HEADER PROTEIN FIBRIL 10-JUN-14 2MPZ
TITLE ATOMIC MODEL OF THE ABETA D23N "IOWA" MUTANT USING SOLID-STATE NMR, EM
TITLE 2 AND ROSETTA MODELING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMYLOID BETA A4 PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U,
COMPND 4 V, W, X, Y, Z, a;
COMPND 5 SYNONYM: ABPP, APPI, APP, ALZHEIMER DISEASE AMYLOID PROTEIN, CEREBRAL
COMPND 6 VASCULAR AMYLOID PEPTIDE, CVAP, PREA4, PROTEASE NEXIN-II, PN-II, N-
COMPND 7 APP, SOLUBLE APP-ALPHA, S-APP-ALPHA, SOLUBLE APP-BETA, S-APP-BETA,
COMPND 8 C99, BETA-AMYLOID PROTEIN 42, BETA-APP42, BETA-AMYLOID PROTEIN 40,
COMPND 9 BETA-APP40, C83, P3(42), P3(40), C80, GAMMA-SECRETASE C-TERMINAL
COMPND 10 FRAGMENT 59, AMYLOID INTRACELLULAR DOMAIN 59, AICD-59, AID(59),
COMPND 11 GAMMA-CTF(59), GAMMA-SECRETASE C-TERMINAL FRAGMENT 57, AMYLOID
COMPND 12 INTRACELLULAR DOMAIN 57, AICD-57, AID(57), GAMMA-CTF(57), GAMMA-
COMPND 13 SECRETASE C-TERMINAL FRAGMENT 50, AMYLOID INTRACELLULAR DOMAIN 50,
COMPND 14 AICD-50, AID(50), GAMMA-CTF(50), C31;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: APP, A4, AD1
KEYWDS AMYLOID, POLYMORHPISM, SPARSE DATA, HYBRID METHODS, PROTEIN FIBRIL
EXPDTA SOLID-STATE NMR
NUMMDL 5
AUTHOR N.G.SGOURAKIS,W.QIANG
REVDAT 2 29-APR-15 2MPZ 1
REVDAT 1 22-APR-15 2MPZ 0
JRNL AUTH N.G.SGOURAKIS,W.M.YAU,W.QIANG
JRNL TITL MODELING AN IN-REGISTER, PARALLEL "IOWA" A BETA FIBRIL
JRNL TITL 2 STRUCTURE USING SOLID-STATE NMR DATA FROM LABELED SAMPLES
JRNL TITL 3 WITH ROSETTA.
JRNL REF STRUCTURE V. 23 216 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 25543257
JRNL DOI 10.1016/J.STR.2014.10.022
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ROSETTA, CS-ROSETTA
REMARK 3 AUTHORS : SGOURAKIS AND BAKER (ROSETTA), (CS-ROSETTA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 1-14 WERE HIGHLY DYNAMIC BASED
REMARK 3 ON SEPARATE SOLID-STATE NMR EXPERIMENTS AND WERE NOT INCLUDED IN
REMARK 3 THE FINAL MODELS
REMARK 4
REMARK 4 2MPZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-14.
REMARK 100 THE RCSB ID CODE IS RCSB103911.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 25 UM [U-99% 13C; U-99% 15N]
REMARK 210 ABETA D23N, SOLID
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 13C/13C SPIN DIFFUSION; 1D
REMARK 210 13C PITHIRDS; 1D 13C/15N REDOR
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ROSETTA
REMARK 210 METHOD USED : ROSETTA REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: WHILE INFORMATION FROM STEM MASS-PER-LENGTH MEASUREMENTS
REMARK 210 WAS USED TO ESTABLISH THE OVERALL 3-FOLD SYMMETRY OF THE SYSTEM,
REMARK 210 NO DETAILED EM MAP DENSITY WAS USED IN STRUCTURE REFINEMENT. THE
REMARK 210 REFINEMENT WAS BASED PRIMARILY ON THE SOLID-STATE NMR DATA
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: 27-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS: J, K, L, M, N, O, P, Q, R,
REMARK 350 AND CHAINS: S, T, U, V, W, X, Y, Z, 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 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 2 VAL A 39 -51.92 -121.39
REMARK 500 2 VAL B 39 -51.93 -121.45
REMARK 500 2 VAL C 39 -51.87 -121.45
REMARK 500 2 VAL D 39 -51.97 -121.42
REMARK 500 2 VAL E 39 -51.93 -121.40
REMARK 500 2 VAL F 39 -51.90 -121.46
REMARK 500 2 VAL G 39 -51.93 -121.44
REMARK 500 2 VAL H 39 -51.90 -121.38
REMARK 500 2 VAL I 39 -52.00 -121.39
REMARK 500 2 VAL J 39 -51.97 -121.36
REMARK 500 2 VAL K 39 -51.85 -121.54
REMARK 500 2 VAL L 39 -51.90 -121.41
REMARK 500 2 VAL M 39 -51.95 -121.41
REMARK 500 2 VAL N 39 -52.03 -121.38
REMARK 500 2 VAL O 39 -51.85 -121.40
REMARK 500 2 VAL P 39 -51.94 -121.39
REMARK 500 2 VAL Q 39 -51.97 -121.44
REMARK 500 2 VAL R 39 -51.99 -121.37
REMARK 500 2 VAL S 39 -51.93 -121.51
REMARK 500 2 VAL T 39 -51.95 -121.42
REMARK 500 2 VAL U 39 -52.01 -121.42
REMARK 500 2 VAL V 39 -51.93 -121.49
REMARK 500 2 VAL W 39 -52.01 -121.51
REMARK 500 2 VAL X 39 -52.03 -121.37
REMARK 500 2 VAL Y 39 -51.94 -121.47
REMARK 500 2 VAL Z 39 -51.93 -121.46
REMARK 500 2 VAL a 39 -51.87 -121.46
REMARK 500 5 VAL A 36 -61.22 -108.66
REMARK 500 5 VAL B 36 -61.12 -108.69
REMARK 500 5 VAL C 36 -61.17 -108.65
REMARK 500 5 VAL D 36 -61.13 -108.66
REMARK 500 5 VAL E 36 -61.25 -108.54
REMARK 500 5 VAL F 36 -61.19 -108.65
REMARK 500 5 VAL G 36 -61.18 -108.67
REMARK 500 5 VAL H 36 -61.20 -108.60
REMARK 500 5 VAL I 36 -61.25 -108.57
REMARK 500 5 VAL J 36 -61.30 -108.66
REMARK 500 5 VAL K 36 -61.08 -108.64
REMARK 500 5 VAL L 36 -61.14 -108.70
REMARK 500 5 VAL M 36 -61.20 -108.74
REMARK 500 5 VAL N 36 -61.20 -108.66
REMARK 500 5 VAL O 36 -61.18 -108.64
REMARK 500 5 VAL P 36 -61.11 -108.67
REMARK 500 5 VAL Q 36 -61.03 -108.69
REMARK 500 5 VAL R 36 -61.16 -108.65
REMARK 500 5 VAL S 36 -61.12 -108.68
REMARK 500 5 VAL T 36 -61.21 -108.65
REMARK 500 5 VAL U 36 -61.14 -108.59
REMARK 500 5 VAL V 36 -61.25 -108.61
REMARK 500 5 VAL W 36 -61.26 -108.65
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 25004 RELATED DB: BMRB
DBREF 2MPZ A 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ B 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ C 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ D 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ E 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ F 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ G 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ H 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ I 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ J 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ K 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ L 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ M 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ N 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ O 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ P 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ Q 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ R 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ S 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ T 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ U 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ V 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ W 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ X 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ Y 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ Z 15 40 UNP P05067 A4_HUMAN 686 711
DBREF 2MPZ a 15 40 UNP P05067 A4_HUMAN 686 711
SEQADV 2MPZ ASN A 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN B 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN C 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN D 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN E 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN F 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN G 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN H 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN I 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN J 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN K 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN L 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN M 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN N 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN O 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN P 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN Q 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN R 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN S 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN T 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN U 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN V 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN W 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN X 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN Y 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN Z 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQADV 2MPZ ASN a 23 UNP P05067 ASP 694 ENGINEERED MUTATION
SEQRES 1 A 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 A 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 B 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 B 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 C 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 C 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 D 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 D 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 E 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 E 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 F 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 F 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 G 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 G 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 H 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 H 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 I 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 I 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 J 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 J 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 K 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 K 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 L 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 L 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 M 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 M 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 N 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 N 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 O 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 O 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 P 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 P 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 Q 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 Q 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 R 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 R 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 S 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 S 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 T 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 T 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 U 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 U 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 V 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 V 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 W 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 W 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 X 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 X 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 Y 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 Y 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 Z 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 Z 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SEQRES 1 a 26 GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER ASN
SEQRES 2 a 26 LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL VAL
SHEET 1 A 9 LEU A 17 VAL A 24 0
SHEET 2 A 9 LEU Y 17 VAL Y 24 1 O VAL Y 18 N LEU A 17
SHEET 3 A 9 LEU V 17 VAL V 24 1 N VAL V 18 O LEU Y 17
SHEET 4 A 9 LEU S 17 VAL S 24 1 N VAL S 18 O LEU V 17
SHEET 5 A 9 LEU P 17 VAL P 24 1 N VAL P 18 O LEU S 17
SHEET 6 A 9 LEU M 17 VAL M 24 1 N VAL M 18 O LEU P 17
SHEET 7 A 9 LEU J 17 VAL J 24 1 N VAL J 18 O LEU M 17
SHEET 8 A 9 LEU G 17 VAL G 24 1 N VAL G 18 O LEU J 17
SHEET 9 A 9 LEU D 17 VAL D 24 1 N VAL D 18 O LEU G 17
SHEET 1 B 9 ILE A 31 VAL A 36 0
SHEET 2 B 9 ILE Y 31 VAL Y 36 1 O GLY Y 33 N LEU A 34
SHEET 3 B 9 ILE V 31 VAL V 36 1 N GLY V 33 O LEU Y 34
SHEET 4 B 9 ILE S 31 VAL S 36 1 N GLY S 33 O LEU V 34
SHEET 5 B 9 ILE P 31 VAL P 36 1 N GLY P 33 O LEU S 34
SHEET 6 B 9 ILE M 31 VAL M 36 1 N GLY M 33 O LEU P 34
SHEET 7 B 9 ILE J 31 VAL J 36 1 N GLY J 33 O LEU M 34
SHEET 8 B 9 ILE G 31 VAL G 36 1 N GLY G 33 O LEU J 34
SHEET 9 B 9 ILE D 31 VAL D 36 1 N GLY D 33 O LEU G 34
SHEET 1 C 9 LEU B 17 VAL B 24 0
SHEET 2 C 9 LEU E 17 VAL E 24 1 O PHE E 19 N VAL B 18
SHEET 3 C 9 LEU H 17 VAL H 24 1 O PHE H 19 N VAL E 18
SHEET 4 C 9 LEU K 17 VAL K 24 1 O PHE K 19 N VAL H 18
SHEET 5 C 9 LEU N 17 VAL N 24 1 O PHE N 19 N VAL K 18
SHEET 6 C 9 LEU Q 17 VAL Q 24 1 O PHE Q 19 N VAL N 18
SHEET 7 C 9 LEU T 17 VAL T 24 1 O PHE T 19 N VAL Q 18
SHEET 8 C 9 LEU W 17 VAL W 24 1 O PHE W 19 N VAL T 18
SHEET 9 C 9 LEU Z 17 VAL Z 24 1 O PHE Z 19 N VAL W 18
SHEET 1 D 9 ILE B 31 VAL B 36 0
SHEET 2 D 9 ILE E 31 VAL E 36 1 O LEU E 34 N GLY B 33
SHEET 3 D 9 ILE H 31 VAL H 36 1 O LEU H 34 N GLY E 33
SHEET 4 D 9 ILE K 31 VAL K 36 1 O LEU K 34 N GLY H 33
SHEET 5 D 9 ILE N 31 VAL N 36 1 O LEU N 34 N GLY K 33
SHEET 6 D 9 ILE Q 31 VAL Q 36 1 O LEU Q 34 N GLY N 33
SHEET 7 D 9 ILE T 31 VAL T 36 1 O LEU T 34 N GLY Q 33
SHEET 8 D 9 ILE W 31 VAL W 36 1 O LEU W 34 N GLY T 33
SHEET 9 D 9 ILE Z 31 VAL Z 36 1 O LEU Z 34 N GLY W 33
SHEET 1 E 9 LEU C 17 VAL C 24 0
SHEET 2 E 9 LEU F 17 VAL F 24 1 O LEU F 17 N VAL C 18
SHEET 3 E 9 LEU I 17 VAL I 24 1 O LEU I 17 N VAL F 18
SHEET 4 E 9 LEU L 17 VAL L 24 1 O LEU L 17 N VAL I 18
SHEET 5 E 9 LEU O 17 VAL O 24 1 O LEU O 17 N VAL L 18
SHEET 6 E 9 LEU R 17 VAL R 24 1 O LEU R 17 N VAL O 18
SHEET 7 E 9 LEU U 17 VAL U 24 1 O LEU U 17 N VAL R 18
SHEET 8 E 9 LEU X 17 VAL X 24 1 O LEU X 17 N VAL U 18
SHEET 9 E 9 LEU a 17 VAL a 24 1 O LEU a 17 N VAL X 18
SHEET 1 F 9 ILE C 31 VAL C 36 0
SHEET 2 F 9 ILE F 31 VAL F 36 1 O LEU F 34 N GLY C 33
SHEET 3 F 9 ILE I 31 VAL I 36 1 O LEU I 34 N GLY F 33
SHEET 4 F 9 ILE L 31 VAL L 36 1 O LEU L 34 N GLY I 33
SHEET 5 F 9 ILE O 31 VAL O 36 1 O LEU O 34 N GLY L 33
SHEET 6 F 9 ILE R 31 VAL R 36 1 O LEU R 34 N GLY O 33
SHEET 7 F 9 ILE U 31 VAL U 36 1 O LEU U 34 N GLY R 33
SHEET 8 F 9 ILE X 31 VAL X 36 1 O LEU X 34 N GLY U 33
SHEET 9 F 9 ILE a 31 VAL a 36 1 O LEU a 34 N GLY X 33
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
