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HEADER OXIDOREDUCTASE, VIRAL PROTEIN 18-MAY-14 4QES
TITLE STRUCTURE OF A 16 NM PROTEIN CAGE DESIGNED BY FUSING SYMMETRIC
TITLE 2 OLIGOMERIC DOMAINS, QUADRUPLE MUTANT, I222 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-HAEM BROMOPEROXIDASE BPO-A2, MATRIX PROTEIN 1 CHIMERA;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: SEE REMARK 999;
COMPND 5 SYNONYM: DESIGNED 16NM TETRAHEDRAL PROTEIN CAGE, BPO2, BROMIDE
COMPND 6 PEROXIDASE, M1;
COMPND 7 EC: 1.11.1.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS, INFLUENZA A VIRUS;
SOURCE 3 ORGANISM_TAXID: 1894, 11320;
SOURCE 4 GENE: BPOA2, M;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PROTEIN DESIGN, BIONANOTECHNOLOGY, PROTEIN ASSEMBLY, SYMMETRY,
KEYWDS 2 BIOMATERIALS, OXIDOREDUCTASE, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-T.LAI,T.O.YEATES
REVDAT 1 20-MAY-15 4QES 0
JRNL AUTH Y.-T.LAI,T.O.YEATES
JRNL TITL STRUCTURAL TRANSITION OF A PROTEIN NANOCAGE AS A FUNCTION OF
JRNL TITL 2 PH AND SALT CONCENTRATION.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 4.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
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) : 4.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 12914
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) : 0.254
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 646
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) : 4.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 865
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10128
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 161.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 198.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.88000
REMARK 3 B22 (A**2) : -3.72000
REMARK 3 B33 (A**2) : 2.84000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 1.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.981
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 76.252
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.911
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10359 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9666 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14112 ; 1.440 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22149 ; 0.949 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1320 ; 4.271 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 465 ;35.453 ;23.742
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1575 ;15.472 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 66 ;19.286 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1605 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11946 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2436 ; 0.003 ; 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): 5289 ;17.367 ;19.675
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5288 ;17.368 ;19.674
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6606 ;28.124 ;29.476
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 441 B 1 441 27229 0.050 0.050
REMARK 3 2 A 1 441 C 1 441 27171 0.060 0.050
REMARK 3 3 B 1 441 C 1 441 27228 0.050 0.050
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 4QES COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-14.
REMARK 100 THE RCSB ID CODE IS RCSB085963.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : CRYO-COOLED DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12914
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.190
REMARK 200 RESOLUTION RANGE LOW (A) : 83.835
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.88500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.320
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, PH 4.4, 11%
REMARK 280 PEG3000, 200 MM SODIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 61.75500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.76000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 83.83500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 61.75500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.76000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.83500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 61.75500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.76000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.83500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 61.75500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.76000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 83.83500
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 186590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 HIS A 442
REMARK 465 ARG A 443
REMARK 465 SER A 444
REMARK 465 HIS A 445
REMARK 465 ARG A 446
REMARK 465 GLN A 447
REMARK 465 LEU A 448
REMARK 465 GLU A 449
REMARK 465 HIS A 450
REMARK 465 HIS A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 MET B 0
REMARK 465 HIS B 442
REMARK 465 ARG B 443
REMARK 465 SER B 444
REMARK 465 HIS B 445
REMARK 465 ARG B 446
REMARK 465 GLN B 447
REMARK 465 LEU B 448
REMARK 465 GLU B 449
REMARK 465 HIS B 450
REMARK 465 HIS B 451
REMARK 465 HIS B 452
REMARK 465 HIS B 453
REMARK 465 HIS B 454
REMARK 465 HIS B 455
REMARK 465 MET C 0
REMARK 465 HIS C 442
REMARK 465 ARG C 443
REMARK 465 SER C 444
REMARK 465 HIS C 445
REMARK 465 ARG C 446
REMARK 465 GLN C 447
REMARK 465 LEU C 448
REMARK 465 GLU C 449
REMARK 465 HIS C 450
REMARK 465 HIS C 451
REMARK 465 HIS C 452
REMARK 465 HIS C 453
REMARK 465 HIS C 454
REMARK 465 HIS C 455
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 GLN A 279 CG CD OE1 NE2
REMARK 470 GLU A 280 CG CD OE1 OE2
REMARK 470 GLN A 282 CG CD OE1 NE2
REMARK 470 LYS A 283 CG CD CE NZ
REMARK 470 GLN A 284 CG CD OE1 NE2
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 GLN B 279 CG CD OE1 NE2
REMARK 470 GLU B 280 CG CD OE1 OE2
REMARK 470 GLN B 282 CG CD OE1 NE2
REMARK 470 LYS B 283 CG CD CE NZ
REMARK 470 GLN B 284 CG CD OE1 NE2
REMARK 470 LYS B 285 CG CD CE NZ
REMARK 470 GLN C 279 CG CD OE1 NE2
REMARK 470 GLU C 280 CG CD OE1 OE2
REMARK 470 GLN C 282 CG CD OE1 NE2
REMARK 470 LYS C 283 CG CD CE NZ
REMARK 470 GLN C 284 CG CD OE1 NE2
REMARK 470 LYS C 285 CG CD CE NZ
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 ASN A 9 -121.97 50.94
REMARK 500 PRO A 33 40.28 -105.84
REMARK 500 SER A 98 -120.19 55.39
REMARK 500 THR A 176 -79.02 -126.45
REMARK 500 TYR A 206 34.77 -98.78
REMARK 500 THR A 236 -68.34 -127.26
REMARK 500 ILE A 334 -54.73 73.11
REMARK 500 ASN B 9 -121.62 50.40
REMARK 500 PRO B 33 40.33 -105.91
REMARK 500 SER B 98 -120.01 55.56
REMARK 500 PHE B 128 135.13 -170.24
REMARK 500 THR B 176 -79.39 -126.92
REMARK 500 TYR B 206 34.81 -98.37
REMARK 500 THR B 236 -69.90 -127.03
REMARK 500 ILE B 334 -54.99 72.26
REMARK 500 ASN C 9 -121.92 50.76
REMARK 500 SER C 98 -119.84 54.85
REMARK 500 THR C 176 -78.80 -126.69
REMARK 500 TYR C 206 35.05 -98.79
REMARK 500 THR C 236 -76.46 -126.48
REMARK 500 ILE C 334 -55.73 72.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QF0 RELATED DB: PDB
REMARK 900 RELATED ID: 4QFF RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE DESIGNED PROTEIN CONSTRUCT IS A CHIMERA COMPRISING BPO2 (UNP
REMARK 999 P29715) AND RESIDUES 2-164 (UNP P03485) OF M1, SEPARATED BY A
REMARK 999 LINKER.
DBREF 4QES A 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QES A 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QES B 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QES B 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QES C 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QES C 286 447 UNP P03485 M1_I34A1 3 164
SEQADV 4QES THR A 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QES ALA A 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QES ALA A 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QES ALA A 278 UNP P03485 LINKER
SEQADV 4QES GLN A 279 UNP P03485 LINKER
SEQADV 4QES GLU A 280 UNP P03485 LINKER
SEQADV 4QES ALA A 281 UNP P03485 LINKER
SEQADV 4QES GLN A 282 UNP P03485 LINKER
SEQADV 4QES LYS A 283 UNP P03485 LINKER
SEQADV 4QES GLN A 284 UNP P03485 LINKER
SEQADV 4QES LYS A 285 UNP P03485 LINKER
SEQADV 4QES LEU A 448 UNP P03485 EXPRESSION TAG
SEQADV 4QES GLU A 449 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS A 450 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS A 451 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS A 452 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS A 453 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS A 454 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS A 455 UNP P03485 EXPRESSION TAG
SEQADV 4QES THR B 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QES ALA B 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QES ALA B 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QES ALA B 278 UNP P03485 LINKER
SEQADV 4QES GLN B 279 UNP P03485 LINKER
SEQADV 4QES GLU B 280 UNP P03485 LINKER
SEQADV 4QES ALA B 281 UNP P03485 LINKER
SEQADV 4QES GLN B 282 UNP P03485 LINKER
SEQADV 4QES LYS B 283 UNP P03485 LINKER
SEQADV 4QES GLN B 284 UNP P03485 LINKER
SEQADV 4QES LYS B 285 UNP P03485 LINKER
SEQADV 4QES LEU B 448 UNP P03485 EXPRESSION TAG
SEQADV 4QES GLU B 449 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS B 450 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS B 451 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS B 452 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS B 453 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS B 454 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS B 455 UNP P03485 EXPRESSION TAG
SEQADV 4QES THR C 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QES ALA C 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QES ALA C 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QES ALA C 278 UNP P03485 LINKER
SEQADV 4QES GLN C 279 UNP P03485 LINKER
SEQADV 4QES GLU C 280 UNP P03485 LINKER
SEQADV 4QES ALA C 281 UNP P03485 LINKER
SEQADV 4QES GLN C 282 UNP P03485 LINKER
SEQADV 4QES LYS C 283 UNP P03485 LINKER
SEQADV 4QES GLN C 284 UNP P03485 LINKER
SEQADV 4QES LYS C 285 UNP P03485 LINKER
SEQADV 4QES LEU C 448 UNP P03485 EXPRESSION TAG
SEQADV 4QES GLU C 449 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS C 450 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS C 451 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS C 452 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS C 453 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS C 454 UNP P03485 EXPRESSION TAG
SEQADV 4QES HIS C 455 UNP P03485 EXPRESSION TAG
SEQRES 1 A 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 A 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 A 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 A 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 A 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 A 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 A 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 A 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 A 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 A 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 A 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 A 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 A 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 A 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 A 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 A 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 A 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 A 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 A 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 A 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 A 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 A 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 A 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 A 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 A 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 A 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 A 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 A 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 A 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 A 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 A 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 A 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 A 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 A 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 A 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 A 456 HIS
SEQRES 1 B 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 B 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 B 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 B 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 B 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 B 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 B 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 B 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 B 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 B 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 B 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 B 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 B 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 B 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 B 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 B 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 B 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 B 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 B 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 B 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 B 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 B 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 B 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 B 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 B 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 B 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 B 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 B 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 B 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 B 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 B 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 B 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 B 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 B 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 B 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 B 456 HIS
SEQRES 1 C 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 C 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 C 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 C 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 C 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 C 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 C 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 C 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 C 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 C 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 C 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 C 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 C 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 C 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 C 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 C 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 C 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 C 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 C 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 C 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 C 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 C 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 C 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 C 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 C 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 C 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 C 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 C 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 C 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 C 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 C 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 C 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 C 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 C 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 C 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 C 456 HIS
HELIX 1 1 SER A 35 SER A 38 5 4
HELIX 2 2 TRP A 39 ALA A 49 1 11
HELIX 3 3 ASP A 72 ASP A 88 1 17
HELIX 4 4 MET A 99 GLY A 112 1 14
HELIX 5 5 PRO A 141 ASP A 155 1 15
HELIX 6 6 ARG A 156 ASN A 169 1 14
HELIX 7 7 ASN A 169 LEU A 174 1 6
HELIX 8 8 SER A 179 SER A 192 1 14
HELIX 9 9 GLY A 194 TRP A 205 1 12
HELIX 10 10 ASP A 212 ILE A 216 5 5
HELIX 11 11 PRO A 232 LEU A 244 1 13
HELIX 12 12 GLY A 258 HIS A 263 1 6
HELIX 13 13 HIS A 263 SER A 296 1 34
HELIX 14 14 GLY A 301 ALA A 316 1 16
HELIX 15 15 ASP A 321 THR A 331 1 11
HELIX 16 16 SER A 336 VAL A 351 1 16
HELIX 17 17 ARG A 360 LEU A 367 1 8
HELIX 18 18 ASN A 368 GLY A 371 5 4
HELIX 19 19 ASP A 372 LYS A 387 1 16
HELIX 20 20 THR A 391 LEU A 400 1 10
HELIX 21 21 SER A 403 ASN A 416 1 14
HELIX 22 22 THR A 422 GLN A 441 1 20
HELIX 23 23 SER B 35 SER B 38 5 4
HELIX 24 24 TRP B 39 ALA B 49 1 11
HELIX 25 25 ASP B 72 ASP B 88 1 17
HELIX 26 26 MET B 99 GLY B 112 1 14
HELIX 27 27 PRO B 141 ASP B 155 1 15
HELIX 28 28 ARG B 156 ASN B 169 1 14
HELIX 29 29 ASN B 169 LEU B 174 1 6
HELIX 30 30 SER B 179 SER B 192 1 14
HELIX 31 31 GLY B 194 TRP B 205 1 12
HELIX 32 32 ASP B 212 ILE B 216 5 5
HELIX 33 33 PRO B 232 LEU B 244 1 13
HELIX 34 34 GLY B 258 HIS B 263 1 6
HELIX 35 35 HIS B 263 SER B 296 1 34
HELIX 36 36 GLY B 301 ALA B 316 1 16
HELIX 37 37 ASP B 321 THR B 331 1 11
HELIX 38 38 SER B 336 VAL B 351 1 16
HELIX 39 39 ARG B 360 LEU B 367 1 8
HELIX 40 40 ASN B 368 GLY B 371 5 4
HELIX 41 41 ASP B 372 ARG B 388 1 17
HELIX 42 42 THR B 391 LEU B 400 1 10
HELIX 43 43 SER B 403 ASN B 416 1 14
HELIX 44 44 THR B 422 GLN B 441 1 20
HELIX 45 45 SER C 35 SER C 38 5 4
HELIX 46 46 TRP C 39 ALA C 49 1 11
HELIX 47 47 ASP C 72 ASP C 88 1 17
HELIX 48 48 MET C 99 GLY C 112 1 14
HELIX 49 49 PRO C 141 ASP C 155 1 15
HELIX 50 50 ARG C 156 ASN C 169 1 14
HELIX 51 51 ASN C 169 LEU C 174 1 6
HELIX 52 52 SER C 179 SER C 192 1 14
HELIX 53 53 GLY C 194 TRP C 205 1 12
HELIX 54 54 ASP C 212 ILE C 216 5 5
HELIX 55 55 THR C 236 LEU C 244 1 9
HELIX 56 56 GLY C 258 HIS C 263 1 6
HELIX 57 57 HIS C 263 SER C 296 1 34
HELIX 58 58 GLY C 301 ALA C 316 1 16
HELIX 59 59 ASP C 321 THR C 331 1 11
HELIX 60 60 SER C 336 VAL C 351 1 16
HELIX 61 61 ARG C 360 LEU C 367 1 8
HELIX 62 62 ASN C 368 GLY C 371 5 4
HELIX 63 63 ASP C 372 ARG C 388 1 17
HELIX 64 64 THR C 391 LEU C 400 1 10
HELIX 65 65 SER C 403 ASN C 416 1 14
HELIX 66 66 THR C 422 GLN C 441 1 20
SHEET 1 A 8 PHE A 2 GLU A 8 0
SHEET 2 A 8 THR A 11 HIS A 20 -1 O LEU A 15 N ILE A 3
SHEET 3 A 8 ARG A 52 TYR A 56 -1 O VAL A 53 N HIS A 20
SHEET 4 A 8 PRO A 25 ILE A 29 1 N VAL A 26 O ARG A 52
SHEET 5 A 8 ALA A 92 PHE A 97 1 O VAL A 93 N VAL A 27
SHEET 6 A 8 ILE A 116 LEU A 122 1 O ALA A 117 N ALA A 92
SHEET 7 A 8 ALA A 220 GLY A 225 1 O LEU A 223 N PHE A 121
SHEET 8 A 8 GLU A 248 VAL A 252 1 O VAL A 252 N HIS A 224
SHEET 1 B 8 PHE B 2 GLU B 8 0
SHEET 2 B 8 THR B 11 HIS B 20 -1 O LEU B 15 N ILE B 3
SHEET 3 B 8 ARG B 52 TYR B 56 -1 O VAL B 53 N HIS B 20
SHEET 4 B 8 PRO B 25 ILE B 29 1 N VAL B 26 O ARG B 52
SHEET 5 B 8 ALA B 92 PHE B 97 1 O VAL B 93 N VAL B 27
SHEET 6 B 8 ILE B 116 LEU B 122 1 O ALA B 117 N ALA B 92
SHEET 7 B 8 ALA B 220 GLY B 225 1 O LEU B 223 N PHE B 121
SHEET 8 B 8 GLU B 248 VAL B 252 1 O VAL B 252 N HIS B 224
SHEET 1 C 8 PHE C 2 GLU C 8 0
SHEET 2 C 8 THR C 11 HIS C 20 -1 O LEU C 15 N ILE C 3
SHEET 3 C 8 ARG C 52 TYR C 56 -1 O VAL C 53 N HIS C 20
SHEET 4 C 8 PRO C 25 ILE C 29 1 N VAL C 26 O ARG C 52
SHEET 5 C 8 ALA C 92 PHE C 97 1 O VAL C 93 N VAL C 27
SHEET 6 C 8 ILE C 116 LEU C 122 1 O ALA C 117 N ALA C 92
SHEET 7 C 8 ALA C 220 GLY C 225 1 O LEU C 223 N PHE C 121
SHEET 8 C 8 GLU C 248 VAL C 252 1 O VAL C 252 N HIS C 224
CISPEP 1 PHE A 32 PRO A 33 0 -1.72
CISPEP 2 GLU A 126 PRO A 127 0 7.61
CISPEP 3 PHE B 32 PRO B 33 0 -1.65
CISPEP 4 GLU B 126 PRO B 127 0 6.48
CISPEP 5 PHE C 32 PRO C 33 0 -1.53
CISPEP 6 GLU C 126 PRO C 127 0 6.85
CRYST1 123.510 165.520 167.670 90.00 90.00 90.00 I 2 2 2 24
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 0.008097 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006042 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005964 0.00000
TER 3377 GLN A 441
TER 6754 GLN B 441
TER 10131 GLN C 441
MASTER 393 0 0 66 24 0 0 610128 3 0 108
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