARG A 417 CZ NH1 NH2
REMARK 470 LYS A 467 CG CD CE NZ
REMARK 470 LEU A 540 CG CD1 CD2
REMARK 470 ARG B 21 CZ NH1 NH2
REMARK 470 TYR B 105 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 109 CG CD CE NZ
REMARK 470 ARG B 143 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 165 NE CZ NH1 NH2
REMARK 470 GLN B 291 CG CD OE1 NE2
REMARK 470 GLU B 292 CG CD OE1 OE2
REMARK 470 GLU B 357 CG CD OE1 OE2
REMARK 470 ASP B 506 OD1 OD2
REMARK 470 LEU B 540 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 203 O2 VX A 601 1.91
REMARK 500 OG SER A 203 O1 VX A 601 2.05
REMARK 500 OG SER A 203 C1 VX A 601 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 296 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 424 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 274 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 PHE A 47 -3.55 63.98
REMARK 500 ALA A 167 69.20 -151.24
REMARK 500 ASN A 170 19.08 56.78
REMARK 500 SER A 203 -123.19 60.48
REMARK 500 ASP A 306 -74.91 -127.06
REMARK 500 GLU A 351 4.28 -69.02
REMARK 500 LEU A 353 88.66 -67.97
REMARK 500 VAL A 407 -52.81 -125.96
REMARK 500 ASP A 514 -157.73 -158.92
REMARK 500 SER A 541 56.17 -69.80
REMARK 500 GLU B 7 -37.31 81.71
REMARK 500 PHE B 47 -4.94 73.26
REMARK 500 PRO B 111 115.45 -39.07
REMARK 500 PHE B 123 5.09 59.30
REMARK 500 PHE B 158 -0.95 -143.40
REMARK 500 SER B 203 -127.33 65.30
REMARK 500 ASN B 233 32.18 -95.28
REMARK 500 ASP B 306 -87.83 -132.84
REMARK 500 SER B 347 145.93 171.13
REMARK 500 HIS B 387 54.97 -140.81
REMARK 500 PRO B 388 2.82 -68.81
REMARK 500 TRP B 442 -45.45 122.18
REMARK 500 ASP B 514 -155.92 -160.03
REMARK 500 ARG B 525 56.99 36.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA B 6 GLU B 7 -146.33
REMARK 500 ASN B 265 ASP B 266 146.96
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 VX A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VX B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 602
DBREF 5HQ3 A 0 547 PDB 5HQ3 5HQ3 0 547
DBREF 5HQ3 B 0 548 PDB 5HQ3 5HQ3 0 548
SEQRES 1 A 548 MET GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR THR
SEQRES 2 A 548 ARG GLY GLY ARG LEU ARG GLY ILE ARG LEU THR THR PRO
SEQRES 3 A 548 GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA
SEQRES 4 A 548 GLU PRO PRO VAL GLY PRO ARG ARG PHE ARG PRO PRO GLU
SEQRES 5 A 548 PRO LYS GLN PRO TRP SER GLY VAL TRP ASP ALA THR THR
SEQRES 6 A 548 PHE GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR
SEQRES 7 A 548 PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG
SEQRES 8 A 548 ASN LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR
SEQRES 9 A 548 PRO TYR PRO ARG PRO LYS ASN PRO ALA PRO VAL MET VAL
SEQRES 10 A 548 TRP ILE TYR GLY GLY GLY PHE TYR SER GLY SER SER SER
SEQRES 11 A 548 LEU ASP VAL TYR ASP GLY ARG PHE LEU VAL ARG THR GLU
SEQRES 12 A 548 ARG VAL VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA
SEQRES 13 A 548 PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO
SEQRES 14 A 548 GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN
SEQRES 15 A 548 TRP VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO
SEQRES 16 A 548 THR SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA
SEQRES 17 A 548 SER VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY
SEQRES 18 A 548 LEU PHE HIS ARG ALA ILE LEU GLN SER GLY ALA PRO ASN
SEQRES 19 A 548 ALA PRO TRP ALA TYR VAL SER ARG GLU GLU ALA ARG ARG
SEQRES 20 A 548 ARG ALA LEU GLN LEU ALA LYS LEU VAL GLY CYS PRO PRO
SEQRES 21 A 548 GLY GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS
SEQRES 22 A 548 LEU ARG ASN ARG PRO PRO GLN GLU LEU VAL ASN HIS GLU
SEQRES 23 A 548 TRP HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER
SEQRES 24 A 548 PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU PRO ASP THR
SEQRES 25 A 548 PRO GLU ALA LEU ILE ASN ASN GLY ASP PHE LYS GLY LEU
SEQRES 26 A 548 ASP VAL LEU VAL GLY VAL ASN LYS ASP GLU GLY SER TYR
SEQRES 27 A 548 PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN
SEQRES 28 A 548 GLU SER LEU ILE SER ARG GLU GLU PHE LEU GLU GLY VAL
SEQRES 29 A 548 ARG VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU
SEQRES 30 A 548 ALA ILE VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU
SEQRES 31 A 548 ASP PRO ALA LYS ASN ARG ASP ALA LEU SER ASP VAL VAL
SEQRES 32 A 548 GLY ASP HIS ASN VAL ILE CYS PRO VAL ALA GLN PHE ALA
SEQRES 33 A 548 GLN ARG TYR ALA ALA ASN GLY ALA ARG VAL TYR ALA TYR
SEQRES 34 A 548 VAL PHE GLU HIS ARG SER SER THR LEU PRO TRP PRO GLU
SEQRES 35 A 548 TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE
SEQRES 36 A 548 PHE GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR LYS
SEQRES 37 A 548 GLU GLU LYS ILE PHE ALA ARG ARG LEU MET ARG TYR TRP
SEQRES 38 A 548 ALA ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG
SEQRES 39 A 548 ASP PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA ASP
SEQRES 40 A 548 GLU GLN LYS TYR VAL SER LEU ASP LEU ARG PRO LEU GLU
SEQRES 41 A 548 VAL ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP
SEQRES 42 A 548 ASN ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR
SEQRES 43 A 548 LEU ASP
SEQRES 1 B 549 MET GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR THR
SEQRES 2 B 549 ARG GLY GLY ARG LEU ARG GLY ILE ARG LEU THR THR PRO
SEQRES 3 B 549 GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA
SEQRES 4 B 549 GLU PRO PRO VAL GLY PRO ARG ARG PHE ARG PRO PRO GLU
SEQRES 5 B 549 PRO LYS GLN PRO TRP SER GLY VAL TRP ASP ALA THR THR
SEQRES 6 B 549 PHE GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR
SEQRES 7 B 549 PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG
SEQRES 8 B 549 ASN LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR
SEQRES 9 B 549 PRO TYR PRO ARG PRO LYS ASN PRO ALA PRO VAL MET VAL
SEQRES 10 B 549 TRP ILE TYR GLY GLY GLY PHE TYR SER GLY SER SER SER
SEQRES 11 B 549 LEU ASP VAL TYR ASP GLY ARG PHE LEU VAL ARG THR GLU
SEQRES 12 B 549 ARG VAL VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA
SEQRES 13 B 549 PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO
SEQRES 14 B 549 GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN
SEQRES 15 B 549 TRP VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO
SEQRES 16 B 549 THR SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA
SEQRES 17 B 549 SER VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY
SEQRES 18 B 549 LEU PHE HIS ARG ALA ILE LEU GLN SER GLY ALA PRO ASN
SEQRES 19 B 549 ALA PRO TRP ALA TYR VAL SER ARG GLU GLU ALA ARG ARG
SEQRES 20 B 549 ARG ALA LEU GLN LEU ALA LYS LEU VAL GLY CYS PRO PRO
SEQRES 21 B 549 GLY GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS
SEQRES 22 B 549 LEU ARG ASN ARG PRO PRO GLN GLU LEU VAL ASN HIS GLU
SEQRES 23 B 549 TRP HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER
SEQRES 24 B 549 PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU PRO ASP THR
SEQRES 25 B 549 PRO GLU ALA LEU ILE ASN ASN GLY ASP PHE LYS GLY LEU
SEQRES 26 B 549 ASP VAL LEU VAL GLY VAL ASN LYS ASP GLU GLY SER TYR
SEQRES 27 B 549 PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN
SEQRES 28 B 549 GLU SER LEU ILE SER ARG GLU GLU PHE LEU GLU GLY VAL
SEQRES 29 B 549 ARG VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU
SEQRES 30 B 549 ALA ILE VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU
SEQRES 31 B 549 ASP PRO ALA LYS ASN ARG ASP ALA LEU SER ASP VAL VAL
SEQRES 32 B 549 GLY ASP HIS ASN VAL ILE CYS PRO VAL ALA GLN PHE ALA
SEQRES 33 B 549 GLN ARG TYR ALA ALA ASN GLY ALA ARG VAL TYR ALA TYR
SEQRES 34 B 549 VAL PHE GLU HIS ARG SER SER THR LEU PRO TRP PRO GLU
SEQRES 35 B 549 TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE
SEQRES 36 B 549 PHE GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR LYS
SEQRES 37 B 549 GLU GLU LYS ILE PHE ALA ARG ARG LEU MET ARG TYR TRP
SEQRES 38 B 549 ALA ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG
SEQRES 39 B 549 ASP PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA ASP
SEQRES 40 B 549 GLU GLN LYS TYR VAL SER LEU ASP LEU ARG PRO LEU GLU
SEQRES 41 B 549 VAL ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP
SEQRES 42 B 549 ASN ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR
SEQRES 43 B 549 LEU ASP GLU
HET VX A 601 6
HET MES A 602 12
HET VX B 601 6
HET MES B 602 12
HETNAM VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 3 VX 2(C3 H9 O3 P)
FORMUL 4 MES 2(C6 H13 N O4 S)
FORMUL 7 HOH *(H2 O)
HELIX 1 AA1 VAL A 42 ARG A 46 5 5
HELIX 2 AA2 PHE A 80 MET A 85 1 6
HELIX 3 AA3 LEU A 130 ASP A 134 5 5
HELIX 4 AA4 GLY A 135 ARG A 143 1 9
HELIX 5 AA5 VAL A 153 LEU A 159 1 7
HELIX 6 AA6 ASN A 170 ILE A 187 1 18
HELIX 7 AA7 ALA A 188 PHE A 190 5 3
HELIX 8 AA8 SER A 203 SER A 215 1 13
HELIX 9 AA9 PRO A 216 PHE A 222 5 7
HELIX 10 AB1 SER A 240 VAL A 255 1 16
HELIX 11 AB2 ASP A 266 ARG A 276 1 11
HELIX 12 AB3 PRO A 277 GLU A 285 1 9
HELIX 13 AB4 TRP A 286 LEU A 289 5 4
HELIX 14 AB5 THR A 311 ASN A 318 1 8
HELIX 15 AB6 GLY A 335 VAL A 340 1 6
HELIX 16 AB7 SER A 355 VAL A 367 1 13
HELIX 17 AB8 SER A 371 TYR A 382 1 12
HELIX 18 AB9 ASP A 390 VAL A 407 1 18
HELIX 19 AC1 VAL A 407 ASN A 421 1 15
HELIX 20 AC2 PRO A 440 GLY A 444 5 5
HELIX 21 AC3 GLU A 450 PHE A 455 1 6
HELIX 22 AC4 GLY A 456 ASP A 460 5 5
HELIX 23 AC5 THR A 466 GLY A 487 1 22
HELIX 24 AC6 ARG A 525 ARG A 534 1 10
HELIX 25 AC7 ARG A 534 SER A 541 1 8
HELIX 26 AC8 VAL B 42 ARG B 46 5 5
HELIX 27 AC9 PHE B 80 MET B 85 1 6
HELIX 28 AD1 LEU B 130 ASP B 134 5 5
HELIX 29 AD2 GLY B 135 ARG B 143 1 9
HELIX 30 AD3 VAL B 153 LEU B 159 1 7
HELIX 31 AD4 ASN B 170 ILE B 187 1 18
HELIX 32 AD5 ALA B 188 PHE B 190 5 3
HELIX 33 AD6 SER B 203 LEU B 214 1 12
HELIX 34 AD7 SER B 215 ARG B 219 5 5
HELIX 35 AD8 SER B 240 VAL B 255 1 16
HELIX 36 AD9 ASP B 266 ARG B 276 1 11
HELIX 37 AE1 PRO B 277 ASN B 283 1 7
HELIX 38 AE2 HIS B 284 LEU B 289 5 6
HELIX 39 AE3 THR B 311 ASN B 318 1 8
HELIX 40 AE4 GLY B 335 VAL B 340 1 6
HELIX 41 AE5 SER B 355 VAL B 367 1 13
HELIX 42 AE6 SER B 371 TYR B 382 1 12
HELIX 43 AE7 ASP B 390 VAL B 407 1 18
HELIX 44 AE8 VAL B 407 ASN B 421 1 15
HELIX 45 AE9 GLU B 450 PHE B 455 1 6
HELIX 46 AF1 GLY B 456 ASP B 460 5 5
HELIX 47 AF2 THR B 466 GLY B 487 1 22
HELIX 48 AF3 ARG B 525 ARG B 534 1 10
HELIX 49 AF4 ARG B 534 SER B 541 1 8
SHEET 1 AA1 3 LEU A 9 THR A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O TRP A 60 N ARG A 16
SHEET 1 AA211 ILE A 20 LEU A 22 0
SHEET 2 AA211 VAL A 29 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O THR A 103 N SER A 30
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 ALA A 112 ILE A 118 1 N PRO A 113 O VAL A 145
SHEET 6 AA211 GLY A 192 GLU A 202 1 O ASP A 193 N ALA A 112
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 ASP A 325 ASN A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 10 AA211 LYS A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 3 LEU B 9 THR B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O TRP B 60 N ARG B 16
SHEET 1 AA511 ILE B 20 LEU B 22 0
SHEET 2 AA511 VAL B 29 PRO B 36 -1 O ALA B 31 N ILE B 20
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O THR B 103 N SER B 30
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 ALA B 112 ILE B 118 1 N TRP B 117 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O THR B 198 N VAL B 114
SHEET 7 AA511 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA511 VAL B 326 ASN B 331 1 O LEU B 327 N ALA B 225
SHEET 9 AA511 VAL B 425 PHE B 430 1 O TYR B 426 N VAL B 328
SHEET 10 AA511 LYS B 509 LEU B 513 1 O VAL B 511 N ALA B 427
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 68 CYS B 69 0
SHEET 2 AA6 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.06
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.06
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.05
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.05
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.01
LINK OG SER A 203 P1 VX A 601 1555 1555 1.55
LINK OG SER B 203 P1 VX B 601 1555 1555 1.52
CISPEP 1 TYR A 105 PRO A 106 0 -4.66
CISPEP 2 TYR B 105 PRO B 106 0 -1.91
SITE 1 AC1 6 GLY A 121 GLY A 122 SER A 203 ALA A 204
SITE 2 AC1 6 TRP A 236 HIS A 447
SITE 1 AC2 4 TRP A 286 SER A 293 PHE A 295 TYR A 341
SITE 1 AC3 8 GLY B 121 GLY B 122 TYR B 124 SER B 203
SITE 2 AC3 8 ALA B 204 TRP B 236 PHE B 295 HIS B 447
SITE 1 AC4 4 TRP B 286 VAL B 294 PHE B 295 TYR B 341
CRYST1 89.534 89.534 395.305 90.00 90.00 90.00 P 43 21 2 8
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 0.011169 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011169 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002530 0.00000
TER 4174 ALA A 542
TER 8321 THR B 543
MASTER 429 0 4 49 32 0 6 6 8350 2 50 86
END |