HEADER CHAPERONE 12-JUL-19 6PSI
TITLE STRUCTURAL BASIS FOR CLIENT RECOGNITION AND ACTIVITY OF HSP40
TITLE 2 CHAPERONES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHAPERONE PROTEIN DNAJ 2;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ALKALINE PHOSPHATASE;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: BACTERIAL ALKALINE PHOSPHATASE;
COMPND 9 EC: 3.1.3.1;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS (STRAIN HB8 / ATCC 27634 /
SOURCE 3 DSM 579);
SOURCE 4 ORGANISM_TAXID: 300852;
SOURCE 5 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 6 GENE: DNAJ2, TTHA1489;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 12 ORGANISM_TAXID: 562;
SOURCE 13 GENE: PHOA, ACU57_12080, AUQ13_18595, BANRA_02023, BANRA_03586,
SOURCE 14 BET08_14335, BHF46_20915, BUE81_15475, C4J69_09555, C5N07_12695,
SOURCE 15 CA593_01230, D0X26_07375, D3821_12940, DNQ41_05820, EAI52_02910,
SOURCE 16 EC3234A_4C00530, EC3426_01222, ECTO6_03716, ED648_16735,
SOURCE 17 EEP23_01005, EL75_3367, EL79_3462, EL80_3416, NCTC13462_01945,
SOURCE 18 NCTC9037_03964, NCTC9062_04458, RK56_026750, SAMEA3753300_00450,
SOURCE 19 UN91_18770;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS CLIENT RECOGNITION, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.JIANG,P.ROSSI,C.G.KALODIMOS
REVDAT 3 01-JAN-20 6PSI 1 REMARK
REVDAT 2 23-OCT-19 6PSI 1 JRNL
REVDAT 1 18-SEP-19 6PSI 0
JRNL AUTH Y.JIANG,P.ROSSI,C.G.KALODIMOS
JRNL TITL STRUCTURAL BASIS FOR CLIENT RECOGNITION AND ACTIVITY OF
JRNL TITL 2 HSP40 CHAPERONES.
JRNL REF SCIENCE V. 365 1313 2019
JRNL REFN ESSN 1095-9203
JRNL PMID 31604242
JRNL DOI 10.1126/SCIENCE.AAX1280
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6PSI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1000242994.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 25
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 100
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM [U-100% 13C; U-100% 15N; U
REMARK 210 -80% 2H] PHOA_DNAJ, 75 MM
REMARK 210 POTASSIUM CHLORIDE, 20 MM
REMARK 210 POTASSIUM PHOSPHATE, 0.04 %
REMARK 210 SODIUM AZIDE, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-13C HSQC; 2D 1H-15N HSQC;
REMARK 210 2D 1H-13C HMQC; 3D 1H-13C NOESY;
REMARK 210 3D 1H-15N NOESY; 3D HNCACB; 3D
REMARK 210 HNCO; 3D CCH-SOFAST HMQC-NOESY-
REMARK 210 HMQC; 3D NCH-SOFAST HMQC-NOESY-
REMARK 210 HMQC; 3D HCH-SOFASTNOESY-HMQC;
REMARK 210 3D HNH-SOFASTNOESY-HMQC; 3D CNH-
REMARK 210 SOFAST HMQC-NOESY-HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE NEO
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, PINE, SPARKY, NMRPIPE,
REMARK 210 TALOS, TOPSPIN, PSVS
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 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 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 ALA A 3 78.55 -66.78
REMARK 500 1 LYS A 4 92.89 -35.99
REMARK 500 1 ARG A 15 21.02 -74.73
REMARK 500 1 TYR A 33 31.25 -96.85
REMARK 500 1 ASN A 38 71.91 -100.54
REMARK 500 1 THR A 71 -59.27 -143.29
REMARK 500 1 PRO A 80 84.45 -60.39
REMARK 500 1 PHE A 85 60.16 -155.98
REMARK 500 1 SER A 86 86.05 -31.93
REMARK 500 1 LEU A 105 38.03 -66.02
REMARK 500 1 PHE A 106 -102.81 55.78
REMARK 500 1 ARG A 111 -31.46 75.80
REMARK 500 1 ASP A 173 89.04 -69.50
REMARK 500 1 PRO A 182 44.01 -75.92
REMARK 500 1 PRO A 184 12.30 -64.34
REMARK 500 1 GLN A 191 -4.79 -147.68
REMARK 500 1 GLU A 259 -70.26 58.25
REMARK 500 1 TYR A 276 -76.66 -77.90
REMARK 500 1 GLN B 3 -72.34 -67.78
REMARK 500 1 SER B 4 -65.87 64.88
REMARK 500 1 ALA B 7 -158.24 -130.35
REMARK 500 1 LEU B 10 -22.46 74.71
REMARK 500 1 THR B 23 83.65 70.69
REMARK 500 1 PRO B 24 33.47 -91.08
REMARK 500 1 MET B 26 -48.24 -164.33
REMARK 500 1 ASP B 37 -83.26 60.51
REMARK 500 1 PRO B 41 89.10 -65.97
REMARK 500 1 ALA B 44 -168.99 58.26
REMARK 500 1 GLN B 51 128.85 66.80
REMARK 500 1 ALA B 53 169.31 63.65
REMARK 500 1 ALA B 54 -16.82 72.76
REMARK 500 1 ARG B 56 -45.49 78.10
REMARK 500 1 ASP B 57 -72.21 -69.38
REMARK 500 1 LEU B 59 95.17 57.94
REMARK 500 1 LYS B 62 141.38 75.11
REMARK 500 1 PRO B 63 90.76 -69.09
REMARK 500 1 ALA B 64 -48.19 76.32
REMARK 500 1 LYS B 65 -73.28 71.89
REMARK 500 1 ASN B 66 -102.03 54.05
REMARK 500 1 LEU B 69 -62.89 72.30
REMARK 500 1 LEU B 70 47.86 -84.19
REMARK 500 1 ASP B 73 -62.50 79.00
REMARK 500 1 GLU B 79 -71.05 68.55
REMARK 500 1 ALA B 87 -34.93 164.03
REMARK 500 1 GLU B 88 -78.04 66.26
REMARK 500 1 ALA B 90 113.18 -176.73
REMARK 500 1 PHE B 93 -75.95 62.73
REMARK 500 1 PHE B 94 -48.78 -143.66
REMARK 500 1 ALA B 99 -40.40 -142.84
REMARK 500 1 THR B 103 78.47 65.35
REMARK 500
REMARK 500 THIS ENTRY HAS 4179 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6PPT RELATED DB: PDB
REMARK 900 RELATED ID: 30638 RELATED DB: BMRB
REMARK 900 STRUCTURAL BASIS FOR CLIENT RECOGNITION AND ACTIVITY OF HSP40
REMARK 900 CHAPERONES
DBREF 6PSI A 1 280 UNP Q56237 DNAJ2_THET8 1 280
DBREF1 6PSI B 1 471 UNP A0A086VD57_ECOLX
DBREF2 6PSI B A0A086VD57 1 471
DBREF 6PSI C 1 280 UNP Q56237 DNAJ2_THET8 1 280
SEQRES 1 A 280 MET ALA ALA LYS LYS ASP TYR TYR ALA ILE LEU GLY VAL
SEQRES 2 A 280 PRO ARG ASN ALA THR GLN GLU GLU ILE LYS ARG ALA TYR
SEQRES 3 A 280 LYS ARG LEU ALA ARG GLN TYR HIS PRO ASP VAL ASN LYS
SEQRES 4 A 280 SER PRO GLU ALA GLU GLU LYS PHE LYS GLU ILE ASN GLU
SEQRES 5 A 280 ALA TYR ALA VAL LEU SER ASP PRO GLU LYS ARG ARG ILE
SEQRES 6 A 280 TYR ASP THR TYR GLY THR THR GLU ALA PRO PRO PRO PRO
SEQRES 7 A 280 PRO PRO GLY GLY TYR ASP PHE SER GLY PHE ASP VAL GLU
SEQRES 8 A 280 ASP PHE SER GLU PHE PHE GLN GLU LEU PHE GLY PRO GLY
SEQRES 9 A 280 LEU PHE GLY GLY PHE GLY ARG ARG SER ARG LYS GLY ARG
SEQRES 10 A 280 ASP LEU ARG ALA GLU LEU PRO LEU THR LEU GLU GLU ALA
SEQRES 11 A 280 PHE HIS GLY GLY GLU ARG VAL VAL GLU VAL ALA GLY ARG
SEQRES 12 A 280 ARG VAL SER VAL ARG ILE PRO PRO GLY VAL ARG GLU GLY
SEQRES 13 A 280 SER VAL ILE ARG VAL PRO GLY MET GLY GLY GLN GLY ASN
SEQRES 14 A 280 PRO PRO GLY ASP LEU LEU LEU VAL VAL ARG LEU LEU PRO
SEQRES 15 A 280 HIS PRO VAL PHE ARG LEU GLU GLY GLN ASP LEU TYR ALA
SEQRES 16 A 280 THR LEU ASP VAL PRO ALA PRO ILE ALA VAL VAL GLY GLY
SEQRES 17 A 280 LYS VAL ARG ALA MET THR LEU GLU GLY PRO VAL GLU VAL
SEQRES 18 A 280 ALA VAL PRO PRO ARG THR GLN ALA GLY ARG LYS LEU ARG
SEQRES 19 A 280 LEU LYS GLY LYS GLY PHE PRO GLY PRO ALA GLY ARG GLY
SEQRES 20 A 280 ASP LEU TYR LEU GLU VAL ARG ILE THR ILE PRO GLU ARG
SEQRES 21 A 280 LEU THR PRO GLU GLU GLU ALA LEU TRP LYS LYS LEU ALA
SEQRES 22 A 280 GLU ALA TYR TYR ALA ARG ALA
SEQRES 1 B 471 MET LYS GLN SER THR ILE ALA LEU ALA LEU LEU PRO LEU
SEQRES 2 B 471 LEU PHE THR PRO VAL THR LYS ALA ARG THR PRO GLU MET
SEQRES 3 B 471 PRO VAL LEU GLU ASN ARG ALA ALA GLN GLY ASP ILE THR
SEQRES 4 B 471 ALA PRO GLY GLY ALA ARG ARG LEU THR GLY ASP GLN THR
SEQRES 5 B 471 ALA ALA LEU ARG ASP SER LEU SER ASP LYS PRO ALA LYS
SEQRES 6 B 471 ASN ILE ILE LEU LEU ILE GLY ASP GLY MET GLY ASP SER
SEQRES 7 B 471 GLU ILE THR ALA ALA ARG ASN TYR ALA GLU GLY ALA GLY
SEQRES 8 B 471 GLY PHE PHE LYS GLY ILE ASP ALA LEU PRO LEU THR GLY
SEQRES 9 B 471 GLN TYR THR HIS TYR ALA LEU ASN LYS LYS THR GLY LYS
SEQRES 10 B 471 PRO ASP TYR VAL THR ASP SER ALA ALA SER ALA THR ALA
SEQRES 11 B 471 TRP SER THR GLY VAL LYS THR TYR ASN GLY ALA LEU GLY
SEQRES 12 B 471 VAL ASP ILE HIS GLU LYS ASP HIS PRO THR ILE LEU GLU
SEQRES 13 B 471 MET ALA LYS ALA ALA GLY LEU ALA THR GLY ASN VAL SER
SEQRES 14 B 471 THR ALA GLU LEU GLN ASP ALA THR PRO ALA ALA LEU VAL
SEQRES 15 B 471 ALA HIS VAL THR SER ARG LYS CYS TYR GLY PRO SER ALA
SEQRES 16 B 471 THR SER GLU LYS CYS PRO GLY ASN ALA LEU GLU LYS GLY
SEQRES 17 B 471 GLY LYS GLY SER ILE THR GLU GLN LEU LEU ASN ALA ARG
SEQRES 18 B 471 ALA ASP VAL THR LEU GLY GLY GLY ALA LYS THR PHE ALA
SEQRES 19 B 471 GLU THR ALA THR ALA GLY GLU TRP GLN GLY LYS THR LEU
SEQRES 20 B 471 ARG GLU GLN ALA GLN ALA ARG GLY TYR GLN LEU VAL SER
SEQRES 21 B 471 ASP ALA ALA SER LEU ASN SER VAL THR GLU ALA ASN GLN
SEQRES 22 B 471 GLN LYS PRO LEU LEU GLY LEU PHE ALA ASP GLY ASN MET
SEQRES 23 B 471 PRO VAL ARG TRP LEU GLY PRO LYS ALA THR TYR HIS GLY
SEQRES 24 B 471 ASN ILE ASP LYS PRO ALA VAL THR CYS THR PRO ASN PRO
SEQRES 25 B 471 GLN ARG ASN ASP SER VAL PRO THR LEU ALA GLN MET THR
SEQRES 26 B 471 ASP LYS ALA ILE GLU LEU LEU SER LYS ASN GLU LYS GLY
SEQRES 27 B 471 PHE PHE LEU GLN VAL GLU GLY ALA SER ILE ASP LYS GLN
SEQRES 28 B 471 ASP HIS ALA ALA ASN PRO CYS GLY GLN ILE GLY GLU THR
SEQRES 29 B 471 VAL ASP LEU ASP GLU ALA VAL GLN ARG ALA LEU GLU PHE
SEQRES 30 B 471 ALA LYS LYS GLU GLY ASN THR LEU VAL ILE VAL THR ALA
SEQRES 31 B 471 ASP HIS ALA HIS ALA SER GLN ILE VAL ALA PRO ASP THR
SEQRES 32 B 471 LYS ALA PRO GLY LEU THR GLN ALA LEU ASN THR LYS ASP
SEQRES 33 B 471 GLY ALA VAL MET VAL MET SER TYR GLY ASN SER GLU GLU
SEQRES 34 B 471 ASP SER GLN GLU HIS THR GLY SER GLN LEU ARG ILE ALA
SEQRES 35 B 471 ALA TYR GLY PRO HIS ALA ALA ASN VAL VAL GLY LEU THR
SEQRES 36 B 471 ASP GLN THR ASP LEU PHE TYR THR MET LYS ALA ALA LEU
SEQRES 37 B 471 GLY LEU LYS
SEQRES 1 C 280 MET ALA ALA LYS LYS ASP TYR TYR ALA ILE LEU GLY VAL
SEQRES 2 C 280 PRO ARG ASN ALA THR GLN GLU GLU ILE LYS ARG ALA TYR
SEQRES 3 C 280 LYS ARG LEU ALA ARG GLN TYR HIS PRO ASP VAL ASN LYS
SEQRES 4 C 280 SER PRO GLU ALA GLU GLU LYS PHE LYS GLU ILE ASN GLU
SEQRES 5 C 280 ALA TYR ALA VAL LEU SER ASP PRO GLU LYS ARG ARG ILE
SEQRES 6 C 280 TYR ASP THR TYR GLY THR THR GLU ALA PRO PRO PRO PRO
SEQRES 7 C 280 PRO PRO GLY GLY TYR ASP PHE SER GLY PHE ASP VAL GLU
SEQRES 8 C 280 ASP PHE SER GLU PHE PHE GLN GLU LEU PHE GLY PRO GLY
SEQRES 9 C 280 LEU PHE GLY GLY PHE GLY ARG ARG SER ARG LYS GLY ARG
SEQRES 10 C 280 ASP LEU ARG ALA GLU LEU PRO LEU THR LEU GLU GLU ALA
SEQRES 11 C 280 PHE HIS GLY GLY GLU ARG VAL VAL GLU VAL ALA GLY ARG
SEQRES 12 C 280 ARG VAL SER VAL ARG ILE PRO PRO GLY VAL ARG GLU GLY
SEQRES 13 C 280 SER VAL ILE ARG VAL PRO GLY MET GLY GLY GLN GLY ASN
SEQRES 14 C 280 PRO PRO GLY ASP LEU LEU LEU VAL VAL ARG LEU LEU PRO
SEQRES 15 C 280 HIS PRO VAL PHE ARG LEU GLU GLY GLN ASP LEU TYR ALA
SEQRES 16 C 280 THR LEU ASP VAL PRO ALA PRO ILE ALA VAL VAL GLY GLY
SEQRES 17 C 280 LYS VAL ARG ALA MET THR LEU GLU GLY PRO VAL GLU VAL
SEQRES 18 C 280 ALA VAL PRO PRO ARG THR GLN ALA GLY ARG LYS LEU ARG
SEQRES 19 C 280 LEU LYS GLY LYS GLY PHE PRO GLY PRO ALA GLY ARG GLY
SEQRES 20 C 280 ASP LEU TYR LEU GLU VAL ARG ILE THR ILE PRO GLU ARG
SEQRES 21 C 280 LEU THR PRO GLU GLU GLU ALA LEU TRP LYS LYS LEU ALA
SEQRES 22 C 280 GLU ALA TYR TYR ALA ARG ALA
HELIX 1 AA1 ASP A 6 GLY A 12 1 7
HELIX 2 AA2 THR A 18 TYR A 33 1 16
HELIX 3 AA3 SER A 40 ASP A 59 1 20
HELIX 4 AA4 ASP A 59 TYR A 69 1 11
HELIX 5 AA5 ASP A 89 PHE A 93 5 5
HELIX 6 AA6 SER A 94 PHE A 101 1 8
HELIX 7 AA7 GLY A 102 LEU A 105 5 4
HELIX 8 AA8 THR A 126 GLY A 133 1 8
HELIX 9 AA9 ALA A 201 GLY A 207 1 7
HELIX 10 AB1 THR A 262 ALA A 278 1 17
HELIX 11 AB2 GLU B 79 ARG B 84 1 6
HELIX 12 AB3 GLY B 192 SER B 197 1 6
HELIX 13 AB4 ALA B 222 LEU B 226 5 5
HELIX 14 AB5 ASP B 368 GLN B 372 5 5
HELIX 15 AB6 HIS B 434 GLN B 438 5 5
HELIX 16 AB7 ASP C 6 GLY C 12 1 7
HELIX 17 AB8 THR C 18 TYR C 33 1 16
HELIX 18 AB9 SER C 40 SER C 58 1 19
HELIX 19 AC1 ASP C 59 TYR C 69 1 11
HELIX 20 AC2 ASP C 89 PHE C 93 5 5
HELIX 21 AC3 SER C 94 PHE C 101 1 8
HELIX 22 AC4 GLY C 102 LEU C 105 5 4
HELIX 23 AC5 LEU C 127 GLY C 133 1 7
HELIX 24 AC6 ALA C 201 GLY C 207 1 7
HELIX 25 AC7 THR C 262 ALA C 278 1 17
SHEET 1 AA1 3 LEU A 119 LEU A 125 0
SHEET 2 AA1 3 LEU A 174 LEU A 180 1 O VAL A 177 N ALA A 121
SHEET 3 AA1 3 VAL A 158 VAL A 161 -1 N ILE A 159 O LEU A 176
SHEET 1 AA2 2 GLY A 134 VAL A 140 0
SHEET 2 AA2 2 ARG A 143 ILE A 149 -1 O VAL A 145 N VAL A 138
SHEET 1 AA3 4 LEU A 193 PRO A 200 0
SHEET 2 AA3 4 LEU A 249 THR A 256 1 O GLU A 252 N LEU A 197
SHEET 3 AA3 4 LYS A 232 LYS A 236 -1 N LEU A 235 O LEU A 249
SHEET 4 AA3 4 ARG B 440 ILE B 441 -1 O ARG B 440 N LYS A 236
SHEET 1 AA4 2 LYS A 209 ALA A 212 0
SHEET 2 AA4 2 VAL A 219 ALA A 222 -1 O VAL A 219 N ALA A 212
SHEET 1 AA5 2 PRO A 241 GLY A 242 0
SHEET 2 AA5 2 GLY A 245 ARG A 246 -1 O GLY A 245 N GLY A 242
SHEET 1 AA6 3 LEU C 119 LEU C 125 0
SHEET 2 AA6 3 LEU C 174 LEU C 180 1 O ARG C 179 N LEU C 123
SHEET 3 AA6 3 VAL C 158 VAL C 161 -1 N ILE C 159 O LEU C 176
SHEET 1 AA7 2 GLY C 134 VAL C 140 0
SHEET 2 AA7 2 ARG C 143 ILE C 149 -1 O VAL C 145 N VAL C 138
SHEET 1 AA8 3 LEU C 193 PRO C 200 0
SHEET 2 AA8 3 LEU C 249 THR C 256 1 O GLU C 252 N ALA C 195
SHEET 3 AA8 3 LYS C 232 LEU C 235 -1 N LEU C 235 O LEU C 249
SHEET 1 AA9 2 LYS C 209 THR C 214 0
SHEET 2 AA9 2 GLY C 217 ALA C 222 -1 O VAL C 221 N VAL C 210
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
