HEADER LYMPHOKINE 06-OCT-93 2TUN
TITLE CONFORMATIONAL CHANGES IN THE (ALA-84-VAL) MUTANT OF TUMOR NECROSIS
TITLE 2 FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR-ALPHA;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS LYMPHOKINE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.SALUDJIAN,T.PRANGE
REVDAT 3 13-JUL-11 2TUN 1 VERSN
REVDAT 2 24-FEB-09 2TUN 1 VERSN
REVDAT 1 31-JAN-94 2TUN 0
JRNL AUTH P.SALUDJIAN,T.PRANGE,R.KAHN,R.FOURME,J.TAVERNIER,
JRNL AUTH 2 X.VAN-OOSTADE,W.FIERS,G.NAVAZA
JRNL TITL CONFORMATIONAL CHANGES IN THE (ALA-84-VAL) MUTANT OF TUMOR
JRNL TITL 2 NECROSIS FACTOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.Y.JONES,N.P.WALKER,D.I.STUART
REMARK 1 TITL METHODOLOGY EMPLOYED FOR THE STRUCTURE DETERMINATION OF
REMARK 1 TITL 2 TUMOR NECROSIS FACTOR, A CASE OF HIGH NON-CRYSTALLOGRAPHIC
REMARK 1 TITL 3 SYMMETRY
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 47 753 1991
REMARK 1 REFN ISSN 0108-7673
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.J.ECK,S.R.SPRANG
REMARK 1 TITL THE STRUCTURE OF TUMOR NECROSIS FACTOR-ALPHA AT 2.6
REMARK 1 TITL 2 ANGSTROMS RESOLUTION. IMPLICATIONS FOR RECEPTOR BINDING
REMARK 1 REF J.BIOL.CHEM. V. 264 17595 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH E.Y.JONES,D.I.STUART,N.P.WALKER
REMARK 1 TITL STRUCTURE OF TUMOR NECROSIS FACTOR
REMARK 1 REF NATURE V. 338 225 1989
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 4
REMARK 1 AUTH A.LEWITT-BENTLEY,R.FOURME,R.KAHN,T.PRANGE,P.VACHETTE,
REMARK 1 AUTH 2 J.TAVERNIER,G.HAUQUIER,W.FIERS
REMARK 1 TITL STRUCTURE OF TUMOR NECROSIS FACTOR BY X-RAY SOLUTION
REMARK 1 TITL 2 SCATTERING AND PRELIMINARY STUDIES BY SINGLE CRYSTAL X-RAY
REMARK 1 TITL 3 DIFFRACTION
REMARK 1 REF J.MOL.BIOL. V. 199 389 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 15325
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7086
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.018 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.037 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.070 ; 0.040
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.007 ; 0.010
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.050 ; 0.030
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.230 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.290 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.180 ; 0.300
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 7.300 ; 2.000
REMARK 3 STAGGERED (DEGREES) : 17.700; 10.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.807 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.210 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.837 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.301 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE WAS SOLVED BY MOLECULAR REPLACEMENT (PROGRAM
REMARK 3 *AMORE*) STARTING FROM THE COORDINATES IN PROTEIN DATA BANK
REMARK 3 ENTRY 1TNF.
REMARK 3
REMARK 3 ONLY FAINT ELECTRON DENSITY IS OBSERVED FOR RESIDUES 1 - 6
REMARK 3 AT THE N-TERMINUS OF EACH CHAIN AND, THEREFORE, NO
REMARK 3 COORDINATES FOR THESE RESIDUES ARE PRESENT IN THIS ENTRY.
REMARK 3 ELECTRON DENSITY FOR THE LOOP 103 - 110 IS ALSO RATHER WEAK
REMARK 3 IN CHAINS A, B, D, AND F. SEVERE DISTORSIONS ARE ALSO
REMARK 3 OBSERVED IN THE SEGMENTS 7-9
REMARK 4
REMARK 4 2TUN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 65.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 31.23333
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 62.46667
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 62.46667
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 31.23333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, E
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 VAL A 1
REMARK 465 ARG A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 ARG A 6
REMARK 465 VAL B 1
REMARK 465 ARG B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 SER B 5
REMARK 465 ARG B 6
REMARK 465 VAL C 1
REMARK 465 ARG C 2
REMARK 465 SER C 3
REMARK 465 SER C 4
REMARK 465 SER C 5
REMARK 465 ARG C 6
REMARK 465 VAL D 1
REMARK 465 ARG D 2
REMARK 465 SER D 3
REMARK 465 SER D 4
REMARK 465 SER D 5
REMARK 465 ARG D 6
REMARK 465 VAL E 1
REMARK 465 ARG E 2
REMARK 465 SER E 3
REMARK 465 SER E 4
REMARK 465 SER E 5
REMARK 465 ARG E 6
REMARK 465 VAL F 1
REMARK 465 ARG F 2
REMARK 465 SER F 3
REMARK 465 SER F 4
REMARK 465 SER F 5
REMARK 465 ARG F 6
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PROTEIN DATA BANK ADVISORY NOTICE:
REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999 SWISS-PROT ENTRY NAME: TNFA_HUMAN
REMARK 999
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE
REMARK 999 ASP 220 LEU 137
DBREF 2TUN A 1 157 UNP P01375 TNFA_HUMAN 77 233
DBREF 2TUN B 1 157 UNP P01375 TNFA_HUMAN 77 233
DBREF 2TUN C 1 157 UNP P01375 TNFA_HUMAN 77 233
DBREF 2TUN D 1 157 UNP P01375 TNFA_HUMAN 77 233
DBREF 2TUN E 1 157 UNP P01375 TNFA_HUMAN 77 233
DBREF 2TUN F 1 157 UNP P01375 TNFA_HUMAN 77 233
SEQADV 2TUN VAL A 84 UNP P01375 ALA 160 CONFLICT
SEQADV 2TUN LEU A 143 UNP P01375 ASP 219 CONFLICT
SEQADV 2TUN VAL B 84 UNP P01375 ALA 160 CONFLICT
SEQADV 2TUN LEU B 143 UNP P01375 ASP 219 CONFLICT
SEQADV 2TUN VAL C 84 UNP P01375 ALA 160 CONFLICT
SEQADV 2TUN LEU C 143 UNP P01375 ASP 219 CONFLICT
SEQADV 2TUN VAL D 84 UNP P01375 ALA 160 CONFLICT
SEQADV 2TUN LEU D 143 UNP P01375 ASP 219 CONFLICT
SEQADV 2TUN VAL E 84 UNP P01375 ALA 160 CONFLICT
SEQADV 2TUN LEU E 143 UNP P01375 ASP 219 CONFLICT
SEQADV 2TUN VAL F 84 UNP P01375 ALA 160 CONFLICT
SEQADV 2TUN LEU F 143 UNP P01375 ASP 219 CONFLICT
SEQRES 1 A 157 VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES 2 A 157 ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES 3 A 157 GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES 4 A 157 GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES 5 A 157 GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES 6 A 157 GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES 7 A 157 THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL
SEQRES 8 A 157 ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES 9 A 157 THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES 10 A 157 ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES 11 A 157 ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES 12 A 157 PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES 13 A 157 LEU
SEQRES 1 B 157 VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES 2 B 157 ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES 3 B 157 GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES 4 B 157 GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES 5 B 157 GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES 6 B 157 GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES 7 B 157 THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL
SEQRES 8 B 157 ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES 9 B 157 THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES 10 B 157 ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES 11 B 157 ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES 12 B 157 PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES 13 B 157 LEU
SEQRES 1 C 157 VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES 2 C 157 ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES 3 C 157 GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES 4 C 157 GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES 5 C 157 GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES 6 C 157 GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES 7 C 157 THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL
SEQRES 8 C 157 ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES 9 C 157 THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES 10 C 157 ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES 11 C 157 ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES 12 C 157 PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES 13 C 157 LEU
SEQRES 1 D 157 VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES 2 D 157 ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES 3 D 157 GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES 4 D 157 GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES 5 D 157 GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES 6 D 157 GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES 7 D 157 THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL
SEQRES 8 D 157 ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES 9 D 157 THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES 10 D 157 ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES 11 D 157 ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES 12 D 157 PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES 13 D 157 LEU
SEQRES 1 E 157 VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES 2 E 157 ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES 3 E 157 GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES 4 E 157 GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES 5 E 157 GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES 6 E 157 GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES 7 E 157 THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL
SEQRES 8 E 157 ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES 9 E 157 THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES 10 E 157 ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES 11 E 157 ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES 12 E 157 PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES 13 E 157 LEU
SEQRES 1 F 157 VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES 2 F 157 ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES 3 F 157 GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES 4 F 157 GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES 5 F 157 GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES 6 F 157 GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES 7 F 157 THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL
SEQRES 8 F 157 ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES 9 F 157 THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES 10 F 157 ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES 11 F 157 ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES 12 F 157 PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES 13 F 157 LEU
HELIX 1 H1A ARG A 138 LEU A 142 5 5
HELIX 2 H1B ARG B 138 LEU B 142 5 5
HELIX 3 H1C ARG C 138 LEU C 142 5 5
HELIX 4 H1D ARG D 138 LEU D 142 5 5
HELIX 5 H1E ARG E 138 LEU E 142 5 5
HELIX 6 H1F ARG F 138 LEU F 142 5 5
SHEET 1 S1A 5 LEU A 36 ALA A 38 0
SHEET 2 S1A 5 PRO A 12 ALA A 18 -1 N HIS A 15 O LEU A 36
SHEET 3 S1A 5 VAL A 150 LEU A 157 -1 O VAL A 150 N ALA A 18
SHEET 4 S1A 5 GLY A 54 GLY A 68 -1 O GLN A 61 N TYR A 151
SHEET 5 S1A 5 LYS A 112 LEU A 126 -1 N LEU A 126 O GLY A 54
SHEET 1 S2A 5 GLU A 42 ARG A 44 0
SHEET 2 S2A 5 GLN A 47 VAL A 50 -1 O GLN A 47 N ARG A 44
SHEET 3 S2A 5 GLY A 129 ILE A 136 -1 N GLY A 129 O VAL A 50
SHEET 4 S2A 5 LEU A 76 VAL A 84 -1 N THR A 79 O GLU A 135
SHEET 5 S2A 5 GLN A 88 LYS A 98 -1 N VAL A 91 O ARG A 82
SHEET 1 S1B 5 LEU B 36 ALA B 38 0
SHEET 2 S1B 5 PRO B 12 ALA B 18 -1 N HIS B 15 O LEU B 36
SHEET 3 S1B 5 VAL B 150 LEU B 157 -1 O VAL B 150 N ALA B 18
SHEET 4 S1B 5 GLY B 54 GLY B 68 -1 O GLN B 61 N TYR B 151
SHEET 5 S1B 5 LYS B 112 LEU B 126 -1 N LEU B 126 O GLY B 54
SHEET 1 S2B 5 GLU B 42 ARG B 44 0
SHEET 2 S2B 5 GLN B 47 VAL B 50 -1 O GLN B 47 N ARG B 44
SHEET 3 S2B 5 GLY B 129 ILE B 136 -1 N GLY B 129 O VAL B 50
SHEET 4 S2B 5 LEU B 76 VAL B 84 -1 N THR B 79 O GLU B 135
SHEET 5 S2B 5 GLN B 88 LYS B 98 -1 N VAL B 91 O ARG B 82
SHEET 1 S1C 5 LEU C 36 ALA C 38 0
SHEET 2 S1C 5 PRO C 12 ALA C 18 -1 N HIS C 15 O LEU C 36
SHEET 3 S1C 5 VAL C 150 LEU C 157 -1 O VAL C 150 N ALA C 18
SHEET 4 S1C 5 GLY C 54 GLY C 68 -1 O GLN C 61 N TYR C 151
SHEET 5 S1C 5 LYS C 112 LEU C 126 -1 N LEU C 126 O GLY C 54
SHEET 1 S2C 5 GLU C 42 ARG C 44 0
SHEET 2 S2C 5 GLN C 47 VAL C 50 -1 O GLN C 47 N ARG C 44
SHEET 3 S2C 5 GLY C 129 ILE C 136 -1 N GLY C 129 O VAL C 50
SHEET 4 S2C 5 LEU C 76 VAL C 84 -1 N THR C 79 O GLU C 135
SHEET 5 S2C 5 GLN C 88 LYS C 98 -1 N VAL C 91 O ARG C 82
SHEET 1 S1D 5 LEU D 36 ALA D 38 0
SHEET 2 S1D 5 PRO D 12 ALA D 18 -1 N HIS D 15 O LEU D 36
SHEET 3 S1D 5 VAL D 150 LEU D 157 -1 O VAL D 150 N ALA D 18
SHEET 4 S1D 5 GLY D 54 GLY D 68 -1 O GLN D 61 N TYR D 151
SHEET 5 S1D 5 LYS D 112 LEU D 126 -1 N LEU D 126 O GLY D 54
SHEET 1 S2D 5 GLU D 42 ARG D 44 0
SHEET 2 S2D 5 GLN D 47 VAL D 50 -1 O GLN D 47 N ARG D 44
SHEET 3 S2D 5 GLY D 129 ILE D 136 -1 N GLY D 129 O VAL D 50
SHEET 4 S2D 5 LEU D 76 VAL D 84 -1 N THR D 79 O GLU D 135
SHEET 5 S2D 5 GLN D 88 LYS D 98 -1 N VAL D 91 O ARG D 82
SHEET 1 S1E 5 LEU E 36 ALA E 38 0
SHEET 2 S1E 5 PRO E 12 ALA E 18 -1 N HIS E 15 O LEU E 36
SHEET 3 S1E 5 VAL E 150 LEU E 157 -1 O VAL E 150 N ALA E 18
SHEET 4 S1E 5 GLY E 54 GLY E 68 -1 O GLN E 61 N TYR E 151
SHEET 5 S1E 5 LYS E 112 LEU E 126 -1 N LEU E 126 O GLY E 54
SHEET 1 S2E 5 GLU E 42 ARG E 44 0
SHEET 2 S2E 5 GLN E 47 VAL E 50 -1 O GLN E 47 N ARG E 44
SHEET 3 S2E 5 GLY E 129 ILE E 136 -1 N GLY E 129 O VAL E 50
SHEET 4 S2E 5 LEU E 76 VAL E 84 -1 N THR E 79 O GLU E 135
SHEET 5 S2E 5 GLN E 88 LYS E 98 -1 N VAL E 91 O ARG E 82
SHEET 1 S1F 5 LEU F 36 ALA F 38 0
SHEET 2 S1F 5 PRO F 12 ALA F 18 -1 N HIS F 15 O LEU F 36
SHEET 3 S1F 5 VAL F 150 LEU F 157 -1 O VAL F 150 N ALA F 18
SHEET 4 S1F 5 GLY F 54 GLY F 68 -1 O GLN F 61 N TYR F 151
SHEET 5 S1F 5 LYS F 112 LEU F 126 -1 N LEU F 126 O GLY F 54
SHEET 1 S2F 5 GLU F 42 ARG F 44 0
SHEET 2 S2F 5 GLN F 47 VAL F 50 -1 O GLN F 47 N ARG F 44
SHEET 3 S2F 5 GLY F 129 ILE F 136 -1 N GLY F 129 O VAL F 50
SHEET 4 S2F 5 LEU F 76 VAL F 84 -1 N THR F 79 O GLU F 135
SHEET 5 S2F 5 GLN F 88 LYS F 98 -1 N VAL F 91 O ARG F 82
SSBOND 1 CYS A 69 CYS A 101 1555 1555 2.07
SSBOND 2 CYS B 69 CYS B 101 1555 1555 2.08
SSBOND 3 CYS C 69 CYS C 101 1555 1555 2.07
SSBOND 4 CYS D 69 CYS D 101 1555 1555 2.07
SSBOND 5 CYS E 69 CYS E 101 1555 1555 2.09
SSBOND 6 CYS F 69 CYS F 101 1555 1555 2.08
CISPEP 1 THR B 7 PRO B 8 0 27.64
CRYST1 166.000 166.000 93.700 90.00 90.00 120.00 P 31 2 1 36
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 0.006024 0.003478 0.000000 0.00000
SCALE2 0.000000 0.006956 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010672 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
