HEADER CYTOSKELETON 01-MAR-94 2SPC
TITLE CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPECTRIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227
KEYWDS CYTOSKELETON
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YAN,E.WINOGRAD,A.VIEL,T.CRONIN,S.C.HARRISON,D.BRANTON
REVDAT 6 21-FEB-24 2SPC 1 REMARK
REVDAT 5 14-AUG-19 2SPC 1 REMARK
REVDAT 4 17-JUL-19 2SPC 1 REMARK
REVDAT 3 16-NOV-11 2SPC 1 VERSN HETATM
REVDAT 2 24-FEB-09 2SPC 1 VERSN
REVDAT 1 31-MAY-94 2SPC 0
JRNL AUTH Y.YAN,E.WINOGRAD,A.VIEL,T.CRONIN,S.C.HARRISON,D.BRANTON
JRNL TITL CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN.
JRNL REF SCIENCE V. 262 2027 1993
JRNL REFN ISSN 0036-8075
JRNL PMID 8266097
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.203
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 USING ALL DATA, NO SIGMA CUTOFF.
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 : 1726
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2SPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178643.
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 23.40000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.61000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.40000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.61000
REMARK 290 SMTRY3 4 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 300 REMARK: THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO
REMARK 300 CHAIN *A*.
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: 5030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 656 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 655 LIES ON A SPECIAL POSITION.
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 NE2 GLN B 0 O HOH B 598 2.08
REMARK 500 NE2 HIS A 73 O HOH A 580 2.18
REMARK 500 OD2 ASP A 29 O HOH A 505 2.19
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 NH2 ARG B 9 NH2 ARG B 9 2665 1.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 38 CD GLU A 38 OE2 0.066
REMARK 500 GLU A 45 CD GLU A 45 OE2 0.092
REMARK 500 GLU A 88 CD GLU A 88 OE1 0.068
REMARK 500 GLU A 95 CD GLU A 95 OE1 0.085
REMARK 500 GLU A 99 CD GLU A 99 OE2 0.074
REMARK 500 GLU B 12 CD GLU B 12 OE1 0.092
REMARK 500 GLU B 38 CD GLU B 38 OE1 0.082
REMARK 500 GLU B 45 CD GLU B 45 OE1 0.067
REMARK 500 GLU B 55 CD GLU B 55 OE2 0.072
REMARK 500 GLU B 81 CD GLU B 81 OE2 0.108
REMARK 500 GLU B 88 CD GLU B 88 OE1 0.081
REMARK 500 GLU B 95 CD GLU B 95 OE1 0.086
REMARK 500 GLU B 99 CD GLU B 99 OE2 0.069
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 10 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP A 10 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP A 29 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 46 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP A 106 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP B 3 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG B 9 NE - CZ - NH1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG B 9 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP B 10 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP B 10 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG B 21 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP B 28 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP B 30 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG B 83 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG B 91 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 91 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 103 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP B 106 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP B 106 CB - CG - OD2 ANGL. DEV. = -7.4 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 ALA A 31 -52.89 -142.55
REMARK 500 ASN A 32 -153.00 74.34
REMARK 500 ALA A 33 -120.90 -88.69
REMARK 500 ASN B 1 -139.45 -112.15
REMARK 500 ASP B 29 -32.26 -26.58
REMARK 500 ALA B 31 47.85 -6.08
REMARK 500 VAL B 37 -72.54 -35.28
REMARK 500 ARG B 101 -72.37 -64.58
REMARK 500 SER B 102 -29.58 -34.64
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2SPC A 0 106 UNP P13395 SPTCA_DROME 1391 1497
DBREF 2SPC B 0 106 UNP P13395 SPTCA_DROME 1391 1497
SEQRES 1 A 107 GLN ASN LEU ASP LEU GLN LEU TYR MET ARG ASP CYS GLU
SEQRES 2 A 107 LEU ALA GLU SER TRP MET SER ALA ARG GLU ALA PHE LEU
SEQRES 3 A 107 ASN ALA ASP ASP ASP ALA ASN ALA GLY GLY ASN VAL GLU
SEQRES 4 A 107 ALA LEU ILE LYS LYS HIS GLU ASP PHE ASP LYS ALA ILE
SEQRES 5 A 107 ASN GLY HIS GLU GLN LYS ILE ALA ALA LEU GLN THR VAL
SEQRES 6 A 107 ALA ASP GLN LEU ILE ALA GLN ASN HIS TYR ALA SER ASN
SEQRES 7 A 107 LEU VAL ASP GLU LYS ARG LYS GLN VAL LEU GLU ARG TRP
SEQRES 8 A 107 ARG HIS LEU LYS GLU GLY LEU ILE GLU LYS ARG SER ARG
SEQRES 9 A 107 LEU GLY ASP
SEQRES 1 B 107 GLN ASN LEU ASP LEU GLN LEU TYR MET ARG ASP CYS GLU
SEQRES 2 B 107 LEU ALA GLU SER TRP MET SER ALA ARG GLU ALA PHE LEU
SEQRES 3 B 107 ASN ALA ASP ASP ASP ALA ASN ALA GLY GLY ASN VAL GLU
SEQRES 4 B 107 ALA LEU ILE LYS LYS HIS GLU ASP PHE ASP LYS ALA ILE
SEQRES 5 B 107 ASN GLY HIS GLU GLN LYS ILE ALA ALA LEU GLN THR VAL
SEQRES 6 B 107 ALA ASP GLN LEU ILE ALA GLN ASN HIS TYR ALA SER ASN
SEQRES 7 B 107 LEU VAL ASP GLU LYS ARG LYS GLN VAL LEU GLU ARG TRP
SEQRES 8 B 107 ARG HIS LEU LYS GLU GLY LEU ILE GLU LYS ARG SER ARG
SEQRES 9 B 107 LEU GLY ASP
FORMUL 3 HOH *156(H2 O)
HELIX 1 AA ASN A 1 ASP A 28 1 28
HELIX 2 BA VAL A 37 ALA A 70 1 34
HELIX 3 CA SER A 76 ASP A 106 1 31
HELIX 4 AB ASN B 1 ASP B 28 1 28
HELIX 5 BB VAL B 37 ALA B 70 1 34
HELIX 6 CB SER B 76 ASP B 106 1 31
CRYST1 46.800 47.220 104.430 90.00 90.00 90.00 P 21 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 0.021368 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021177 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009576 0.00000
MTRIX1 1 -0.550000 -0.835000 0.001000 36.22000 1
MTRIX2 1 -0.835000 0.550000 -0.006000 19.87000 1
MTRIX3 1 0.005000 -0.004000 -1.000000 114.97000 1
(ATOM LINES ARE NOT SHOWN.)
END