HEADER VIRAL PROTEIN 17-MAR-17 5NGJ
TITLE CRYSTAL STRUCTURE OF PB6, MAJOR TAIL TUBE PROTEIN OF BACTERIOPHAGE T5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TAIL TUBE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TTP,TAIL PROTEIN PB6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA PHAGE T5;
SOURCE 3 ORGANISM_TAXID: 10726;
SOURCE 4 GENE: N4, ORF134, T5.145, T5P141;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS BACTERIOPHAGE, VIRAL PROTEIN, TUBE PROTEIN, VIRION PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-A.ARNAUD,G.EFFANTIN,C.VIVES,S.ENGILBERGE,M.BACIA,P.BOULANGER,
AUTHOR 2 E.GIRARD,G.SCHOEHN,C.BREYTON
REVDAT 2 16-OCT-19 5NGJ 1 REMARK
REVDAT 1 03-JAN-18 5NGJ 0
JRNL AUTH C.A.ARNAUD,G.EFFANTIN,C.VIVES,S.ENGILBERGE,M.BACIA,
JRNL AUTH 2 P.BOULANGER,E.GIRARD,G.SCHOEHN,C.BREYTON
JRNL TITL BACTERIOPHAGE T5 TAIL TUBE STRUCTURE SUGGESTS A TRIGGER
JRNL TITL 2 MECHANISM FOR SIPHOVIRIDAE DNA EJECTION.
JRNL REF NAT COMMUN V. 8 1953 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29209037
JRNL DOI 10.1038/S41467-017-02049-3
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 67990
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3399
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.26
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.80
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4943
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2465
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4696
REMARK 3 BIN R VALUE (WORKING SET) : 0.2451
REMARK 3 BIN FREE R VALUE : 0.2756
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 247
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6667
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.54
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.40640
REMARK 3 B22 (A**2) : -10.76470
REMARK 3 B33 (A**2) : 14.17110
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -7.10150
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.340
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.181
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.160
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.318
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.165
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 13407 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 24225 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2972 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 187 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1968 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 13407 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 984 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 14322 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.19
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.73
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.18
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8335 15.1346 54.1985
REMARK 3 T TENSOR
REMARK 3 T11: -0.0954 T22: -0.0371
REMARK 3 T33: -0.1920 T12: 0.0112
REMARK 3 T13: 0.0385 T23: -0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 0.8736 L22: 0.7899
REMARK 3 L33: 3.1967 L12: -0.2369
REMARK 3 L13: -1.1367 L23: 0.6295
REMARK 3 S TENSOR
REMARK 3 S11: 0.0038 S12: 0.0736 S13: 0.0718
REMARK 3 S21: -0.0248 S22: 0.0108 S23: 0.1041
REMARK 3 S31: -0.2008 S32: -0.1950 S33: -0.0146
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0476 31.9201 52.0983
REMARK 3 T TENSOR
REMARK 3 T11: -0.2113 T22: -0.0690
REMARK 3 T33: -0.1844 T12: 0.0553
REMARK 3 T13: 0.0050 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 1.3430 L22: 1.4509
REMARK 3 L33: 3.9436 L12: 0.3485
REMARK 3 L13: 0.6417 L23: 0.4107
REMARK 3 S TENSOR
REMARK 3 S11: -0.0563 S12: 0.0150 S13: 0.0298
REMARK 3 S21: 0.0207 S22: -0.0297 S23: 0.0331
REMARK 3 S31: 0.1971 S32: -0.0004 S33: 0.0860
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5NGJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004080.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97965
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68061
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 57.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % 3350 PEG, 0.2 M HEPES PH 7.5, 0.3
REMARK 280 M LISO4, 0.1 MM MGCL2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 57.54050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: 2050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 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 1
REMARK 465 SER A 2
REMARK 465 ASP A 39
REMARK 465 SER A 40
REMARK 465 ASN A 41
REMARK 465 SER A 42
REMARK 465 THR A 43
REMARK 465 ASP A 44
REMARK 465 ILE A 45
REMARK 465 THR A 46
REMARK 465 VAL A 47
REMARK 465 ASN A 48
REMARK 465 GLU A 49
REMARK 465 ALA A 50
REMARK 465 GLY A 51
REMARK 465 PRO A 52
REMARK 465 ARG A 53
REMARK 465 PRO A 54
REMARK 465 THR A 55
REMARK 465 ARG A 56
REMARK 465 GLY A 57
REMARK 465 SER A 58
REMARK 465 LYS A 59
REMARK 465 ARG A 60
REMARK 465 PHE A 61
REMARK 465 ASN A 62
REMARK 465 ASP A 63
REMARK 465 SER A 64
REMARK 465 LEU A 65
REMARK 465 ASN A 66
REMARK 465 GLY A 471
REMARK 465 HIS A 472
REMARK 465 HIS A 473
REMARK 465 HIS A 474
REMARK 465 HIS A 475
REMARK 465 HIS A 476
REMARK 465 HIS A 477
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LEU B 3
REMARK 465 GLN B 4
REMARK 465 LEU B 5
REMARK 465 LEU B 6
REMARK 465 GLN B 38
REMARK 465 ALA B 50
REMARK 465 GLY B 51
REMARK 465 PRO B 52
REMARK 465 ARG B 53
REMARK 465 PRO B 54
REMARK 465 THR B 55
REMARK 465 ARG B 56
REMARK 465 GLY B 57
REMARK 465 SER B 58
REMARK 465 LYS B 59
REMARK 465 ARG B 60
REMARK 465 PHE B 61
REMARK 465 ASN B 62
REMARK 465 ASP B 63
REMARK 465 SER B 64
REMARK 465 LEU B 65
REMARK 465 ASN B 66
REMARK 465 GLY B 438
REMARK 465 ALA B 439
REMARK 465 VAL B 440
REMARK 465 THR B 461
REMARK 465 ALA B 462
REMARK 465 GLY B 463
REMARK 465 GLY B 464
REMARK 465 GLU B 465
REMARK 465 ASN B 466
REMARK 465 LEU B 467
REMARK 465 TYR B 468
REMARK 465 PHE B 469
REMARK 465 GLN B 470
REMARK 465 GLY B 471
REMARK 465 HIS B 472
REMARK 465 HIS B 473
REMARK 465 HIS B 474
REMARK 465 HIS B 475
REMARK 465 HIS B 476
REMARK 465 HIS B 477
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 ASP B 39 CG OD1 OD2
REMARK 470 SER B 40 OG
REMARK 470 ASN B 41 CG OD1 ND2
REMARK 470 SER B 42 OG
REMARK 470 THR B 43 OG1 CG2
REMARK 470 ASP B 44 CG OD1 OD2
REMARK 470 ILE B 45 CG1 CG2 CD1
REMARK 470 THR B 46 OG1 CG2
REMARK 470 VAL B 47 CG1 CG2
REMARK 470 ASN B 48 CG OD1 ND2
REMARK 470 GLU B 49 CG CD OE1 OE2
REMARK 470 ALA B 67 N CA CB
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 SER A 149 74.79 60.51
REMARK 500 ASP A 163 49.68 -159.32
REMARK 500 ASN A 270 -178.12 -176.86
REMARK 500 SER A 393 -15.71 80.08
REMARK 500 ASN A 466 97.23 -68.48
REMARK 500 ASP B 32 87.46 -157.39
REMARK 500 ASP B 33 151.22 70.23
REMARK 500 SER B 40 50.49 -162.23
REMARK 500 ASN B 41 71.23 64.73
REMARK 500 VAL B 47 67.13 69.84
REMARK 500 SER B 149 74.16 59.55
REMARK 500 ASP B 163 50.62 -159.62
REMARK 500 VAL B 329 0.13 -156.17
REMARK 500 ALA B 384 97.38 -68.00
REMARK 500 ASN B 386 42.28 -147.95
REMARK 500 THR B 389 43.03 -84.76
REMARK 500 SER B 393 58.16 19.07
REMARK 500 ALA B 421 41.36 -155.26
REMARK 500 ASP B 448 -40.49 -17.40
REMARK 500 THR B 459 -70.78 -50.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 743 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH A 744 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH A 745 DISTANCE = 14.99 ANGSTROMS
REMARK 525 HOH B 583 DISTANCE = 8.44 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 505
DBREF 5NGJ A 1 464 UNP Q6QGE2 TUBE_BPT5 1 464
DBREF 5NGJ B 1 464 UNP Q6QGE2 TUBE_BPT5 1 464
SEQADV 5NGJ GLU A 465 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ ASN A 466 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ LEU A 467 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ TYR A 468 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ PHE A 469 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ GLN A 470 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ GLY A 471 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS A 472 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS A 473 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS A 474 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS A 475 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS A 476 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS A 477 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ GLU B 465 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ ASN B 466 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ LEU B 467 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ TYR B 468 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ PHE B 469 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ GLN B 470 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ GLY B 471 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS B 472 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS B 473 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS B 474 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS B 475 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS B 476 UNP Q6QGE2 EXPRESSION TAG
SEQADV 5NGJ HIS B 477 UNP Q6QGE2 EXPRESSION TAG
SEQRES 1 A 477 MET SER LEU GLN LEU LEU ARG ASN THR ARG ILE PHE VAL
SEQRES 2 A 477 SER THR VAL LYS THR GLY HIS ASN LYS THR ASN THR GLN
SEQRES 3 A 477 GLU ILE LEU VAL GLN ASP ASP ILE SER TRP GLY GLN ASP
SEQRES 4 A 477 SER ASN SER THR ASP ILE THR VAL ASN GLU ALA GLY PRO
SEQRES 5 A 477 ARG PRO THR ARG GLY SER LYS ARG PHE ASN ASP SER LEU
SEQRES 6 A 477 ASN ALA ALA GLU TRP SER PHE SER THR TYR ILE LEU PRO
SEQRES 7 A 477 TYR LYS ASP LYS ASN THR SER LYS GLN ILE VAL PRO ASP
SEQRES 8 A 477 TYR MET LEU TRP HIS ALA LEU SER SER GLY ARG ALA ILE
SEQRES 9 A 477 ASN LEU GLU GLY THR THR GLY ALA HIS ASN ASN ALA THR
SEQRES 10 A 477 ASN PHE MET VAL ASN PHE LYS ASP ASN SER TYR HIS GLU
SEQRES 11 A 477 LEU ALA MET LEU HIS ILE TYR ILE LEU THR ASP LYS THR
SEQRES 12 A 477 TRP SER TYR ILE ASP SER CYS GLN ILE ASN GLN ALA GLU
SEQRES 13 A 477 VAL ASN VAL ASP ILE GLU ASP ILE GLY ARG VAL THR TRP
SEQRES 14 A 477 SER GLY ASN GLY ASN GLN LEU ILE PRO LEU ASP GLU GLN
SEQRES 15 A 477 PRO PHE ASP PRO ASP GLN ILE GLY ILE ASP ASP GLU THR
SEQRES 16 A 477 TYR MET THR ILE GLN GLY SER TYR ILE LYS ASN LYS LEU
SEQRES 17 A 477 THR ILE LEU LYS ILE LYS ASP MET ASP THR ASN LYS SER
SEQRES 18 A 477 TYR ASP ILE PRO ILE THR GLY GLY THR PHE THR ILE ASN
SEQRES 19 A 477 ASN ASN ILE THR TYR LEU THR PRO ASN VAL MET SER ARG
SEQRES 20 A 477 VAL THR ILE PRO ILE GLY SER PHE THR GLY ALA PHE GLU
SEQRES 21 A 477 LEU THR GLY SER LEU THR ALA TYR LEU ASN ASP LYS SER
SEQRES 22 A 477 LEU GLY SER MET GLU LEU TYR LYS ASP LEU ILE LYS THR
SEQRES 23 A 477 LEU LYS VAL VAL ASN ARG PHE GLU ILE ALA LEU VAL LEU
SEQRES 24 A 477 GLY GLY GLU TYR ASP ASP GLU ARG PRO ALA ALA ILE LEU
SEQRES 25 A 477 VAL ALA LYS GLN ALA HIS VAL ASN ILE PRO THR ILE GLU
SEQRES 26 A 477 THR ASP ASP VAL LEU GLY THR SER VAL GLU PHE LYS ALA
SEQRES 27 A 477 ILE PRO SER ASP LEU ASP ALA GLY ASP GLU GLY TYR LEU
SEQRES 28 A 477 GLY PHE SER SER LYS TYR THR ARG THR THR ILE ASN ASN
SEQRES 29 A 477 LEU ILE VAL ASN GLY ASP GLY ALA THR ASP ALA VAL THR
SEQRES 30 A 477 ALA ILE THR VAL LYS SER ALA GLY ASN VAL THR THR LEU
SEQRES 31 A 477 ASN ARG SER ALA THR LEU GLN MET SER VAL GLU VAL THR
SEQRES 32 A 477 PRO SER SER ALA ARG ASN LYS GLU VAL THR TRP ALA ILE
SEQRES 33 A 477 THR ALA GLY ASP ALA ALA THR ILE ASN ALA THR GLY LEU
SEQRES 34 A 477 LEU ARG ALA ASP ALA SER LYS THR GLY ALA VAL THR VAL
SEQRES 35 A 477 GLU ALA THR ALA LYS ASP GLY SER GLY VAL LYS GLY THR
SEQRES 36 A 477 LYS VAL ILE THR VAL THR ALA GLY GLY GLU ASN LEU TYR
SEQRES 37 A 477 PHE GLN GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 477 MET SER LEU GLN LEU LEU ARG ASN THR ARG ILE PHE VAL
SEQRES 2 B 477 SER THR VAL LYS THR GLY HIS ASN LYS THR ASN THR GLN
SEQRES 3 B 477 GLU ILE LEU VAL GLN ASP ASP ILE SER TRP GLY GLN ASP
SEQRES 4 B 477 SER ASN SER THR ASP ILE THR VAL ASN GLU ALA GLY PRO
SEQRES 5 B 477 ARG PRO THR ARG GLY SER LYS ARG PHE ASN ASP SER LEU
SEQRES 6 B 477 ASN ALA ALA GLU TRP SER PHE SER THR TYR ILE LEU PRO
SEQRES 7 B 477 TYR LYS ASP LYS ASN THR SER LYS GLN ILE VAL PRO ASP
SEQRES 8 B 477 TYR MET LEU TRP HIS ALA LEU SER SER GLY ARG ALA ILE
SEQRES 9 B 477 ASN LEU GLU GLY THR THR GLY ALA HIS ASN ASN ALA THR
SEQRES 10 B 477 ASN PHE MET VAL ASN PHE LYS ASP ASN SER TYR HIS GLU
SEQRES 11 B 477 LEU ALA MET LEU HIS ILE TYR ILE LEU THR ASP LYS THR
SEQRES 12 B 477 TRP SER TYR ILE ASP SER CYS GLN ILE ASN GLN ALA GLU
SEQRES 13 B 477 VAL ASN VAL ASP ILE GLU ASP ILE GLY ARG VAL THR TRP
SEQRES 14 B 477 SER GLY ASN GLY ASN GLN LEU ILE PRO LEU ASP GLU GLN
SEQRES 15 B 477 PRO PHE ASP PRO ASP GLN ILE GLY ILE ASP ASP GLU THR
SEQRES 16 B 477 TYR MET THR ILE GLN GLY SER TYR ILE LYS ASN LYS LEU
SEQRES 17 B 477 THR ILE LEU LYS ILE LYS ASP MET ASP THR ASN LYS SER
SEQRES 18 B 477 TYR ASP ILE PRO ILE THR GLY GLY THR PHE THR ILE ASN
SEQRES 19 B 477 ASN ASN ILE THR TYR LEU THR PRO ASN VAL MET SER ARG
SEQRES 20 B 477 VAL THR ILE PRO ILE GLY SER PHE THR GLY ALA PHE GLU
SEQRES 21 B 477 LEU THR GLY SER LEU THR ALA TYR LEU ASN ASP LYS SER
SEQRES 22 B 477 LEU GLY SER MET GLU LEU TYR LYS ASP LEU ILE LYS THR
SEQRES 23 B 477 LEU LYS VAL VAL ASN ARG PHE GLU ILE ALA LEU VAL LEU
SEQRES 24 B 477 GLY GLY GLU TYR ASP ASP GLU ARG PRO ALA ALA ILE LEU
SEQRES 25 B 477 VAL ALA LYS GLN ALA HIS VAL ASN ILE PRO THR ILE GLU
SEQRES 26 B 477 THR ASP ASP VAL LEU GLY THR SER VAL GLU PHE LYS ALA
SEQRES 27 B 477 ILE PRO SER ASP LEU ASP ALA GLY ASP GLU GLY TYR LEU
SEQRES 28 B 477 GLY PHE SER SER LYS TYR THR ARG THR THR ILE ASN ASN
SEQRES 29 B 477 LEU ILE VAL ASN GLY ASP GLY ALA THR ASP ALA VAL THR
SEQRES 30 B 477 ALA ILE THR VAL LYS SER ALA GLY ASN VAL THR THR LEU
SEQRES 31 B 477 ASN ARG SER ALA THR LEU GLN MET SER VAL GLU VAL THR
SEQRES 32 B 477 PRO SER SER ALA ARG ASN LYS GLU VAL THR TRP ALA ILE
SEQRES 33 B 477 THR ALA GLY ASP ALA ALA THR ILE ASN ALA THR GLY LEU
SEQRES 34 B 477 LEU ARG ALA ASP ALA SER LYS THR GLY ALA VAL THR VAL
SEQRES 35 B 477 GLU ALA THR ALA LYS ASP GLY SER GLY VAL LYS GLY THR
SEQRES 36 B 477 LYS VAL ILE THR VAL THR ALA GLY GLY GLU ASN LEU TYR
SEQRES 37 B 477 PHE GLN GLY HIS HIS HIS HIS HIS HIS
HET CL A 501 1
HET CL A 502 1
HET CL A 503 1
HET CL A 504 1
HET CL A 505 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 5(CL 1-)
FORMUL 8 HOH *228(H2 O)
HELIX 1 AA1 ASP A 91 SER A 100 1 10
HELIX 2 AA2 ASP A 185 GLY A 190 1 6
HELIX 3 AA3 ASP A 192 GLY A 201 1 10
HELIX 4 AA4 ASN A 270 GLY A 275 1 6
HELIX 5 AA5 SER A 276 VAL A 290 1 15
HELIX 6 AA6 THR A 358 GLY A 369 1 12
HELIX 7 AA7 GLY A 385 VAL A 387 5 3
HELIX 8 AA8 ASP B 91 SER B 100 1 10
HELIX 9 AA9 ASP B 185 GLY B 190 1 6
HELIX 10 AB1 ASP B 192 GLY B 201 1 10
HELIX 11 AB2 ASN B 270 GLY B 275 1 6
HELIX 12 AB3 SER B 276 VAL B 290 1 15
HELIX 13 AB4 THR B 358 GLY B 369 1 12
HELIX 14 AB5 ALA B 432 LYS B 436 5 5
SHEET 1 A 5 THR A 25 ILE A 28 0
SHEET 2 A 5 THR A 9 SER A 14 -1
SHEET 3 A 5 HIS A 135 THR A 140 -1
SHEET 4 A 5 THR A 143 ASP A 148 -1
SHEET 5 A 5 GLN A 175 LEU A 179 -1
SHEET 1 B 8 ILE A 34 GLY A 37 0
SHEET 2 B 8 ALA A 68 TYR A 75 -1
SHEET 3 B 8 ARG A 166 GLY A 173 -1
SHEET 4 B 8 CYS A 150 ASN A 158 -1
SHEET 5 B 8 ILE A 226 ASN A 234 -1
SHEET 6 B 8 GLU A 260 ALA A 267 -1
SHEET 7 B 8 THR A 332 ALA A 338 -1
SHEET 8 B 8 ALA A 317 ASN A 320 -1
SHEET 1 C 2 PRO A 78 LYS A 80 0
SHEET 2 C 2 GLN A 87 VAL A 89 -1
SHEET 1 D 7 GLY A 111 ASN A 114 0
SHEET 2 D 7 PHE A 119 ASN A 122 -1
SHEET 3 D 7 TYR A 350 SER A 354 -1
SHEET 4 D 7 ALA A 309 ALA A 314 -1
SHEET 5 D 7 GLU A 294 LEU A 299 -1
SHEET 6 D 7 THR A 209 ASP A 215 -1
SHEET 7 D 7 LYS A 220 ILE A 226 -1
SHEET 1 E 2 ALA A 378 SER A 383 0
SHEET 2 E 2 MET A 398 THR A 403 -1
SHEET 1 F 4 THR A 389 ASN A 391 0
SHEET 2 F 4 LYS A 453 THR A 461 1
SHEET 3 F 4 GLY A 438 ALA A 446 -1
SHEET 4 F 4 VAL A 412 ALA A 418 -1
SHEET 1 G 3 THR A 395 GLN A 397 0
SHEET 2 G 3 LEU A 429 ALA A 432 -1
SHEET 3 G 3 ALA A 422 ILE A 424 -1
SHEET 1 H 5 THR B 25 ILE B 28 0
SHEET 2 H 5 THR B 9 SER B 14 -1
SHEET 3 H 5 HIS B 135 THR B 140 -1
SHEET 4 H 5 THR B 143 ASP B 148 -1
SHEET 5 H 5 GLN B 175 LEU B 179 -1
SHEET 1 I 8 SER B 35 GLY B 37 0
SHEET 2 I 8 ALA B 68 TYR B 75 -1
SHEET 3 I 8 ARG B 166 GLY B 173 -1
SHEET 4 I 8 GLN B 151 ASN B 158 -1
SHEET 5 I 8 ILE B 226 ASN B 234 -1
SHEET 6 I 8 GLU B 260 ALA B 267 -1
SHEET 7 I 8 THR B 332 ALA B 338 -1
SHEET 8 I 8 ALA B 317 ASN B 320 -1
SHEET 1 J 2 ASP B 44 THR B 46 0
SHEET 2 J 2 THR B 238 LEU B 240 1
SHEET 1 K 2 PRO B 78 LYS B 80 0
SHEET 2 K 2 GLN B 87 VAL B 89 -1
SHEET 1 L 7 GLY B 111 ASN B 114 0
SHEET 2 L 7 PHE B 119 ASN B 122 -1
SHEET 3 L 7 TYR B 350 SER B 354 -1
SHEET 4 L 7 ALA B 309 ALA B 314 -1
SHEET 5 L 7 GLU B 294 LEU B 299 -1
SHEET 6 L 7 THR B 209 ASP B 215 -1
SHEET 7 L 7 LYS B 220 ILE B 226 -1
SHEET 1 M 2 ALA B 378 LYS B 382 0
SHEET 2 M 2 SER B 399 THR B 403 -1
SHEET 1 N 3 VAL B 412 THR B 417 0
SHEET 2 N 3 THR B 441 ALA B 446 -1
SHEET 3 N 3 LYS B 453 LYS B 456 -1
CISPEP 1 THR A 403 PRO A 404 0 -9.47
CISPEP 2 THR B 403 PRO B 404 0 -8.31
SITE 1 AC1 5 ALA A 97 LEU A 131 ALA A 132 GLN A 151
SITE 2 AC1 5 ILE A 152
SITE 1 AC2 7 SER A 99 SER A 100 GLY A 111 ASN A 122
SITE 2 AC2 7 PHE A 123 LYS A 124 ASP A 125
SITE 1 AC3 2 THR A 388 THR A 389
SITE 1 AC4 1 GLY A 464
SITE 1 AC5 2 ARG A 102 ALA A 103
CRYST1 76.790 115.081 83.366 90.00 111.88 90.00 P 1 21 1 4
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 0.013023 0.000000 0.005230 0.00000
SCALE2 0.000000 0.008690 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012926 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
