HEADER PROTEIN FIBRIL 08-DEC-11 2LMN
TITLE STRUCTURAL MODEL FOR A 40-RESIDUE BETA-AMYLOID FIBRIL WITH TWO-FOLD
TITLE 2 SYMMETRY, POSITIVE STAGGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-AMYLOID PROTEIN 40;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: BETA-APP40;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606
KEYWDS ALZHEIMER'S DISEASE, TWO-FOLD SYMMETRY, PROTEIN FIBRIL
EXPDTA SOLID-STATE NMR
NUMMDL 10
AUTHOR R.TYCKO,A.PETKOVA
REVDAT 2 03-MAY-17 2LMN 1 JRNL
REVDAT 1 28-DEC-11 2LMN 0
JRNL AUTH A.K.PARAVASTU,R.D.LEAPMAN,W.M.YAU,R.TYCKO
JRNL TITL MOLECULAR STRUCTURAL BASIS FOR POLYMORPHISM IN ALZHEIMER'S
JRNL TITL 2 BETA-AMYLOID FIBRILS.
JRNL REF PROC. NATL. ACAD. SCI. V. 105 18349 2008
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 19015532
JRNL DOI 10.1073/PNAS.0806270105
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH, X-PLOR_NIH
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE (X
REMARK 3 -PLOR_NIH), SCHWIETERS, KUSZEWSKI, TJANDRA AND
REMARK 3 CLORE (X-PLOR_NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LMN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000102569.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : SELECTIVE 13C AND 15N BETA
REMARK 210 -AMYLOID, 10 MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D FPRFDR; 2D RAD; 2D TEDOR;
REMARK 210 FSREDOR; 15N-BARE; 13C-BARE;
REMARK 210 PITHIRDS-CT; 2D NCACX
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INFINITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 THESE RECORDS ARE MEANINGLESS.
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: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L
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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 ASP A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 PHE A 4
REMARK 465 ARG A 5
REMARK 465 HIS A 6
REMARK 465 ASP A 7
REMARK 465 SER A 8
REMARK 465 ASP B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 PHE B 4
REMARK 465 ARG B 5
REMARK 465 HIS B 6
REMARK 465 ASP B 7
REMARK 465 SER B 8
REMARK 465 ASP C 1
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 PHE C 4
REMARK 465 ARG C 5
REMARK 465 HIS C 6
REMARK 465 ASP C 7
REMARK 465 SER C 8
REMARK 465 ASP D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 3
REMARK 465 PHE D 4
REMARK 465 ARG D 5
REMARK 465 HIS D 6
REMARK 465 ASP D 7
REMARK 465 SER D 8
REMARK 465 ASP E 1
REMARK 465 ALA E 2
REMARK 465 GLU E 3
REMARK 465 PHE E 4
REMARK 465 ARG E 5
REMARK 465 HIS E 6
REMARK 465 ASP E 7
REMARK 465 SER E 8
REMARK 465 ASP F 1
REMARK 465 ALA F 2
REMARK 465 GLU F 3
REMARK 465 PHE F 4
REMARK 465 ARG F 5
REMARK 465 HIS F 6
REMARK 465 ASP F 7
REMARK 465 SER F 8
REMARK 465 ASP G 1
REMARK 465 ALA G 2
REMARK 465 GLU G 3
REMARK 465 PHE G 4
REMARK 465 ARG G 5
REMARK 465 HIS G 6
REMARK 465 ASP G 7
REMARK 465 SER G 8
REMARK 465 ASP H 1
REMARK 465 ALA H 2
REMARK 465 GLU H 3
REMARK 465 PHE H 4
REMARK 465 ARG H 5
REMARK 465 HIS H 6
REMARK 465 ASP H 7
REMARK 465 SER H 8
REMARK 465 ASP I 1
REMARK 465 ALA I 2
REMARK 465 GLU I 3
REMARK 465 PHE I 4
REMARK 465 ARG I 5
REMARK 465 HIS I 6
REMARK 465 ASP I 7
REMARK 465 SER I 8
REMARK 465 ASP J 1
REMARK 465 ALA J 2
REMARK 465 GLU J 3
REMARK 465 PHE J 4
REMARK 465 ARG J 5
REMARK 465 HIS J 6
REMARK 465 ASP J 7
REMARK 465 SER J 8
REMARK 465 ASP K 1
REMARK 465 ALA K 2
REMARK 465 GLU K 3
REMARK 465 PHE K 4
REMARK 465 ARG K 5
REMARK 465 HIS K 6
REMARK 465 ASP K 7
REMARK 465 SER K 8
REMARK 465 ASP L 1
REMARK 465 ALA L 2
REMARK 465 GLU L 3
REMARK 465 PHE L 4
REMARK 465 ARG L 5
REMARK 465 HIS L 6
REMARK 465 ASP L 7
REMARK 465 SER L 8
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 H GLY G 29 HD21 ASN H 27 1.22
REMARK 500 HD21 ASN J 27 H GLY K 29 1.25
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 6 ALA G 30 N - CA - C ANGL. DEV. = -16.6 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 1 GLU A 22 82.00 -155.47
REMARK 500 1 ASP A 23 120.64 -34.84
REMARK 500 1 LYS A 28 -110.77 -45.34
REMARK 500 1 LYS B 16 115.72 -171.08
REMARK 500 1 ASN B 27 173.94 -42.02
REMARK 500 1 LYS C 16 104.31 -170.17
REMARK 500 1 VAL C 24 -112.85 -98.53
REMARK 500 1 SER C 26 170.11 171.15
REMARK 500 1 ASN C 27 158.61 -17.56
REMARK 500 1 LYS C 28 110.63 -161.26
REMARK 500 1 VAL C 36 70.10 -116.33
REMARK 500 1 VAL D 24 104.45 62.64
REMARK 500 1 SER D 26 171.93 -52.44
REMARK 500 1 LYS D 28 -106.51 -38.60
REMARK 500 1 ALA D 30 -163.86 67.55
REMARK 500 1 VAL D 36 74.06 -118.51
REMARK 500 1 LYS E 28 110.98 42.88
REMARK 500 1 HIS F 13 109.84 -161.11
REMARK 500 1 ASN F 27 174.88 -38.60
REMARK 500 1 HIS G 13 -168.78 -104.77
REMARK 500 1 ASN H 27 174.82 -40.16
REMARK 500 1 SER I 26 -174.11 -60.04
REMARK 500 1 ASN I 27 -175.30 98.53
REMARK 500 1 LYS I 28 110.36 38.71
REMARK 500 1 LYS J 16 114.03 -165.34
REMARK 500 1 VAL J 24 -131.60 -110.12
REMARK 500 1 SER J 26 177.76 169.65
REMARK 500 1 ASN J 27 172.36 -28.08
REMARK 500 1 LYS J 28 104.31 144.63
REMARK 500 1 LYS K 16 114.88 -164.81
REMARK 500 1 ASN K 27 170.50 -29.01
REMARK 500 1 VAL K 36 79.86 -116.56
REMARK 500 2 VAL A 36 77.74 -104.94
REMARK 500 2 ASP B 23 121.92 -38.09
REMARK 500 2 VAL B 24 -120.98 -58.55
REMARK 500 2 ASN B 27 -171.72 57.72
REMARK 500 2 LYS B 28 -111.30 -56.96
REMARK 500 2 ASN C 27 179.93 52.73
REMARK 500 2 LYS C 28 110.60 53.40
REMARK 500 2 SER D 26 -169.60 163.92
REMARK 500 2 ASN D 27 179.77 -50.64
REMARK 500 2 LYS D 28 112.38 60.49
REMARK 500 2 ASN E 27 -179.13 51.36
REMARK 500 2 LYS E 28 110.97 53.76
REMARK 500 2 LYS F 16 121.90 -170.90
REMARK 500 2 ASP F 23 -141.02 78.13
REMARK 500 2 SER F 26 150.61 -48.08
REMARK 500 2 LYS F 28 -103.95 -28.87
REMARK 500 2 ALA F 30 151.97 54.83
REMARK 500 2 LYS G 16 114.04 -171.57
REMARK 500
REMARK 500 THIS ENTRY HAS 375 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18127 RELATED DB: BMRB
REMARK 900 RELATED ID: 2LMO RELATED DB: PDB
REMARK 900 RELATED ID: 2LMP RELATED DB: PDB
REMARK 900 RELATED ID: 2LMQ RELATED DB: PDB
DBREF 2LMN A 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN B 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN C 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN D 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN E 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN F 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN G 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN H 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN I 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN J 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN K 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LMN L 1 40 UNP P05067 A4_HUMAN 672 711
SEQRES 1 A 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 A 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 A 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 A 40 VAL
SEQRES 1 B 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 B 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 B 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 B 40 VAL
SEQRES 1 C 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 C 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 C 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 C 40 VAL
SEQRES 1 D 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 D 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 D 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 D 40 VAL
SEQRES 1 E 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 E 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 E 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 E 40 VAL
SEQRES 1 F 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 F 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 F 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 F 40 VAL
SEQRES 1 G 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 G 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 G 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 G 40 VAL
SEQRES 1 H 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 H 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 H 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 H 40 VAL
SEQRES 1 I 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 I 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 I 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 I 40 VAL
SEQRES 1 J 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 J 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 J 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 J 40 VAL
SEQRES 1 K 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 K 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 K 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 K 40 VAL
SEQRES 1 L 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 L 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 L 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 L 40 VAL
SHEET 1 A 6 LEU A 17 ALA A 21 0
SHEET 2 A 6 LEU B 17 GLU B 22 1 O PHE B 20 N PHE A 19
SHEET 3 A 6 LEU C 17 GLU C 22 1 O VAL C 18 N PHE B 19
SHEET 4 A 6 LEU D 17 ALA D 21 1 O VAL D 18 N PHE C 19
SHEET 5 A 6 LYS E 16 VAL E 24 1 O PHE E 20 N PHE D 19
SHEET 6 A 6 LYS F 16 VAL F 24 1 O PHE F 20 N PHE E 19
SHEET 1 B 6 ALA A 30 MET A 35 0
SHEET 2 B 6 ALA B 30 MET B 35 1 O GLY B 33 N ILE A 32
SHEET 3 B 6 ALA C 30 MET C 35 1 O GLY C 33 N ILE B 32
SHEET 4 B 6 ILE D 31 MET D 35 1 O GLY D 33 N ILE C 32
SHEET 5 B 6 ILE E 31 MET E 35 1 O GLY E 33 N LEU D 34
SHEET 6 B 6 ILE F 31 MET F 35 1 O GLY F 33 N ILE E 32
SHEET 1 C 4 VAL C 12 HIS C 13 0
SHEET 2 C 4 GLU D 11 HIS D 13 1 O VAL D 12 N HIS C 13
SHEET 3 C 4 GLU E 11 HIS E 13 1 O VAL E 12 N GLU D 11
SHEET 4 C 4 VAL F 12 HIS F 13 1 O VAL F 12 N GLU E 11
SHEET 1 D 6 LEU G 17 ALA G 21 0
SHEET 2 D 6 LYS H 16 ALA H 21 1 O VAL H 18 N PHE G 19
SHEET 3 D 6 LYS I 16 ALA I 21 1 O VAL I 18 N LEU H 17
SHEET 4 D 6 LEU J 17 ASP J 23 1 O VAL J 18 N PHE I 19
SHEET 5 D 6 LEU K 17 ASP K 23 1 O VAL K 18 N PHE J 19
SHEET 6 D 6 LEU L 17 ALA L 21 1 O VAL L 18 N LEU K 17
SHEET 1 E 6 ILE G 31 MET G 35 0
SHEET 2 E 6 ILE H 31 MET H 35 1 O GLY H 33 N ILE G 32
SHEET 3 E 6 ILE I 31 MET I 35 1 O GLY I 33 N ILE H 32
SHEET 4 E 6 ILE J 31 MET J 35 1 O GLY J 33 N ILE I 32
SHEET 5 E 6 ILE K 31 MET K 35 1 O GLY K 33 N ILE J 32
SHEET 6 E 6 ILE L 31 MET L 35 1 O GLY L 33 N ILE K 32
SHEET 1 F 2 VAL J 12 HIS J 13 0
SHEET 2 F 2 VAL K 12 HIS K 13 1 O VAL K 12 N HIS J 13
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END