HEADER VIRAL PROTEIN 17-MAY-99 1TOL
TITLE FUSION OF N-TERMINAL DOMAIN OF THE MINOR COAT PROTEIN FROM GENE III IN
TITLE 2 PHAGE M13, AND C-TERMINAL DOMAIN OF E. COLI PROTEIN-TOLA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (FUSION PROTEIN CONSISTING OF MINOR COAT PROTEIN,
COMPND 3 GLYCINE RICH LINKER, TOLA, AND A HIS TAG);
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: N-TERMINAL DOMAIN OF MINOR COAT PROTEIN AND C-TERMINAL
COMPND 6 DOMAIN OF TOLA;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: FUSION PROTEIN COMPRISES RESIDUES 1-86 OF MATURE MINOR
COMPND 9 COAT PROTEIN FROM GENE III, INCLUDING GLYCINE-RICH LINKER
COMPND 10 (GGGSEGGGSEGGGSEGGG), AND RESIDUES 295-421 OF TOLA, AND C-TERMINAL
COMPND 11 TAIL WITH SEQUENCE AAAHHHHHH
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE M13, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 10870, 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PTFT74;
SOURCE 8 OTHER_DETAILS: FUSION GENE
KEYWDS BACTERIOPHAGE M13, PHAGE INFECTION, TOL PATHWAY, FUSION PROTEIN,
KEYWDS 2 VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LUBKOWSKI,A.WLODAWER,F.HENNECKE,A.PLUECKTHUN
REVDAT 6 27-DEC-23 1TOL 1 REMARK
REVDAT 5 21-JUN-17 1TOL 1 DBREF DBREF1 DBREF2
REVDAT 4 24-FEB-09 1TOL 1 VERSN
REVDAT 3 01-APR-03 1TOL 1 JRNL
REVDAT 2 22-JUN-99 1TOL 1 JRNL
REVDAT 1 20-MAY-99 1TOL 0
JRNL AUTH J.LUBKOWSKI,F.HENNECKE,A.PLUCKTHUN,A.WLODAWER
JRNL TITL FILAMENTOUS PHAGE INFECTION: CRYSTAL STRUCTURE OF G3P IN
JRNL TITL 2 COMPLEX WITH ITS CORECEPTOR, THE C-TERMINAL DOMAIN OF TOLA.
JRNL REF STRUCTURE FOLD.DES. V. 7 711 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10404600
JRNL DOI 10.1016/S0969-2126(99)80092-6
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 CROSS-VALIDATION METHOD : FREE-R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.230
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.228
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1534
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 22065
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.222
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.220
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1415
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 20172
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1172
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1325.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 5335
REMARK 3 NUMBER OF RESTRAINTS : 4829
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 ANGLE DISTANCES (A) : 0.024
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.030
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.040
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.047
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.005
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.085
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28 (1995)53-56
REMARK 4
REMARK 4 1TOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SI CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22243
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 15.10
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.05
REMARK 200 R MERGE FOR SHELL (I) : 0.44600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.850
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: PHASES, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: MIRAS WAS SUPPORTED BY MOLECULAR REPLACEMENT USING N
REMARK 200 -TERMINAL DOMAIN FROM PREVIOUSLY SOLVED STRUCTURE OF G3P (1G3P)
REMARK 200 AS A STARTING MODEL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT CONCENTRATION 8-12 MG/ML IN
REMARK 280 50 MM HEPES (PH=7.5) WITH ADDITION OF DTT C=2MM, WAS
REMARK 280 CRYSTALLIZED USING VAPOR DIFFUSION FROM THE SITTING OR HANGING
REMARK 280 DROP, WITH THE SOLUTION CONTAINING 25% PEG4000, 0.08M TRIS (PH=
REMARK 280 8.5), AND 0.15 M SODIUM ACETATE AS A PRECIPITANT. BEFORE SETTING
REMARK 280 THE DROPS, PROTEIN SOLUTION WAS MIXED WITH THE PRECIPITANT IN
REMARK 280 THE RATIO 1:1. CRYSTALS WERE GROWING BEST AT TEMPERATURE 15
REMARK 280 DEGREES CELSIUS., PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.77800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 44.44000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 44.44000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.66700
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 44.44000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 44.44000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 15.88900
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 44.44000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.44000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 47.66700
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 44.44000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.44000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 15.88900
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 31.77800
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 GLU A 66
REMARK 465 ASN A 67
REMARK 465 GLU A 68
REMARK 465 GLY A 69
REMARK 465 GLY A 70
REMARK 465 GLY A 71
REMARK 465 SER A 72
REMARK 465 GLU A 73
REMARK 465 GLY A 74
REMARK 465 GLY A 75
REMARK 465 GLY A 76
REMARK 465 SER A 77
REMARK 465 GLU A 78
REMARK 465 GLY A 79
REMARK 465 GLY A 80
REMARK 465 GLY A 81
REMARK 465 SER A 82
REMARK 465 GLU A 83
REMARK 465 GLY A 84
REMARK 465 GLY A 85
REMARK 465 GLY A 86
REMARK 465 ASP A 87
REMARK 465 ASP A 88
REMARK 465 ILE A 89
REMARK 465 PHE A 90
REMARK 465 GLY A 91
REMARK 465 GLU A 92
REMARK 465 LEU A 93
REMARK 465 SER A 94
REMARK 465 SER A 95
REMARK 465 GLY A 96
REMARK 465 LYS A 97
REMARK 465 ASN A 98
REMARK 465 ALA A 99
REMARK 465 PRO A 100
REMARK 465 LYS A 101
REMARK 465 THR A 102
REMARK 465 GLY A 103
REMARK 465 GLY A 104
REMARK 465 GLY A 105
REMARK 465 ALA A 106
REMARK 465 LYS A 107
REMARK 465 GLY A 108
REMARK 465 ASN A 109
REMARK 465 ASN A 110
REMARK 465 ALA A 111
REMARK 465 SER A 112
REMARK 465 PRO A 113
REMARK 465 ALA A 114
REMARK 465 GLY A 115
REMARK 465 SER A 116
REMARK 465 GLY A 117
REMARK 465 ASN A 118
REMARK 465 THR A 119
REMARK 465 LYS A 120
REMARK 465 ASN A 121
REMARK 465 ASN A 122
REMARK 465 GLY A 123
REMARK 465 ALA A 124
REMARK 465 HIS A 217
REMARK 465 HIS A 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
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 ALA A 216 CA C O CB
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 158 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 164 C - N - CA ANGL. DEV. = 21.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 25 -78.49 -87.18
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 418 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A 427 DISTANCE = 9.09 ANGSTROMS
REMARK 525 HOH A 436 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 446 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH A 447 DISTANCE = 8.39 ANGSTROMS
REMARK 525 HOH A 449 DISTANCE = 6.68 ANGSTROMS
DBREF1 1TOL A 1 86 UNP A0A0N8P2C2_9PROT
DBREF2 1TOL A A0A0N8P2C2 19 104
DBREF 1TOL A 87 213 UNP P19934 TOLA_ECOLI 295 421
SEQADV 1TOL ALA A 214 UNP P19934 EXPRESSION TAG
SEQADV 1TOL ALA A 215 UNP P19934 EXPRESSION TAG
SEQADV 1TOL ALA A 216 UNP P19934 EXPRESSION TAG
SEQADV 1TOL HIS A 217 UNP P19934 EXPRESSION TAG
SEQADV 1TOL HIS A 218 UNP P19934 EXPRESSION TAG
SEQADV 1TOL HIS A 219 UNP P19934 EXPRESSION TAG
SEQADV 1TOL HIS A 220 UNP P19934 EXPRESSION TAG
SEQADV 1TOL HIS A 221 UNP P19934 EXPRESSION TAG
SEQADV 1TOL HIS A 222 UNP P19934 EXPRESSION TAG
SEQRES 1 A 222 ALA GLU THR VAL GLU SER CYS LEU ALA LYS SER HIS THR
SEQRES 2 A 222 GLU ASN SER PHE THR ASN VAL TRP LYS ASP ASP LYS THR
SEQRES 3 A 222 LEU ASP ARG TYR ALA ASN TYR GLU GLY CYS LEU TRP ASN
SEQRES 4 A 222 ALA THR GLY VAL VAL VAL CYS THR GLY ASP GLU THR GLN
SEQRES 5 A 222 CYS TYR GLY THR TRP VAL PRO ILE GLY LEU ALA ILE PRO
SEQRES 6 A 222 GLU ASN GLU GLY GLY GLY SER GLU GLY GLY GLY SER GLU
SEQRES 7 A 222 GLY GLY GLY SER GLU GLY GLY GLY ASP ASP ILE PHE GLY
SEQRES 8 A 222 GLU LEU SER SER GLY LYS ASN ALA PRO LYS THR GLY GLY
SEQRES 9 A 222 GLY ALA LYS GLY ASN ASN ALA SER PRO ALA GLY SER GLY
SEQRES 10 A 222 ASN THR LYS ASN ASN GLY ALA SER GLY ALA ASP ILE ASN
SEQRES 11 A 222 ASN TYR ALA GLY GLN ILE LYS SER ALA ILE GLU SER LYS
SEQRES 12 A 222 PHE TYR ASP ALA SER SER TYR ALA GLY LYS THR CYS THR
SEQRES 13 A 222 LEU ARG ILE LYS LEU ALA PRO ASP GLY MET LEU LEU ASP
SEQRES 14 A 222 ILE LYS PRO GLU GLY GLY ASP PRO ALA LEU CYS GLN ALA
SEQRES 15 A 222 ALA LEU ALA ALA ALA LYS LEU ALA LYS ILE PRO LYS PRO
SEQRES 16 A 222 PRO SER GLN ALA VAL TYR GLU VAL PHE LYS ASN ALA PRO
SEQRES 17 A 222 LEU ASP PHE LYS PRO ALA ALA ALA HIS HIS HIS HIS HIS
SEQRES 18 A 222 HIS
FORMUL 2 HOH *159(H2 O)
HELIX 1 1 VAL A 4 ALA A 9 1 6
HELIX 2 2 ALA A 127 LYS A 143 1 17
HELIX 3 3 ALA A 147 TYR A 150 5 4
HELIX 4 4 PRO A 177 LEU A 189 1 13
HELIX 5 5 GLN A 198 PHE A 204 1 7
SHEET 1 A 4 THR A 13 PHE A 17 0
SHEET 2 A 4 CYS A 53 LEU A 62 -1 N TRP A 57 O THR A 13
SHEET 3 A 4 CYS A 36 THR A 41 -1 N THR A 41 O THR A 56
SHEET 4 A 4 TYR A 30 TYR A 33 -1 N TYR A 33 O CYS A 36
SHEET 1 B 4 GLY A 42 VAL A 45 0
SHEET 2 B 4 PRO A 208 LYS A 212 -1 N LYS A 212 O GLY A 42
SHEET 3 B 4 CYS A 155 LYS A 160 -1 N LEU A 157 O LEU A 209
SHEET 4 B 4 ASP A 169 GLY A 175 -1 N GLY A 174 O THR A 156
SSBOND 1 CYS A 7 CYS A 36 1555 1555 2.04
SSBOND 2 CYS A 46 CYS A 53 1555 1555 2.06
SSBOND 3 CYS A 155 CYS A 180 1555 1555 2.04
CRYST1 88.880 88.880 63.556 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011251 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011251 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015734 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
