HEADER MEMBRANE PROTEIN 22-JUN-01 1JFU
TITLE CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF TLPA FROM
TITLE 2 BRADYRHIZOBIUM JAPONICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN TLPA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SOLUBLE DOMAIN OF TLPA (RESIDUES 36-221);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRADYRHIZOBIUM JAPONICUM;
SOURCE 3 ORGANISM_TAXID: 375;
SOURCE 4 GENE: TLPA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMAL-P
KEYWDS THIOREDOXIN-LIKE, DOUBLE DISULFIDE BRIDGE, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.CAPITANI,R.ROSSMANN,D.F.SARGENT,M.G.GRUETTER,T.J.RICHMOND,
AUTHOR 2 H.HENNECKE
REVDAT 4 24-FEB-09 1JFU 1 VERSN
REVDAT 3 01-APR-03 1JFU 1 JRNL
REVDAT 2 25-DEC-02 1JFU 1 REMARK
REVDAT 1 19-SEP-01 1JFU 0
JRNL AUTH G.CAPITANI,R.ROSSMANN,D.F.SARGENT,M.G.GRUTTER,
JRNL AUTH 2 T.J.RICHMOND,H.HENNECKE
JRNL TITL STRUCTURE OF THE SOLUBLE DOMAIN OF A
JRNL TITL 2 MEMBRANE-ANCHORED THIOREDOXIN-LIKE PROTEIN FROM
JRNL TITL 3 BRADYRHIZOBIUM JAPONICUM REVEALS UNUSUAL
JRNL TITL 4 PROPERTIES.
JRNL REF J.MOL.BIOL. V. 311 1037 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11531338
JRNL DOI 10.1006/JMBI.2001.4913
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 36890
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1863
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2671
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 555
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : 0.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.013 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 1.560 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.880 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.540 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JFU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUN-01.
REMARK 100 THE RCSB ID CODE IS RCSB013719.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
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 : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC CONFOCAL MAX-FLUX
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36890
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
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 (%): 38.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BICINE, NACL, PEG550 MME, PH 9.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 280K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 25.31000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.49500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.57500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.49500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.31000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.57500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 1
REMARK 465 ARG A 2
REMARK 465 ALA A 3
REMARK 465 PRO A 4
REMARK 465 LYS A 181
REMARK 465 ALA A 182
REMARK 465 ALA A 183
REMARK 465 ALA A 184
REMARK 465 ALA A 185
REMARK 465 LEU A 186
REMARK 465 SER B 1
REMARK 465 ARG B 2
REMARK 465 ALA B 3
REMARK 465 LYS B 181
REMARK 465 ALA B 182
REMARK 465 ALA B 183
REMARK 465 ALA B 184
REMARK 465 ALA B 185
REMARK 465 LEU B 186
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS A 39 O HOH A 331 1.93
REMARK 500 O HOH A 248 O HOH A 371 1.97
REMARK 500 O HOH B 217 O HOH B 328 1.98
REMARK 500 NZ LYS B 110 O HOH B 338 2.00
REMARK 500 NZ LYS A 88 O HOH A 440 2.00
REMARK 500 NH1 ARG B 104 O HOH B 394 2.00
REMARK 500 O HOH A 422 O HOH A 475 2.01
REMARK 500 NH1 ARG B 176 O HOH B 410 2.06
REMARK 500 O HOH A 347 O HOH A 408 2.09
REMARK 500 OE2 GLU A 107 O HOH A 438 2.14
REMARK 500 O HOH A 362 O HOH A 419 2.14
REMARK 500 NZ LYS B 51 O HOH B 442 2.14
REMARK 500 O HOH A 379 O HOH A 460 2.15
REMARK 500 O HOH A 271 O HOH A 423 2.17
REMARK 500 O HOH B 306 O HOH B 365 2.18
REMARK 500 O HOH B 360 O HOH B 437 2.18
REMARK 500 OE2 GLU B 46 O HOH B 428 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS A 51 O HOH B 359 3645 1.83
REMARK 500 OG1 THR A 5 OE2 GLU B 84 4465 1.95
REMARK 500 O HOH A 414 O HOH B 423 4455 2.06
REMARK 500 O HOH A 408 O HOH B 225 3545 2.13
REMARK 500 O HOH A 384 O HOH B 375 2565 2.19
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 ALA A 129 19.87 56.90
REMARK 500 ASP B 105 76.32 60.87
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 480 DISTANCE = 5.48 ANGSTROMS
DBREF 1JFU A 1 186 UNP P43221 TLPA_BRAJA 36 221
DBREF 1JFU B 1 186 UNP P43221 TLPA_BRAJA 36 221
SEQRES 1 A 186 SER ARG ALA PRO THR GLY ASP PRO ALA CYS ARG ALA ALA
SEQRES 2 A 186 VAL ALA THR ALA GLN LYS ILE ALA PRO LEU ALA HIS GLY
SEQRES 3 A 186 GLU VAL ALA ALA LEU THR MET ALA SER ALA PRO LEU LYS
SEQRES 4 A 186 LEU PRO ASP LEU ALA PHE GLU ASP ALA ASP GLY LYS PRO
SEQRES 5 A 186 LYS LYS LEU SER ASP PHE ARG GLY LYS THR LEU LEU VAL
SEQRES 6 A 186 ASN LEU TRP ALA THR TRP CYS VAL PRO CYS ARG LYS GLU
SEQRES 7 A 186 MET PRO ALA LEU ASP GLU LEU GLN GLY LYS LEU SER GLY
SEQRES 8 A 186 PRO ASN PHE GLU VAL VAL ALA ILE ASN ILE ASP THR ARG
SEQRES 9 A 186 ASP PRO GLU LYS PRO LYS THR PHE LEU LYS GLU ALA ASN
SEQRES 10 A 186 LEU THR ARG LEU GLY TYR PHE ASN ASP GLN LYS ALA LYS
SEQRES 11 A 186 VAL PHE GLN ASP LEU LYS ALA ILE GLY ARG ALA LEU GLY
SEQRES 12 A 186 MET PRO THR SER VAL LEU VAL ASP PRO GLN GLY CYS GLU
SEQRES 13 A 186 ILE ALA THR ILE ALA GLY PRO ALA GLU TRP ALA SER GLU
SEQRES 14 A 186 ASP ALA LEU LYS LEU ILE ARG ALA ALA THR GLY LYS ALA
SEQRES 15 A 186 ALA ALA ALA LEU
SEQRES 1 B 186 SER ARG ALA PRO THR GLY ASP PRO ALA CYS ARG ALA ALA
SEQRES 2 B 186 VAL ALA THR ALA GLN LYS ILE ALA PRO LEU ALA HIS GLY
SEQRES 3 B 186 GLU VAL ALA ALA LEU THR MET ALA SER ALA PRO LEU LYS
SEQRES 4 B 186 LEU PRO ASP LEU ALA PHE GLU ASP ALA ASP GLY LYS PRO
SEQRES 5 B 186 LYS LYS LEU SER ASP PHE ARG GLY LYS THR LEU LEU VAL
SEQRES 6 B 186 ASN LEU TRP ALA THR TRP CYS VAL PRO CYS ARG LYS GLU
SEQRES 7 B 186 MET PRO ALA LEU ASP GLU LEU GLN GLY LYS LEU SER GLY
SEQRES 8 B 186 PRO ASN PHE GLU VAL VAL ALA ILE ASN ILE ASP THR ARG
SEQRES 9 B 186 ASP PRO GLU LYS PRO LYS THR PHE LEU LYS GLU ALA ASN
SEQRES 10 B 186 LEU THR ARG LEU GLY TYR PHE ASN ASP GLN LYS ALA LYS
SEQRES 11 B 186 VAL PHE GLN ASP LEU LYS ALA ILE GLY ARG ALA LEU GLY
SEQRES 12 B 186 MET PRO THR SER VAL LEU VAL ASP PRO GLN GLY CYS GLU
SEQRES 13 B 186 ILE ALA THR ILE ALA GLY PRO ALA GLU TRP ALA SER GLU
SEQRES 14 B 186 ASP ALA LEU LYS LEU ILE ARG ALA ALA THR GLY LYS ALA
SEQRES 15 B 186 ALA ALA ALA LEU
FORMUL 3 HOH *555(H2 O)
HELIX 1 1 ASP A 7 ALA A 9 5 3
HELIX 2 2 CYS A 10 ALA A 21 1 12
HELIX 3 3 PRO A 22 ALA A 24 5 3
HELIX 4 4 HIS A 25 ALA A 29 5 5
HELIX 5 5 SER A 56 ARG A 59 5 4
HELIX 6 6 CYS A 72 SER A 90 1 19
HELIX 7 7 GLU A 107 ALA A 116 1 10
HELIX 8 8 ALA A 129 ALA A 137 1 9
HELIX 9 9 SER A 168 GLY A 180 1 13
HELIX 10 10 ASP B 7 ALA B 9 5 3
HELIX 11 11 CYS B 10 ALA B 21 1 12
HELIX 12 12 PRO B 22 ALA B 24 5 3
HELIX 13 13 HIS B 25 ALA B 29 5 5
HELIX 14 14 SER B 56 ARG B 59 5 4
HELIX 15 15 CYS B 72 SER B 90 1 19
HELIX 16 16 GLU B 107 ALA B 116 1 10
HELIX 17 17 ALA B 129 ILE B 138 1 10
HELIX 18 18 SER B 168 GLY B 180 1 13
SHEET 1 A 6 THR A 32 MET A 33 0
SHEET 2 A 6 GLU A 156 ALA A 161 -1 O THR A 159 N THR A 32
SHEET 3 A 6 THR A 146 VAL A 150 -1 O SER A 147 N ILE A 160
SHEET 4 A 6 THR A 62 TRP A 68 -1 O LEU A 63 N VAL A 150
SHEET 5 A 6 PHE A 94 ASN A 100 1 O GLU A 95 N LEU A 64
SHEET 6 A 6 PHE A 124 ASN A 125 1 O PHE A 124 N ASN A 100
SHEET 1 B 2 ALA A 44 GLU A 46 0
SHEET 2 B 2 PRO A 52 LYS A 54 -1 N LYS A 53 O PHE A 45
SHEET 1 C 6 THR B 32 MET B 33 0
SHEET 2 C 6 GLU B 156 ALA B 161 -1 O THR B 159 N THR B 32
SHEET 3 C 6 THR B 146 VAL B 150 -1 O SER B 147 N ILE B 160
SHEET 4 C 6 THR B 62 TRP B 68 -1 O LEU B 63 N VAL B 150
SHEET 5 C 6 PHE B 94 ASN B 100 1 O GLU B 95 N LEU B 64
SHEET 6 C 6 PHE B 124 ASN B 125 1 O PHE B 124 N ASN B 100
SHEET 1 D 2 ALA B 44 GLU B 46 0
SHEET 2 D 2 PRO B 52 LYS B 54 -1 N LYS B 53 O PHE B 45
SSBOND 1 CYS A 10 CYS A 155 1555 1555 2.02
SSBOND 2 CYS A 72 CYS A 75 1555 1555 2.03
SSBOND 3 CYS B 10 CYS B 155 1555 1555 2.04
SSBOND 4 CYS B 72 CYS B 75 1555 1555 2.06
CISPEP 1 MET A 144 PRO A 145 0 -2.62
CISPEP 2 MET B 144 PRO B 145 0 1.07
CRYST1 50.620 75.150 82.990 90.00 90.00 90.00 P 21 21 21 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 0.019755 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013307 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012050 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
