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HEADER DE NOVO PROTEIN 06-JAN-12 3VDX
TITLE STRUCTURE OF A 16 NM PROTEIN CAGE DESIGNED BY FUSING SYMMETRIC
TITLE 2 OLIGOMERIC DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DESIGNED 16NM TETRAHEDRAL PROTEIN CAGE CONTAINING NON-HAEM
COMPND 3 BROMOPEROXIDASE BPO-A2 AND MATRIX PROTEIN 1;
COMPND 4 CHAIN: A, B, C;
COMPND 5 SYNONYM: BPO2, BROMIDE PEROXIDASE, M1;
COMPND 6 EC: 1.11.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS, INFLUENZA A VIRUS;
SOURCE 3 ORGANISM_TAXID: 1894, 211044;
SOURCE 4 STRAIN: A/PUERTO RICO/8/1934 H1N1;
SOURCE 5 GENE: BPOA2, BROMOPEROXIDASE A2, M, M1 MATRIX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PROTEIN DESIGN, BIONANOTECHNOLOGY, PROTEIN ASSEMBLY, SYMMETRY,
KEYWDS 2 BIOMATERIALS, DE NOVO PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-T.LAI,D.CASCIO,T.O.YEATES
REVDAT 1 20-JUN-12 3VDX 0
JRNL AUTH Y.T.LAI,D.CASCIO,T.O.YEATES
JRNL TITL STRUCTURE OF A 16-NM CAGE DESIGNED BY USING PROTEIN
JRNL TITL 2 OLIGOMERS.
JRNL REF SCIENCE V. 336 1129 2012
JRNL REFN ISSN 0036-8075
JRNL PMID 22654051
JRNL DOI 10.1126/SCIENCE.1219351
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 68.6
REMARK 3 NUMBER OF REFLECTIONS : 22131
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1133
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 19.7287 - 5.9562 1.00 3983 204 0.2096 0.2370
REMARK 3 2 5.9562 - 4.7493 1.00 3843 203 0.2195 0.2619
REMARK 3 3 4.7493 - 4.1554 1.00 3809 218 0.1917 0.2729
REMARK 3 4 4.1554 - 3.7783 0.73 2775 146 0.2432 0.3188
REMARK 3 5 3.7783 - 3.5091 0.61 2300 126 0.2726 0.3273
REMARK 3 6 3.5091 - 3.3033 0.41 1525 90 0.2952 0.3196
REMARK 3 7 3.3033 - 3.1385 0.47 1797 87 0.2878 0.3217
REMARK 3 8 3.1385 - 3.0020 0.26 966 59 0.2753 0.3658
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.28
REMARK 3 B_SOL : 0.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.56
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.64830
REMARK 3 B22 (A**2) : -7.64470
REMARK 3 B33 (A**2) : -5.12960
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 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 : 0.002 10380
REMARK 3 ANGLE : 0.555 14127
REMARK 3 CHIRALITY : 0.040 1599
REMARK 3 PLANARITY : 0.003 1836
REMARK 3 DIHEDRAL : 11.692 3684
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3VDX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB069923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX HR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22135
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 19.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 68.3
REMARK 200 DATA REDUNDANCY : 4.950
REMARK 200 R MERGE (I) : 0.20600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 20.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.66900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.910
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: PDB ENTRIES 1BRO, 1AA7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M NAH2PO4, 0.8M K2HPO4, 0.1M CAPS,
REMARK 280 PH 10.3, VAPOR DIFFUSION, HANGING DROP, 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 61.29500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.85500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 102.11000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 61.29500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.85500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 102.11000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 61.29500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.85500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 102.11000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 61.29500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.85500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 102.11000
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: 40820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 184730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -122.59000
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 -122.59000
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 ASP A 439
REMARK 465 SER A 440
REMARK 465 GLN A 441
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 ASP B 439
REMARK 465 SER B 440
REMARK 465 GLN B 441
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 ASP C 439
REMARK 465 SER C 440
REMARK 465 GLN C 441
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 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 -115.74 57.06
REMARK 500 LEU A 34 -155.14 -82.67
REMARK 500 SER A 98 -107.09 53.85
REMARK 500 GLU A 172 -29.50 -140.87
REMARK 500 THR A 176 -72.49 -140.55
REMARK 500 TYR A 206 48.82 -91.42
REMARK 500 THR A 236 -79.88 -131.63
REMARK 500 PRO A 256 -145.19 -76.86
REMARK 500 LEU A 357 -157.54 -128.55
REMARK 500 ASN A 370 -49.13 69.90
REMARK 500 ALA A 420 74.06 56.39
REMARK 500 ASN B 9 -121.40 55.81
REMARK 500 LEU B 34 -152.62 -76.14
REMARK 500 TYR B 71 73.89 -103.90
REMARK 500 SER B 98 -107.99 51.87
REMARK 500 SER B 110 -24.55 -145.68
REMARK 500 THR B 132 -168.69 -115.42
REMARK 500 ASN B 169 71.93 53.30
REMARK 500 GLU B 172 -36.29 -130.18
REMARK 500 THR B 176 -81.27 -118.97
REMARK 500 TYR B 206 38.90 -89.37
REMARK 500 THR B 236 -86.45 -120.25
REMARK 500 GLU B 248 109.38 -59.23
REMARK 500 HIS B 263 48.62 -97.49
REMARK 500 LEU B 286 -47.46 -130.96
REMARK 500 SER B 353 88.93 -67.53
REMARK 500 ARG B 355 -2.72 63.78
REMARK 500 LEU B 357 -159.16 -144.45
REMARK 500 ARG B 360 158.28 -43.40
REMARK 500 ASN B 368 -71.87 -64.47
REMARK 500 ILE B 390 -62.02 -126.62
REMARK 500 ASN B 416 14.90 -64.08
REMARK 500 THR B 422 -155.68 -90.81
REMARK 500 ASN C 9 -113.69 52.42
REMARK 500 PRO C 33 65.04 -118.38
REMARK 500 LEU C 34 -164.10 -105.99
REMARK 500 SER C 98 -110.82 52.70
REMARK 500 THR C 176 -67.52 -135.52
REMARK 500 TYR C 206 55.94 -90.24
REMARK 500 THR C 236 -83.52 -128.95
REMARK 500 PRO C 256 -158.06 -79.65
REMARK 500 HIS C 263 58.18 -109.66
REMARK 500 SER C 353 60.24 -109.98
REMARK 500 ARG C 355 -8.85 68.76
REMARK 500 ASN C 370 -33.98 67.77
REMARK 500 MET C 418 -74.09 -101.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4D9J RELATED DB: PDB
DBREF 3VDX A 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 3VDX A 286 447 UNP P03485 M1_I34A1 3 164
DBREF 3VDX B 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 3VDX B 286 447 UNP P03485 M1_I34A1 3 164
DBREF 3VDX C 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 3VDX C 286 447 UNP P03485 M1_I34A1 3 164
SEQADV 3VDX VAL A 24 UNP P29715 GLN 25 CONFLICT
SEQADV 3VDX ALA A 118 UNP P29715 LYS 119 CONFLICT
SEQADV 3VDX ALA A 278 UNP P29715 LINKER
SEQADV 3VDX LEU A 279 UNP P29715 LINKER
SEQADV 3VDX GLU A 280 UNP P29715 LINKER
SEQADV 3VDX ALA A 281 UNP P29715 LINKER
SEQADV 3VDX GLN A 282 UNP P29715 LINKER
SEQADV 3VDX LYS A 283 UNP P29715 LINKER
SEQADV 3VDX GLN A 284 UNP P29715 LINKER
SEQADV 3VDX LYS A 285 UNP P29715 LINKER
SEQADV 3VDX LEU A 448 UNP P03485 EXPRESSION TAG
SEQADV 3VDX GLU A 449 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS A 450 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS A 451 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS A 452 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS A 453 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS A 454 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS A 455 UNP P03485 EXPRESSION TAG
SEQADV 3VDX VAL B 24 UNP P29715 GLN 25 CONFLICT
SEQADV 3VDX ALA B 118 UNP P29715 LYS 119 CONFLICT
SEQADV 3VDX ALA B 278 UNP P29715 LINKER
SEQADV 3VDX LEU B 279 UNP P29715 LINKER
SEQADV 3VDX GLU B 280 UNP P29715 LINKER
SEQADV 3VDX ALA B 281 UNP P29715 LINKER
SEQADV 3VDX GLN B 282 UNP P29715 LINKER
SEQADV 3VDX LYS B 283 UNP P29715 LINKER
SEQADV 3VDX GLN B 284 UNP P29715 LINKER
SEQADV 3VDX LYS B 285 UNP P29715 LINKER
SEQADV 3VDX LEU B 448 UNP P03485 EXPRESSION TAG
SEQADV 3VDX GLU B 449 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS B 450 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS B 451 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS B 452 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS B 453 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS B 454 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS B 455 UNP P03485 EXPRESSION TAG
SEQADV 3VDX VAL C 24 UNP P29715 GLN 25 CONFLICT
SEQADV 3VDX ALA C 118 UNP P29715 LYS 119 CONFLICT
SEQADV 3VDX ALA C 278 UNP P29715 LINKER
SEQADV 3VDX LEU C 279 UNP P29715 LINKER
SEQADV 3VDX GLU C 280 UNP P29715 LINKER
SEQADV 3VDX ALA C 281 UNP P29715 LINKER
SEQADV 3VDX GLN C 282 UNP P29715 LINKER
SEQADV 3VDX LYS C 283 UNP P29715 LINKER
SEQADV 3VDX GLN C 284 UNP P29715 LINKER
SEQADV 3VDX LYS C 285 UNP P29715 LINKER
SEQADV 3VDX LEU C 448 UNP P03485 EXPRESSION TAG
SEQADV 3VDX GLU C 449 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS C 450 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS C 451 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS C 452 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS C 453 UNP P03485 EXPRESSION TAG
SEQADV 3VDX HIS C 454 UNP P03485 EXPRESSION TAG
SEQADV 3VDX 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 VAL 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 TYR
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 LEU 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 VAL 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 TYR
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 LEU 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 VAL 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 TYR
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 LEU 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 GLU A 40 5 6
HELIX 2 2 ARG A 41 GLY A 50 1 10
HELIX 3 3 ASP A 72 ASP A 88 1 17
HELIX 4 4 THR A 101 GLY A 112 1 12
HELIX 5 5 PRO A 141 ASP A 155 1 15
HELIX 6 6 ASP A 155 TYR A 168 1 14
HELIX 7 7 SER A 179 SER A 192 1 14
HELIX 8 8 PHE A 196 ALA A 201 1 6
HELIX 9 9 PRO A 202 TRP A 205 5 4
HELIX 10 10 PRO A 232 ASN A 235 5 4
HELIX 11 11 THR A 236 LEU A 244 1 9
HELIX 12 12 HIS A 263 LEU A 295 1 33
HELIX 13 13 PRO A 302 ALA A 316 1 15
HELIX 14 14 ASP A 321 THR A 331 1 11
HELIX 15 15 SER A 336 VAL A 351 1 16
HELIX 16 16 ARG A 361 GLY A 369 1 9
HELIX 17 17 LYS A 378 LYS A 387 1 10
HELIX 18 18 THR A 391 LEU A 400 1 10
HELIX 19 19 SER A 403 ARG A 417 1 15
HELIX 20 20 THR A 422 ILE A 437 1 16
HELIX 21 21 SER B 35 SER B 38 5 4
HELIX 22 22 TRP B 39 GLY B 50 1 12
HELIX 23 23 ASP B 72 LEU B 87 1 16
HELIX 24 24 GLY B 100 VAL B 108 1 9
HELIX 25 25 PRO B 141 ASP B 155 1 15
HELIX 26 26 ASP B 155 TYR B 168 1 14
HELIX 27 27 SER B 179 SER B 192 1 14
HELIX 28 28 ALA B 201 TRP B 205 5 5
HELIX 29 29 PRO B 232 ASN B 235 5 4
HELIX 30 30 THR B 236 LEU B 244 1 9
HELIX 31 31 HIS B 263 GLN B 284 1 22
HELIX 32 32 LEU B 286 ILE B 298 1 13
HELIX 33 33 PRO B 302 ALA B 316 1 15
HELIX 34 34 ASP B 321 LEU B 329 1 9
HELIX 35 35 SER B 336 VAL B 351 1 16
HELIX 36 36 ARG B 361 LEU B 367 1 7
HELIX 37 37 ASP B 372 LYS B 378 1 7
HELIX 38 38 LYS B 378 LYS B 387 1 10
HELIX 39 39 THR B 391 GLU B 397 1 7
HELIX 40 40 SER B 403 ILE B 414 1 12
HELIX 41 41 THR B 423 CYS B 434 1 12
HELIX 42 42 SER C 35 GLU C 40 5 6
HELIX 43 43 ARG C 41 GLY C 50 1 10
HELIX 44 44 ASP C 72 ASP C 88 1 17
HELIX 45 45 MET C 99 GLY C 112 1 14
HELIX 46 46 PRO C 141 ASP C 155 1 15
HELIX 47 47 ASP C 155 PHE C 164 1 10
HELIX 48 48 PHE C 164 ASN C 169 1 6
HELIX 49 49 ASN C 169 LEU C 174 1 6
HELIX 50 50 SER C 179 SER C 192 1 14
HELIX 51 51 GLY C 194 ALA C 201 1 8
HELIX 52 52 PRO C 202 TRP C 205 5 4
HELIX 53 53 ASP C 212 ILE C 216 5 5
HELIX 54 54 PRO C 232 ASN C 235 5 4
HELIX 55 55 THR C 236 LEU C 244 1 9
HELIX 56 56 HIS C 263 LEU C 279 1 17
HELIX 57 57 LEU C 279 GLN C 284 1 6
HELIX 58 58 GLN C 284 SER C 296 1 13
HELIX 59 59 GLY C 301 GLY C 317 1 17
HELIX 60 60 ASP C 321 THR C 331 1 11
HELIX 61 61 SER C 336 THR C 350 1 15
HELIX 62 62 ARG C 360 ASN C 365 1 6
HELIX 63 63 ASP C 372 LYS C 387 1 16
HELIX 64 64 THR C 391 SER C 399 1 9
HELIX 65 65 SER C 403 ASN C 416 1 14
HELIX 66 66 THR C 422 ILE C 437 1 16
SHEET 1 A 8 PHE A 2 GLU A 8 0
SHEET 2 A 8 THR A 11 HIS A 20 -1 O THR A 11 N GLU A 8
SHEET 3 A 8 TYR A 51 TYR A 56 -1 O THR A 55 N GLU A 18
SHEET 4 A 8 VAL A 24 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 95 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 LEU A 221 GLY A 225 1 O LEU A 221 N PHE A 121
SHEET 8 A 8 GLU A 248 VAL A 252 1 O VAL A 250 N ILE A 222
SHEET 1 B 8 PHE B 2 THR B 4 0
SHEET 2 B 8 ASP B 14 GLY B 21 -1 O LEU B 15 N ILE B 3
SHEET 3 B 8 ARG B 52 TYR B 56 -1 O THR B 55 N GLU B 18
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 95 N ILE B 29
SHEET 6 B 8 ILE B 116 LEU B 122 1 O ALA B 120 N LEU B 94
SHEET 7 B 8 LEU B 221 GLY B 225 1 O LEU B 221 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 THR C 4 0
SHEET 2 C 8 ASP C 14 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 95 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 221 N PHE C 121
SHEET 8 C 8 GLU C 248 VAL C 252 1 O GLU C 248 N ILE C 222
CISPEP 1 PHE A 32 PRO A 33 0 -6.06
CISPEP 2 GLU A 126 PRO A 127 0 -4.42
CISPEP 3 MET A 418 GLY A 419 0 0.97
CISPEP 4 GLY A 419 ALA A 420 0 2.51
CISPEP 5 ALA A 420 VAL A 421 0 0.33
CISPEP 6 PHE B 32 PRO B 33 0 -6.35
CISPEP 7 GLU B 126 PRO B 127 0 -3.06
CISPEP 8 PHE C 32 PRO C 33 0 -5.82
CISPEP 9 GLU C 126 PRO C 127 0 -3.21
CRYST1 122.590 127.710 204.220 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 0.008157 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007830 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004897 0.00000
TER 3384 ALA A 438
TER 6768 ALA B 438
TER 10152 ALA C 438
MASTER 352 0 0 66 24 0 0 610149 3 0 108
END |