| content |
HEADER TRANSPORT PROTEIN 02-JAN-20 6LNW
TITLE CRYSTAL STRUCTURE OF ACCESSORY SECRETORY PROTEIN 1,2 AND 3 IN
TITLE 2 STREPTOCOCCUS PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACCESSORY SECRETORY PROTEIN ASP1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ACCESSORY SECRETORY PROTEIN ASP2;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ACCESSORY SECRETORY PROTEIN ASP3;
COMPND 11 CHAIN: C;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE TIGR4;
SOURCE 3 ORGANISM_TAXID: 170187;
SOURCE 4 STRAIN: TIGR4;
SOURCE 5 GENE: SP_1762;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE TIGR4;
SOURCE 10 ORGANISM_TAXID: 170187;
SOURCE 11 STRAIN: TIGR4;
SOURCE 12 GENE: SP_1761;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE TIGR4;
SOURCE 17 ORGANISM_TAXID: 170187;
SOURCE 18 STRAIN: TIGR4;
SOURCE 19 GENE: SP_1760;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.GUO,Z.FENG,G.ZUO
REVDAT 2 25-MAR-20 6LNW 1 JRNL
REVDAT 1 26-FEB-20 6LNW 0
JRNL AUTH C.GUO,Z.FENG,G.ZUO,Y.L.JIANG,C.Z.ZHOU,Y.CHEN,W.T.HOU
JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHTS INTO THE ASP1/2/3 COMPLEX
JRNL TITL 2 MEDIATED SECRETION OF PNEUMOCOCCAL SERINE-RICH REPEAT
JRNL TITL 3 PROTEIN PSRP.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 524 784 2020
JRNL REFN ESSN 1090-2104
JRNL PMID 32037091
JRNL DOI 10.1016/J.BBRC.2020.01.146
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25180
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1310
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1822
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6407
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 90
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.22000
REMARK 3 B22 (A**2) : -0.22000
REMARK 3 B33 (A**2) : 0.71000
REMARK 3 B12 (A**2) : -0.11000
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): 0.362
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.873
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6575 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5895 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8900 ; 1.298 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13675 ; 3.561 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 763 ; 6.802 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 359 ;37.204 ;24.234
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1132 ;17.997 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;26.075 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 941 ; 0.048 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7301 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1455 ; 0.005 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES :
REMARK 3 REFINED INDIVIDUALLY
REMARK 3
REMARK 3 SF FILE CONTAINS FRIEDEL PAIRS UNDER I/F_MINUS AND I/F_PLUS
REMARK 3 COLUMNS.
REMARK 4
REMARK 4 6LNW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1300015122.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-17
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26531
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5VAE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.0, 15% PEG 6000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.61700
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 131.23400
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 131.23400
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 65.61700
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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 ASN A 380
REMARK 465 ILE A 381
REMARK 465 GLN A 382
REMARK 465 SER A 383
REMARK 465 GLU A 384
REMARK 465 ASN A 385
REMARK 465 LEU A 386
REMARK 465 GLY A 387
REMARK 465 LYS A 388
REMARK 465 ALA A 389
REMARK 465 ILE A 390
REMARK 465 ASP A 391
REMARK 465 TYR A 392
REMARK 465 GLY A 393
REMARK 465 ASP A 394
REMARK 465 ALA A 395
REMARK 465 GLU A 396
REMARK 465 ASN A 397
REMARK 465 PRO A 398
REMARK 465 LEU A 399
REMARK 465 GLU A 400
REMARK 465 GLU A 401
REMARK 465 ASN A 402
REMARK 465 GLN A 403
REMARK 465 HIS A 404
REMARK 465 GLN A 405
REMARK 465 ASP A 406
REMARK 465 LEU A 407
REMARK 465 ARG A 408
REMARK 465 GLY A 525
REMARK 465 THR A 526
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 GLU B 4
REMARK 465 LEU B 5
REMARK 465 ASN B 6
REMARK 465 ILE B 7
REMARK 465 LEU B 8
REMARK 465 GLN B 9
REMARK 465 ILE B 10
REMARK 465 GLY B 11
REMARK 465 LEU B 12
REMARK 465 ALA B 13
REMARK 465 ASN B 14
REMARK 465 TRP B 15
REMARK 465 GLU B 16
REMARK 465 ASN B 17
REMARK 465 HIS B 18
REMARK 465 TYR B 19
REMARK 465 ASP B 20
REMARK 465 ILE B 21
REMARK 465 PRO B 22
REMARK 465 GLU B 23
REMARK 465 ASN B 24
REMARK 465 MET B 25
REMARK 465 SER B 26
REMARK 465 TRP B 27
REMARK 465 TYR B 28
REMARK 465 TYR B 29
REMARK 465 PHE B 30
REMARK 465 TYR B 31
REMARK 465 PRO B 32
REMARK 465 ASN B 33
REMARK 465 SER B 34
REMARK 465 SER B 35
REMARK 465 LYS B 36
REMARK 465 ALA B 37
REMARK 465 LEU B 38
REMARK 465 ARG B 39
REMARK 465 GLU B 40
REMARK 465 ILE B 41
REMARK 465 ILE B 42
REMARK 465 GLU B 43
REMARK 465 LYS B 44
REMARK 465 GLU B 45
REMARK 465 ASP B 46
REMARK 465 ILE B 47
REMARK 465 ASN B 48
REMARK 465 ARG B 49
REMARK 465 PHE B 50
REMARK 465 HIS B 51
REMARK 465 ALA B 52
REMARK 465 VAL B 53
REMARK 465 LEU B 54
REMARK 465 ILE B 55
REMARK 465 GLU B 56
REMARK 465 ASP B 57
REMARK 465 GLY B 58
REMARK 465 GLN B 59
REMARK 465 TYR B 60
REMARK 465 SER B 61
REMARK 465 ARG B 62
REMARK 465 ASP B 63
REMARK 465 LEU B 64
REMARK 465 PHE B 65
REMARK 465 SER B 66
REMARK 465 TYR B 67
REMARK 465 VAL B 68
REMARK 465 LYS B 69
REMARK 465 TYR B 70
REMARK 465 PHE B 71
REMARK 465 GLU B 72
REMARK 465 PRO B 73
REMARK 465 TYR B 74
REMARK 465 THR B 75
REMARK 465 LEU B 76
REMARK 465 PHE B 77
REMARK 465 TYR B 78
REMARK 465 ASN B 79
REMARK 465 GLN B 80
REMARK 465 ASN B 81
REMARK 465 LEU B 82
REMARK 465 GLN B 83
REMARK 465 ILE B 84
REMARK 465 ASN B 85
REMARK 465 ASP B 86
REMARK 465 ARG B 87
REMARK 465 GLU B 88
REMARK 465 VAL B 89
REMARK 465 VAL B 90
REMARK 465 ASP B 91
REMARK 465 PHE B 92
REMARK 465 LEU B 93
REMARK 465 LYS B 94
REMARK 465 LYS B 95
REMARK 465 ARG B 96
REMARK 465 CYS B 97
REMARK 465 ALA B 98
REMARK 465 GLN B 99
REMARK 465 ALA B 100
REMARK 465 ILE B 101
REMARK 465 ASP B 102
REMARK 465 PHE B 103
REMARK 465 LEU B 104
REMARK 465 SER B 105
REMARK 465 PRO B 106
REMARK 465 GLN B 107
REMARK 465 GLN B 108
REMARK 465 LEU B 109
REMARK 465 ILE B 110
REMARK 465 ASN B 111
REMARK 465 ASP B 112
REMARK 465 LEU B 113
REMARK 465 SER B 114
REMARK 465 LYS B 115
REMARK 465 SER B 116
REMARK 465 LEU B 117
REMARK 465 PHE B 118
REMARK 465 GLY B 119
REMARK 465 GLY B 120
REMARK 465 GLY B 121
REMARK 465 TYR B 122
REMARK 465 GLY B 123
REMARK 465 ASP B 124
REMARK 465 SER B 254
REMARK 465 ARG B 255
REMARK 465 LYS B 256
REMARK 465 GLN B 257
REMARK 465 PHE B 258
REMARK 465 GLY B 259
REMARK 465 LYS B 260
REMARK 465 PHE B 261
REMARK 465 VAL B 262
REMARK 465 LEU B 263
REMARK 465 GLY B 264
REMARK 465 GLY B 265
REMARK 465 ASN B 266
REMARK 465 ILE B 267
REMARK 465 LEU B 268
REMARK 465 HIS B 269
REMARK 465 ASP B 270
REMARK 465 SER B 271
REMARK 465 LYS B 272
REMARK 465 ARG B 273
REMARK 465 ASP B 274
REMARK 465 GLU B 275
REMARK 465 ILE B 276
REMARK 465 ASN B 277
REMARK 465 TYR B 278
REMARK 465 PHE B 279
REMARK 465 PHE B 280
REMARK 465 HIS B 281
REMARK 465 PRO B 282
REMARK 465 GLY B 283
REMARK 465 ASP B 284
REMARK 465 PHE B 285
REMARK 465 LYS B 286
REMARK 465 PRO B 287
REMARK 465 PRO B 288
REMARK 465 LEU B 289
REMARK 465 THR B 290
REMARK 465 VAL B 291
REMARK 465 TYR B 292
REMARK 465 PHE B 293
REMARK 465 ALA B 294
REMARK 465 GLY B 295
REMARK 465 TYR B 296
REMARK 465 ARG B 297
REMARK 465 PRO B 298
REMARK 465 ALA B 299
REMARK 465 GLU B 300
REMARK 465 GLY B 301
REMARK 465 PHE B 302
REMARK 465 GLU B 303
REMARK 465 GLY B 304
REMARK 465 TYR B 305
REMARK 465 PHE B 306
REMARK 465 MET B 307
REMARK 465 MET B 308
REMARK 465 LYS B 309
REMARK 465 THR B 310
REMARK 465 LEU B 311
REMARK 465 GLY B 312
REMARK 465 CYS B 313
REMARK 465 PRO B 314
REMARK 465 PHE B 315
REMARK 465 ILE B 316
REMARK 465 LEU B 317
REMARK 465 PHE B 318
REMARK 465 SER B 319
REMARK 465 ASP B 320
REMARK 465 PRO B 321
REMARK 465 ARG B 322
REMARK 465 LEU B 323
REMARK 465 GLU B 324
REMARK 465 GLY B 325
REMARK 465 GLY B 326
REMARK 465 ALA B 327
REMARK 465 PHE B 328
REMARK 465 TYR B 329
REMARK 465 LEU B 330
REMARK 465 GLY B 331
REMARK 465 THR B 332
REMARK 465 ASP B 333
REMARK 465 GLU B 334
REMARK 465 LEU B 335
REMARK 465 GLU B 336
REMARK 465 GLY B 337
REMARK 465 LYS B 338
REMARK 465 VAL B 339
REMARK 465 LYS B 340
REMARK 465 ASP B 341
REMARK 465 THR B 342
REMARK 465 ILE B 343
REMARK 465 THR B 344
REMARK 465 HIS B 345
REMARK 465 TYR B 346
REMARK 465 LEU B 347
REMARK 465 ASP B 348
REMARK 465 TYR B 349
REMARK 465 LEU B 350
REMARK 465 GLY B 351
REMARK 465 PHE B 352
REMARK 465 ASP B 353
REMARK 465 HIS B 354
REMARK 465 LYS B 355
REMARK 465 ASP B 356
REMARK 465 LEU B 357
REMARK 465 ILE B 358
REMARK 465 LEU B 359
REMARK 465 SER B 360
REMARK 465 GLY B 361
REMARK 465 LEU B 362
REMARK 465 SER B 363
REMARK 465 MET B 364
REMARK 465 GLY B 365
REMARK 465 THR B 366
REMARK 465 PHE B 367
REMARK 465 PRO B 368
REMARK 465 ALA B 369
REMARK 465 LEU B 370
REMARK 465 TYR B 371
REMARK 465 TYR B 372
REMARK 465 GLY B 373
REMARK 465 ALA B 374
REMARK 465 SER B 375
REMARK 465 PHE B 376
REMARK 465 GLU B 377
REMARK 465 PRO B 378
REMARK 465 HIS B 379
REMARK 465 ALA B 380
REMARK 465 ILE B 381
REMARK 465 ILE B 382
REMARK 465 VAL B 383
REMARK 465 GLY B 384
REMARK 465 LYS B 385
REMARK 465 PRO B 386
REMARK 465 LEU B 387
REMARK 465 ALA B 388
REMARK 465 ASN B 389
REMARK 465 LEU B 390
REMARK 465 GLY B 391
REMARK 465 THR B 392
REMARK 465 ILE B 393
REMARK 465 ALA B 394
REMARK 465 SER B 395
REMARK 465 ARG B 396
REMARK 465 GLY B 397
REMARK 465 ARG B 398
REMARK 465 LEU B 399
REMARK 465 ASP B 400
REMARK 465 ALA B 401
REMARK 465 PRO B 402
REMARK 465 GLY B 403
REMARK 465 VAL B 404
REMARK 465 SER B 405
REMARK 465 ASN B 406
REMARK 465 LEU B 407
REMARK 465 ALA B 408
REMARK 465 PHE B 409
REMARK 465 ASP B 410
REMARK 465 CYS B 411
REMARK 465 LEU B 412
REMARK 465 ILE B 413
REMARK 465 HIS B 414
REMARK 465 HIS B 415
REMARK 465 THR B 416
REMARK 465 GLY B 417
REMARK 465 GLY B 418
REMARK 465 THR B 419
REMARK 465 SER B 420
REMARK 465 SER B 421
REMARK 465 GLN B 422
REMARK 465 ASP B 423
REMARK 465 MET B 424
REMARK 465 THR B 425
REMARK 465 GLU B 426
REMARK 465 LEU B 427
REMARK 465 ASP B 428
REMARK 465 GLN B 429
REMARK 465 ARG B 430
REMARK 465 PHE B 431
REMARK 465 TRP B 432
REMARK 465 LYS B 433
REMARK 465 ILE B 434
REMARK 465 PHE B 435
REMARK 465 LYS B 436
REMARK 465 GLN B 437
REMARK 465 ALA B 438
REMARK 465 ASN B 439
REMARK 465 PHE B 440
REMARK 465 SER B 441
REMARK 465 LYS B 442
REMARK 465 THR B 443
REMARK 465 THR B 444
REMARK 465 PHE B 445
REMARK 465 GLY B 446
REMARK 465 LEU B 447
REMARK 465 SER B 448
REMARK 465 TYR B 449
REMARK 465 MET B 450
REMARK 465 LYS B 451
REMARK 465 ASP B 452
REMARK 465 GLU B 453
REMARK 465 GLU B 454
REMARK 465 MET B 455
REMARK 465 ASP B 456
REMARK 465 PRO B 457
REMARK 465 GLN B 458
REMARK 465 ALA B 459
REMARK 465 TYR B 460
REMARK 465 GLU B 461
REMARK 465 GLN B 462
REMARK 465 LEU B 463
REMARK 465 VAL B 464
REMARK 465 SER B 465
REMARK 465 TYR B 466
REMARK 465 LEU B 467
REMARK 465 CYS B 468
REMARK 465 ASN B 469
REMARK 465 THR B 470
REMARK 465 GLY B 471
REMARK 465 ALA B 472
REMARK 465 LYS B 473
REMARK 465 ILE B 474
REMARK 465 LEU B 475
REMARK 465 SER B 476
REMARK 465 LYS B 477
REMARK 465 GLY B 478
REMARK 465 THR B 479
REMARK 465 ALA B 480
REMARK 465 GLY B 481
REMARK 465 ARG B 482
REMARK 465 HIS B 483
REMARK 465 ASN B 484
REMARK 465 ASP B 485
REMARK 465 ASP B 486
REMARK 465 THR B 487
REMARK 465 ASP B 488
REMARK 465 THR B 489
REMARK 465 ASN B 490
REMARK 465 ILE B 491
REMARK 465 SER B 492
REMARK 465 TRP B 493
REMARK 465 PHE B 494
REMARK 465 LEU B 495
REMARK 465 HIS B 496
REMARK 465 PHE B 497
REMARK 465 TYR B 498
REMARK 465 ARG B 499
REMARK 465 MET B 500
REMARK 465 VAL B 501
REMARK 465 LEU B 502
REMARK 465 GLU B 503
REMARK 465 THR B 504
REMARK 465 GLY B 505
REMARK 465 PHE B 506
REMARK 465 GLY B 507
REMARK 465 ARG B 508
REMARK 465 GLU B 509
REMARK 465 LYS B 510
REMARK 465 ARG B 511
REMARK 465 MET C 1
REMARK 465 SER C 145
REMARK 465 VAL C 146
REMARK 465 LEU C 147
REMARK 465 GLU C 148
REMARK 465 HIS C 149
REMARK 465 HIS C 150
REMARK 465 HIS C 151
REMARK 465 HIS C 152
REMARK 465 HIS C 153
REMARK 465 HIS C 154
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 ALA A 7 60.79 -104.53
REMARK 500 HIS A 144 -61.02 -102.23
REMARK 500 GLU A 186 138.75 -34.92
REMARK 500 ARG A 260 -39.80 -135.26
REMARK 500 LEU A 464 -0.11 71.50
REMARK 500 ASN A 466 27.86 -143.03
REMARK 500 GLU A 475 4.34 -68.65
REMARK 500 ASP A 485 -74.10 -60.82
REMARK 500 SER B 225 156.77 -48.85
REMARK 500 ASN C 36 94.69 -161.51
REMARK 500 LEU C 38 38.03 -75.76
REMARK 500 GLU C 101 137.22 -176.27
REMARK 500 TYR C 119 -37.52 -137.64
REMARK 500 ALA C 128 41.72 -143.39
REMARK 500 TYR C 136 -62.36 -92.39
REMARK 500 HIS C 137 171.01 179.94
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 6LNW A 1 526 UNP A0A0H2UR88_STRPN
DBREF2 6LNW A A0A0H2UR88 1 526
DBREF1 6LNW B 1 511 UNP A0A0H2URA6_STRPN
DBREF2 6LNW B A0A0H2URA6 1 511
DBREF1 6LNW C 1 146 UNP A0A0H2URJ0_STRPN
DBREF2 6LNW C A0A0H2URJ0 1 146
SEQADV 6LNW LEU C 147 UNP A0A0H2URJ EXPRESSION TAG
SEQADV 6LNW GLU C 148 UNP A0A0H2URJ EXPRESSION TAG
SEQADV 6LNW HIS C 149 UNP A0A0H2URJ EXPRESSION TAG
SEQADV 6LNW HIS C 150 UNP A0A0H2URJ EXPRESSION TAG
SEQADV 6LNW HIS C 151 UNP A0A0H2URJ EXPRESSION TAG
SEQADV 6LNW HIS C 152 UNP A0A0H2URJ EXPRESSION TAG
SEQADV 6LNW HIS C 153 UNP A0A0H2URJ EXPRESSION TAG
SEQADV 6LNW HIS C 154 UNP A0A0H2URJ EXPRESSION TAG
SEQRES 1 A 526 MET TYR TYR PHE ILE PRO ALA TRP TYR GLY SER GLU ARG
SEQRES 2 A 526 THR TRP HIS ALA ASP ILE THR PRO TRP TYR PHE SER HIS
SEQRES 3 A 526 PHE ARG LEU GLU PHE ASP ASP THR PHE HIS GLN ILE ARG
SEQRES 4 A 526 LEU PHE GLN GLU GLN ASP ILE ASP SER ARG LEU LEU VAL
SEQRES 5 A 526 LEU ALA TYR GLN PRO HIS LEU ARG TYR PHE LEU TYR ARG
SEQRES 6 A 526 HIS GLY VAL LEU GLU MET ASP THR TYR SER VAL PHE ASP
SEQRES 7 A 526 VAL MET GLN ASP PHE HIS ASN LEU HIS THR GLN VAL LEU
SEQRES 8 A 526 SER ILE ARG ASP ILE GLU TRP ASP ASP ASP CYS GLU PHE
SEQRES 9 A 526 ILE TYR SER PRO PHE THR ILE ILE VAL GLN LYS ASN GLY
SEQRES 10 A 526 LYS LYS PHE ALA LYS VAL GLU HIS GLY VAL GLU GLY PHE
SEQRES 11 A 526 ILE SER ASP ILE GLN TYR PHE GLU PRO ASN GLY GLN ILE
SEQRES 12 A 526 HIS MET HIS HIS ILE VAL ASP ASP ARG GLY PHE VAL SER
SEQRES 13 A 526 SER ILE ILE PHE PHE GLU ASP GLY GLN ALA ALA TYR GLN
SEQRES 14 A 526 GLU TYR LEU ASN LEU LYS GLY GLU TRP GLN PHE ARG GLU
SEQRES 15 A 526 ARG LEU LYS GLU GLY GLY GLN VAL GLU VAL ASN PRO ILE
SEQRES 16 A 526 LEU GLY TYR ARG PHE LYS MET LEU THR TYR GLN ASN MET
SEQRES 17 A 526 GLY ASP LEU VAL ALA GLU PHE PHE GLU ASN TYR LEU GLN
SEQRES 18 A 526 THR TYR VAL LYS ASP GLN ASP ILE PHE MET LEU PRO SER
SEQRES 19 A 526 HIS SER HIS HIS ASP GLN LEU VAL LEU ASP ARG LEU PRO
SEQRES 20 A 526 SER THR ASN PRO LYS LEU LEU SER LEU PHE ILE GLY ARG
SEQRES 21 A 526 ASN PRO GLN ASP THR PHE ARG ASP LEU ASP VAL THR PHE
SEQRES 22 A 526 GLU LYS SER ASP LEU ILE LEU VAL ASP ARG GLU ASP SER
SEQRES 23 A 526 LEU ARG LEU LEU GLN GLU LEU TYR PRO GLU ARG MET HIS
SEQRES 24 A 526 GLN CYS TYR HIS LEU SER SER PHE ASP THR ARG LEU ARG
SEQRES 25 A 526 LEU GLY ARG SER GLN THR LYS LYS GLU SER ILE ILE TYR
SEQRES 26 A 526 PHE GLN LEU ASP PHE GLU GLN GLY ILE ASP ASN GLN ALA
SEQRES 27 A 526 LEU LEU GLN VAL LEU SER PHE VAL ALA GLU ASN LYS ASP
SEQRES 28 A 526 THR GLU VAL ILE PHE GLY ALA PHE ALA ALA SER GLN GLU
SEQRES 29 A 526 GLN MET ASN GLU VAL GLU GLY ILE VAL GLU SER PHE ILE
SEQRES 30 A 526 GLN GLU ASN ILE GLN SER GLU ASN LEU GLY LYS ALA ILE
SEQRES 31 A 526 ASP TYR GLY ASP ALA GLU ASN PRO LEU GLU GLU ASN GLN
SEQRES 32 A 526 HIS GLN ASP LEU ARG LEU GLN PHE VAL ASN LEU ASN ASP
SEQRES 33 A 526 GLU LEU ASP LEU ILE LYS THR LEU GLU PHE VAL ARG LEU
SEQRES 34 A 526 ILE VAL ASP LEU ASN ARG HIS PRO HIS LEU TYR THR GLN
SEQRES 35 A 526 ILE ALA GLY ILE SER ALA GLY ILE PRO GLN ILE ASN LEU
SEQRES 36 A 526 VAL GLU THR VAL TYR VAL GLU HIS LEU LYS ASN GLY TYR
SEQRES 37 A 526 LEU LEU ALA ASP VAL THR GLU PHE SER LYS ALA ALA HIS
SEQRES 38 A 526 TYR TYR THR ASP ARG LEU LYS GLU TRP ASN GLU SER LEU
SEQRES 39 A 526 ILE TYR SER ILE ASP LYS ILE LYS GLU HIS THR GLY GLN
SEQRES 40 A 526 GLN PHE LEU GLY LYS LEU GLU LYS TRP ILE GLU GLU VAL
SEQRES 41 A 526 LYS ASN VAL LYS GLY THR
SEQRES 1 B 511 MET SER LYS GLU LEU ASN ILE LEU GLN ILE GLY LEU ALA
SEQRES 2 B 511 ASN TRP GLU ASN HIS TYR ASP ILE PRO GLU ASN MET SER
SEQRES 3 B 511 TRP TYR TYR PHE TYR PRO ASN SER SER LYS ALA LEU ARG
SEQRES 4 B 511 GLU ILE ILE GLU LYS GLU ASP ILE ASN ARG PHE HIS ALA
SEQRES 5 B 511 VAL LEU ILE GLU ASP GLY GLN TYR SER ARG ASP LEU PHE
SEQRES 6 B 511 SER TYR VAL LYS TYR PHE GLU PRO TYR THR LEU PHE TYR
SEQRES 7 B 511 ASN GLN ASN LEU GLN ILE ASN ASP ARG GLU VAL VAL ASP
SEQRES 8 B 511 PHE LEU LYS LYS ARG CYS ALA GLN ALA ILE ASP PHE LEU
SEQRES 9 B 511 SER PRO GLN GLN LEU ILE ASN ASP LEU SER LYS SER LEU
SEQRES 10 B 511 PHE GLY GLY GLY TYR GLY ASP LYS LEU PHE PRO PRO THR
SEQRES 11 B 511 ILE GLN VAL ASN PRO ASN PHE THR GLY ALA ILE SER TYR
SEQRES 12 B 511 GLN GLY LEU ASP TYR VAL SER LEU GLU GLY GLU PHE GLY
SEQRES 13 B 511 GLN ASP PHE ALA GLN LEU ALA TYR TRP ALA TYR ASN ILE
SEQRES 14 B 511 MET VAL GLN LYS THR LEU PRO ILE GLU LEU TRP LEU GLU
SEQRES 15 B 511 TYR GLU LYS GLU GLY ASN CYS ASP PHE ARG LEU VAL ILE
SEQRES 16 B 511 ARG LYS MET TRP SER GLY SER VAL ASP ASP PHE PHE GLU
SEQRES 17 B 511 GLU VAL ILE VAL SER GLU LYS ASP LEU GLU GLN ALA LEU
SEQRES 18 B 511 PHE MET ASP SER ARG ASP GLY ASP TYR PHE LEU SER ILE
SEQRES 19 B 511 SER VAL GLU ALA ARG GLY ARG GLY THR ILE LYS LEU GLY
SEQRES 20 B 511 ASN LEU HIS GLN ARG TRP SER ARG LYS GLN PHE GLY LYS
SEQRES 21 B 511 PHE VAL LEU GLY GLY ASN ILE LEU HIS ASP SER LYS ARG
SEQRES 22 B 511 ASP GLU ILE ASN TYR PHE PHE HIS PRO GLY ASP PHE LYS
SEQRES 23 B 511 PRO PRO LEU THR VAL TYR PHE ALA GLY TYR ARG PRO ALA
SEQRES 24 B 511 GLU GLY PHE GLU GLY TYR PHE MET MET LYS THR LEU GLY
SEQRES 25 B 511 CYS PRO PHE ILE LEU PHE SER ASP PRO ARG LEU GLU GLY
SEQRES 26 B 511 GLY ALA PHE TYR LEU GLY THR ASP GLU LEU GLU GLY LYS
SEQRES 27 B 511 VAL LYS ASP THR ILE THR HIS TYR LEU ASP TYR LEU GLY
SEQRES 28 B 511 PHE ASP HIS LYS ASP LEU ILE LEU SER GLY LEU SER MET
SEQRES 29 B 511 GLY THR PHE PRO ALA LEU TYR TYR GLY ALA SER PHE GLU
SEQRES 30 B 511 PRO HIS ALA ILE ILE VAL GLY LYS PRO LEU ALA ASN LEU
SEQRES 31 B 511 GLY THR ILE ALA SER ARG GLY ARG LEU ASP ALA PRO GLY
SEQRES 32 B 511 VAL SER ASN LEU ALA PHE ASP CYS LEU ILE HIS HIS THR
SEQRES 33 B 511 GLY GLY THR SER SER GLN ASP MET THR GLU LEU ASP GLN
SEQRES 34 B 511 ARG PHE TRP LYS ILE PHE LYS GLN ALA ASN PHE SER LYS
SEQRES 35 B 511 THR THR PHE GLY LEU SER TYR MET LYS ASP GLU GLU MET
SEQRES 36 B 511 ASP PRO GLN ALA TYR GLU GLN LEU VAL SER TYR LEU CYS
SEQRES 37 B 511 ASN THR GLY ALA LYS ILE LEU SER LYS GLY THR ALA GLY
SEQRES 38 B 511 ARG HIS ASN ASP ASP THR ASP THR ASN ILE SER TRP PHE
SEQRES 39 B 511 LEU HIS PHE TYR ARG MET VAL LEU GLU THR GLY PHE GLY
SEQRES 40 B 511 ARG GLU LYS ARG
SEQRES 1 C 154 MET ILE ILE THR GLN ARG GLN SER ILE HIS TRP GLY GLU
SEQRES 2 C 154 VAL GLY GLY THR TYR MET TYR GLY THR THR VAL SER TYR
SEQRES 3 C 154 TYR PRO ASP LYS SER VAL ARG LEU TYR ASN PRO LEU LEU
SEQRES 4 C 154 PRO SER GLY GLU ILE LEU LYS THR TRP PHE SER SER VAL
SEQRES 5 C 154 ASN TYR GLN ALA ALA ARG THR GLN PRO GLN LEU PRO LEU
SEQRES 6 C 154 LEU LYS ARG LYS GLN GLU TYR GLN LEU SER LEU VAL PHE
SEQRES 7 C 154 ASP CYS GLN PRO GLU ASN GLY VAL TYR THR LYS ILE THR
SEQRES 8 C 154 PHE PHE ASP ARG TYR GLY ASP ILE LEU GLU LYS LYS VAL
SEQRES 9 C 154 GLU LYS VAL LYS ASP PHE ILE PHE THR TYR PRO GLU ASP
SEQRES 10 C 154 SER TYR THR TYR ARG VAL SER LEU LEU SER ALA GLY PHE
SEQRES 11 C 154 GLU SER LEU THR PHE TYR HIS PHE SER ILE LYS GLU ILE
SEQRES 12 C 154 ARG SER VAL LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 4 HOH *90(H2 O)
HELIX 1 AA1 ASP A 32 GLN A 44 1 13
HELIX 2 AA2 HIS A 58 HIS A 66 1 9
HELIX 3 AA3 VAL A 76 GLN A 81 1 6
HELIX 4 AA4 SER A 92 ILE A 96 5 5
HELIX 5 AA5 PRO A 194 PHE A 200 5 7
HELIX 6 AA6 ASN A 207 VAL A 224 1 18
HELIX 7 AA7 HIS A 235 ASP A 244 1 10
HELIX 8 AA8 PRO A 262 ASP A 268 5 7
HELIX 9 AA9 LEU A 269 LYS A 275 1 7
HELIX 10 AB1 ARG A 283 TYR A 294 1 12
HELIX 11 AB2 PRO A 295 MET A 298 5 4
HELIX 12 AB3 GLY A 314 LYS A 319 5 6
HELIX 13 AB4 ASP A 335 ASN A 349 1 15
HELIX 14 AB5 SER A 362 GLU A 379 1 18
HELIX 15 AB6 ASP A 416 LEU A 424 1 9
HELIX 16 AB7 HIS A 438 GLY A 449 1 12
HELIX 17 AB8 ASP A 472 THR A 474 5 3
HELIX 18 AB9 GLU A 475 ASP A 485 1 11
HELIX 19 AC1 LEU A 487 GLU A 503 1 17
HELIX 20 AC2 GLY A 506 LYS A 524 1 19
HELIX 21 AC3 PHE B 127 PRO B 129 5 3
HELIX 22 AC4 LYS B 215 GLN B 219 5 5
HELIX 23 AC5 ASN C 53 ARG C 58 1 6
SHEET 1 AA1 7 THR A 73 SER A 75 0
SHEET 2 AA1 7 SER A 48 VAL A 52 1 N LEU A 50 O TYR A 74
SHEET 3 AA1 7 TYR A 2 PHE A 4 1 N PHE A 4 O LEU A 51
SHEET 4 AA1 7 ILE A 229 PRO A 233 1 O MET A 231 N TYR A 3
SHEET 5 AA1 7 LYS A 252 LEU A 256 1 O SER A 255 N LEU A 232
SHEET 6 AA1 7 LEU A 278 VAL A 281 1 O LEU A 280 N LEU A 254
SHEET 7 AA1 7 CYS A 301 HIS A 303 1 O TYR A 302 N VAL A 281
SHEET 1 AA210 GLU A 103 TYR A 106 0
SHEET 2 AA210 ILE A 111 LYS A 115 -1 O ILE A 112 N ILE A 105
SHEET 3 AA210 LYS A 118 HIS A 125 -1 O LYS A 118 N LYS A 115
SHEET 4 AA210 ILE A 131 PHE A 137 -1 O PHE A 137 N PHE A 120
SHEET 5 AA210 ILE A 143 ASP A 150 -1 O HIS A 144 N TYR A 136
SHEET 6 AA210 PHE A 154 GLU A 162 -1 O PHE A 154 N ASP A 150
SHEET 7 AA210 GLN A 165 LEU A 172 -1 O TYR A 168 N PHE A 160
SHEET 8 AA210 TRP A 178 ARG A 183 -1 O GLN A 179 N TYR A 171
SHEET 9 AA210 VAL A 190 VAL A 192 -1 O GLU A 191 N ARG A 181
SHEET 10 AA210 THR A 204 TYR A 205 -1 O TYR A 205 N VAL A 190
SHEET 1 AA3 6 GLN A 410 LEU A 414 0
SHEET 2 AA3 6 THR A 352 PHE A 359 1 N PHE A 356 O GLN A 410
SHEET 3 AA3 6 SER A 322 GLN A 327 1 N ILE A 324 O ILE A 355
SHEET 4 AA3 6 VAL A 427 ASP A 432 1 O VAL A 431 N TYR A 325
SHEET 5 AA3 6 GLN A 452 ASN A 454 1 O ILE A 453 N ASP A 432
SHEET 6 AA3 6 GLY A 467 LEU A 469 1 O TYR A 468 N GLN A 452
SHEET 1 AA4 8 ILE B 131 VAL B 133 0
SHEET 2 AA4 8 TYR B 148 TRP B 165 -1 O TYR B 164 N GLN B 132
SHEET 3 AA4 8 ALA B 140 GLN B 144 -1 N SER B 142 O SER B 150
SHEET 4 AA4 8 THR C 23 TYR C 26 -1 O VAL C 24 N TYR B 143
SHEET 5 AA4 8 VAL C 32 TYR C 35 -1 O ARG C 33 N SER C 25
SHEET 6 AA4 8 LEU C 133 GLU C 142 -1 O PHE C 135 N VAL C 32
SHEET 7 AA4 8 GLU C 71 CYS C 80 -1 N GLN C 73 O LYS C 141
SHEET 8 AA4 8 ASP C 109 THR C 113 -1 O PHE C 112 N TYR C 72
SHEET 1 AA5 4 ILE B 169 VAL B 171 0
SHEET 2 AA5 4 TYR B 230 ARG B 252 -1 O LEU B 232 N ILE B 169
SHEET 3 AA5 4 ILE B 177 GLU B 186 -1 N TRP B 180 O HIS B 250
SHEET 4 AA5 4 LEU B 221 MET B 223 -1 O MET B 223 N ILE B 177
SHEET 1 AA6 5 GLU B 208 VAL B 212 0
SHEET 2 AA6 5 CYS B 189 TRP B 199 -1 N ILE B 195 O VAL B 210
SHEET 3 AA6 5 TYR B 230 ARG B 252 -1 O PHE B 231 N MET B 198
SHEET 4 AA6 5 TYR B 148 TRP B 165 -1 N LEU B 162 O VAL B 236
SHEET 5 AA6 5 ILE B 131 VAL B 133 -1 N GLN B 132 O TYR B 164
SHEET 1 AA7 4 ILE C 44 PHE C 49 0
SHEET 2 AA7 4 THR C 120 SER C 127 -1 O VAL C 123 N TRP C 48
SHEET 3 AA7 4 VAL C 86 PHE C 93 -1 N TYR C 87 O LEU C 126
SHEET 4 AA7 4 ILE C 99 GLU C 105 -1 O GLU C 105 N THR C 88
CRYST1 101.158 101.158 196.851 90.00 90.00 120.00 P 31 2 1 6
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 0.009886 0.005707 0.000000 0.00000
SCALE2 0.000000 0.011415 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005080 0.00000
TER 4156 LYS A 524
TER 5216 TRP B 253
TER 6410 ARG C 144
MASTER 715 0 0 23 44 0 0 6 6497 3 0 93
END |