HEADER TRANSFERASE 24-OCT-16 5TQY
TITLE CRYOEM RECONSTRUCTION OF HUMAN IKK1, CLOSED CONFORMATION 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INHIBITOR OF NUCLEAR FACTOR KAPPA-B KINASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IKAPPAB KINASE, CONSERVED HELIX-LOOP-HELIX UBIQUITOUS
COMPND 5 KINASE, I-KAPPA-B KINASE 1, IKK1, NUCLEAR FACTOR NF-KAPPA-B INHIBITOR
COMPND 6 KINASE ALPHA, NFKBIKA, TRANSCRIPTION FACTOR 16, TCF-16;
COMPND 7 EC: 2.7.11.10;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CHUK, IKKA, TCF16;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTA
KEYWDS KINASE, CONSERVED HELIX-LOOP-HELIX, TRANSCRIPTION, ONCOGENE,
KEYWDS 2 TRANSFERASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR D.LYUMKIS,G.GHOSH,S.POLLEY,T.BISWATH,D.HUANG,D.O.PASSOS
REVDAT 6 13-MAR-24 5TQY 1 REMARK
REVDAT 5 04-DEC-19 5TQY 1 REMARK
REVDAT 4 18-JUL-18 5TQY 1 REMARK
REVDAT 3 13-SEP-17 5TQY 1 REMARK
REVDAT 2 30-NOV-16 5TQY 1 JRNL
REVDAT 1 09-NOV-16 5TQY 0
JRNL AUTH S.POLLEY,D.O.PASSOS,D.B.HUANG,M.C.MULERO,A.MAZUMDER,
JRNL AUTH 2 T.BISWAS,I.M.VERMA,D.LYUMKIS,G.GHOSH
JRNL TITL STRUCTURAL BASIS FOR THE ACTIVATION OF IKK1/ ALPHA.
JRNL REF CELL REP V. 17 1907 2016
JRNL REFN ESSN 2211-1247
JRNL PMID 27851956
JRNL DOI 10.1016/J.CELREP.2016.10.067
REMARK 2
REMARK 2 RESOLUTION. 5.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : FINDEM, LEGINON, CTFFIND, ROSETTA,
REMARK 3 PHENIX, RELION, FREALIGN, FREALIGN,
REMARK 3 FREALIGN
REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : FSC 0.5
REMARK 3 OVERALL ANISOTROPIC B VALUE : 340.000
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 5.200
REMARK 3 NUMBER OF PARTICLES : 23505
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 5TQY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224662.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : INHIBITOR OF KAPPAB KINASE 1
REMARK 245 DIMER
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.50
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : SAMPLE CONTAINING IKK1 DIMERS
REMARK 245 IN SEC BUFFER WAS APPLIED ONTO
REMARK 245 FRESHLY PLASMA-TREATED (6
REMARK 245 SECONDS, GATAN SOLARUS PLASMA
REMARK 245 CLEANER) HOLEY CARBON C-FLAT
REMARK 245 GRIDS (PROTOCHIPS), ADSORBED
REMARK 245 FOR 30 SECONDS, AND THEN
REMARK 245 PLUNGED INTO LIQUID ETHANE
REMARK 245 USING A MANUAL CRYO-PLUNGER IN
REMARK 245 AN AMBIENT ENVIRONMENT OF 4
REMARK 245 DEGREES C.
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : DIMER
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 2918
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 22500
REMARK 245 CALIBRATED MAGNIFICATION : 38167
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: DIMERIC
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 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 ASP A 6
REMARK 465 PRO A 7
REMARK 465 GLU A 8
REMARK 465 PHE A 9
REMARK 465 GLY A 10
REMARK 465 ALA A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 68
REMARK 465 ASN A 69
REMARK 465 HIS A 70
REMARK 465 ALA A 71
REMARK 465 ASN A 72
REMARK 465 VAL A 73
REMARK 465 VAL A 74
REMARK 465 LYS A 75
REMARK 465 ALA A 76
REMARK 465 CYS A 77
REMARK 465 ASP A 78
REMARK 465 VAL A 79
REMARK 465 PRO A 80
REMARK 465 GLU A 81
REMARK 465 GLU A 82
REMARK 465 LEU A 83
REMARK 465 ASN A 84
REMARK 465 ILE A 85
REMARK 465 LEU A 86
REMARK 465 ILE A 87
REMARK 465 HIS A 88
REMARK 465 ASP A 89
REMARK 465 VAL A 90
REMARK 465 PRO A 91
REMARK 465 LEU A 92
REMARK 465 LEU A 93
REMARK 465 ALA A 94
REMARK 465 MET A 95
REMARK 465 GLU A 96
REMARK 465 TYR A 97
REMARK 465 CYS A 98
REMARK 465 SER A 99
REMARK 465 GLY A 100
REMARK 465 GLY A 101
REMARK 465 ASP A 102
REMARK 465 ASP A 165
REMARK 465 LEU A 166
REMARK 465 GLY A 167
REMARK 465 TYR A 168
REMARK 465 ALA A 169
REMARK 465 LYS A 170
REMARK 465 ASP A 171
REMARK 465 VAL A 172
REMARK 465 ASP A 173
REMARK 465 GLN A 174
REMARK 465 GLY A 175
REMARK 465 GLU A 176
REMARK 465 LEU A 177
REMARK 465 CYS A 178
REMARK 465 THR A 179
REMARK 465 GLU A 180
REMARK 465 PHE A 181
REMARK 465 VAL A 182
REMARK 465 GLY A 183
REMARK 465 ALA A 368
REMARK 465 SER A 369
REMARK 465 GLN A 370
REMARK 465 CYS A 371
REMARK 465 VAL A 372
REMARK 465 LEU A 373
REMARK 465 ASP A 374
REMARK 465 GLY A 375
REMARK 465 VAL A 376
REMARK 465 ARG A 377
REMARK 465 GLY A 378
REMARK 465 CYS A 379
REMARK 465 ASP A 380
REMARK 465 SER A 381
REMARK 465 TYR A 382
REMARK 465 ASP B 6
REMARK 465 PRO B 7
REMARK 465 GLU B 8
REMARK 465 PHE B 9
REMARK 465 GLY B 10
REMARK 465 ALA B 11
REMARK 465 GLY B 12
REMARK 465 GLY B 13
REMARK 465 LEU B 68
REMARK 465 ASN B 69
REMARK 465 HIS B 70
REMARK 465 ALA B 71
REMARK 465 ASN B 72
REMARK 465 VAL B 73
REMARK 465 VAL B 74
REMARK 465 LYS B 75
REMARK 465 ALA B 76
REMARK 465 CYS B 77
REMARK 465 ASP B 78
REMARK 465 VAL B 79
REMARK 465 PRO B 80
REMARK 465 GLU B 81
REMARK 465 GLU B 82
REMARK 465 LEU B 83
REMARK 465 ASN B 84
REMARK 465 ILE B 85
REMARK 465 LEU B 86
REMARK 465 ILE B 87
REMARK 465 HIS B 88
REMARK 465 ASP B 89
REMARK 465 VAL B 90
REMARK 465 PRO B 91
REMARK 465 LEU B 92
REMARK 465 LEU B 93
REMARK 465 ALA B 94
REMARK 465 MET B 95
REMARK 465 GLU B 96
REMARK 465 TYR B 97
REMARK 465 CYS B 98
REMARK 465 SER B 99
REMARK 465 GLY B 100
REMARK 465 GLY B 101
REMARK 465 ASP B 102
REMARK 465 ASP B 165
REMARK 465 LEU B 166
REMARK 465 GLY B 167
REMARK 465 TYR B 168
REMARK 465 ALA B 169
REMARK 465 LYS B 170
REMARK 465 ASP B 171
REMARK 465 VAL B 172
REMARK 465 ASP B 173
REMARK 465 GLN B 174
REMARK 465 GLY B 175
REMARK 465 GLU B 176
REMARK 465 LEU B 177
REMARK 465 CYS B 178
REMARK 465 THR B 179
REMARK 465 GLU B 180
REMARK 465 PHE B 181
REMARK 465 VAL B 182
REMARK 465 GLY B 183
REMARK 465 ALA B 368
REMARK 465 SER B 369
REMARK 465 GLN B 370
REMARK 465 CYS B 371
REMARK 465 VAL B 372
REMARK 465 LEU B 373
REMARK 465 ASP B 374
REMARK 465 GLY B 375
REMARK 465 VAL B 376
REMARK 465 ARG B 377
REMARK 465 GLY B 378
REMARK 465 CYS B 379
REMARK 465 ASP B 380
REMARK 465 SER B 381
REMARK 465 TYR B 382
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 GLY A 289 C PRO A 290 N 0.199
REMARK 500 GLY B 289 C PRO B 290 N 0.198
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 ASP A 144 45.55 -140.16
REMARK 500 ASN A 262 -166.04 -100.33
REMARK 500 PRO A 290 77.30 -67.88
REMARK 500 ASP A 331 24.42 -146.32
REMARK 500 THR A 392 -65.36 -93.81
REMARK 500 ALA A 522 50.13 -119.55
REMARK 500 ASP B 144 45.63 -140.11
REMARK 500 ASN B 262 -166.17 -100.30
REMARK 500 PRO B 290 77.33 -67.85
REMARK 500 ASP B 331 24.48 -146.32
REMARK 500 THR B 392 -65.32 -93.77
REMARK 500 ALA B 522 50.25 -119.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-8438 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-8436 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-8437 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-8439 RELATED DB: EMDB
REMARK 900 RELATED ID: 5TQW RELATED DB: PDB
REMARK 900 RELATED ID: 5TQX RELATED DB: PDB
DBREF 5TQY A 10 660 UNP O15111 IKKA_HUMAN 10 660
DBREF 5TQY B 10 660 UNP O15111 IKKA_HUMAN 10 660
SEQADV 5TQY ASP A 6 UNP O15111 EXPRESSION TAG
SEQADV 5TQY PRO A 7 UNP O15111 EXPRESSION TAG
SEQADV 5TQY GLU A 8 UNP O15111 EXPRESSION TAG
SEQADV 5TQY PHE A 9 UNP O15111 EXPRESSION TAG
SEQADV 5TQY GLU A 176 UNP O15111 SER 176 ENGINEERED MUTATION
SEQADV 5TQY GLU A 180 UNP O15111 SER 180 ENGINEERED MUTATION
SEQADV 5TQY ILE A 268 UNP O15111 VAL 268 VARIANT
SEQADV 5TQY ASP B 6 UNP O15111 EXPRESSION TAG
SEQADV 5TQY PRO B 7 UNP O15111 EXPRESSION TAG
SEQADV 5TQY GLU B 8 UNP O15111 EXPRESSION TAG
SEQADV 5TQY PHE B 9 UNP O15111 EXPRESSION TAG
SEQADV 5TQY GLU B 176 UNP O15111 SER 176 ENGINEERED MUTATION
SEQADV 5TQY GLU B 180 UNP O15111 SER 180 ENGINEERED MUTATION
SEQADV 5TQY ILE B 268 UNP O15111 VAL 268 VARIANT
SEQRES 1 A 655 ASP PRO GLU PHE GLY ALA GLY GLY PRO TRP GLU MET ARG
SEQRES 2 A 655 GLU ARG LEU GLY THR GLY GLY PHE GLY ASN VAL CYS LEU
SEQRES 3 A 655 TYR GLN HIS ARG GLU LEU ASP LEU LYS ILE ALA ILE LYS
SEQRES 4 A 655 SER CYS ARG LEU GLU LEU SER THR LYS ASN ARG GLU ARG
SEQRES 5 A 655 TRP CYS HIS GLU ILE GLN ILE MET LYS LYS LEU ASN HIS
SEQRES 6 A 655 ALA ASN VAL VAL LYS ALA CYS ASP VAL PRO GLU GLU LEU
SEQRES 7 A 655 ASN ILE LEU ILE HIS ASP VAL PRO LEU LEU ALA MET GLU
SEQRES 8 A 655 TYR CYS SER GLY GLY ASP LEU ARG LYS LEU LEU ASN LYS
SEQRES 9 A 655 PRO GLU ASN CYS CYS GLY LEU LYS GLU SER GLN ILE LEU
SEQRES 10 A 655 SER LEU LEU SER ASP ILE GLY SER GLY ILE ARG TYR LEU
SEQRES 11 A 655 HIS GLU ASN LYS ILE ILE HIS ARG ASP LEU LYS PRO GLU
SEQRES 12 A 655 ASN ILE VAL LEU GLN ASP VAL GLY GLY LYS ILE ILE HIS
SEQRES 13 A 655 LYS ILE ILE ASP LEU GLY TYR ALA LYS ASP VAL ASP GLN
SEQRES 14 A 655 GLY GLU LEU CYS THR GLU PHE VAL GLY THR LEU GLN TYR
SEQRES 15 A 655 LEU ALA PRO GLU LEU PHE GLU ASN LYS PRO TYR THR ALA
SEQRES 16 A 655 THR VAL ASP TYR TRP SER PHE GLY THR MET VAL PHE GLU
SEQRES 17 A 655 CYS ILE ALA GLY TYR ARG PRO PHE LEU HIS HIS LEU GLN
SEQRES 18 A 655 PRO PHE THR TRP HIS GLU LYS ILE LYS LYS LYS ASP PRO
SEQRES 19 A 655 LYS CYS ILE PHE ALA CYS GLU GLU MET SER GLY GLU VAL
SEQRES 20 A 655 ARG PHE SER SER HIS LEU PRO GLN PRO ASN SER LEU CYS
SEQRES 21 A 655 SER LEU ILE VAL GLU PRO MET GLU ASN TRP LEU GLN LEU
SEQRES 22 A 655 MET LEU ASN TRP ASP PRO GLN GLN ARG GLY GLY PRO VAL
SEQRES 23 A 655 ASP LEU THR LEU LYS GLN PRO ARG CYS PHE VAL LEU MET
SEQRES 24 A 655 ASP HIS ILE LEU ASN LEU LYS ILE VAL HIS ILE LEU ASN
SEQRES 25 A 655 MET THR SER ALA LYS ILE ILE SER PHE LEU LEU PRO PRO
SEQRES 26 A 655 ASP GLU SER LEU HIS SER LEU GLN SER ARG ILE GLU ARG
SEQRES 27 A 655 GLU THR GLY ILE ASN THR GLY SER GLN GLU LEU LEU SER
SEQRES 28 A 655 GLU THR GLY ILE SER LEU ASP PRO ARG LYS PRO ALA SER
SEQRES 29 A 655 GLN CYS VAL LEU ASP GLY VAL ARG GLY CYS ASP SER TYR
SEQRES 30 A 655 MET VAL TYR LEU PHE ASP LYS SER LYS THR VAL TYR GLU
SEQRES 31 A 655 GLY PRO PHE ALA SER ARG SER LEU SER ASP CYS VAL ASN
SEQRES 32 A 655 TYR ILE VAL GLN ASP SER LYS ILE GLN LEU PRO ILE ILE
SEQRES 33 A 655 GLN LEU ARG LYS VAL TRP ALA GLU ALA VAL HIS TYR VAL
SEQRES 34 A 655 SER GLY LEU LYS GLU ASP TYR SER ARG LEU PHE GLN GLY
SEQRES 35 A 655 GLN ARG ALA ALA MET LEU SER LEU LEU ARG TYR ASN ALA
SEQRES 36 A 655 ASN LEU THR LYS MET LYS ASN THR LEU ILE SER ALA SER
SEQRES 37 A 655 GLN GLN LEU LYS ALA LYS LEU GLU PHE PHE HIS LYS SER
SEQRES 38 A 655 ILE GLN LEU ASP LEU GLU ARG TYR SER GLU GLN MET THR
SEQRES 39 A 655 TYR GLY ILE SER SER GLU LYS MET LEU LYS ALA TRP LYS
SEQRES 40 A 655 GLU MET GLU GLU LYS ALA ILE HIS TYR ALA GLU VAL GLY
SEQRES 41 A 655 VAL ILE GLY TYR LEU GLU ASP GLN ILE MET SER LEU HIS
SEQRES 42 A 655 ALA GLU ILE MET GLU LEU GLN LYS SER PRO TYR GLY ARG
SEQRES 43 A 655 ARG GLN GLY ASP LEU MET GLU SER LEU GLU GLN ARG ALA
SEQRES 44 A 655 ILE ASP LEU TYR LYS GLN LEU LYS HIS ARG PRO SER ASP
SEQRES 45 A 655 HIS SER TYR SER ASP SER THR GLU MET VAL LYS ILE ILE
SEQRES 46 A 655 VAL HIS THR VAL GLN SER GLN ASP ARG VAL LEU LYS GLU
SEQRES 47 A 655 LEU PHE GLY HIS LEU SER LYS LEU LEU GLY CYS LYS GLN
SEQRES 48 A 655 LYS ILE ILE ASP LEU LEU PRO LYS VAL GLU VAL ALA LEU
SEQRES 49 A 655 SER ASN ILE LYS GLU ALA ASP ASN THR VAL MET PHE MET
SEQRES 50 A 655 GLN GLY LYS ARG GLN LYS GLU ILE TRP HIS LEU LEU LYS
SEQRES 51 A 655 ILE ALA CYS THR GLN
SEQRES 1 B 655 ASP PRO GLU PHE GLY ALA GLY GLY PRO TRP GLU MET ARG
SEQRES 2 B 655 GLU ARG LEU GLY THR GLY GLY PHE GLY ASN VAL CYS LEU
SEQRES 3 B 655 TYR GLN HIS ARG GLU LEU ASP LEU LYS ILE ALA ILE LYS
SEQRES 4 B 655 SER CYS ARG LEU GLU LEU SER THR LYS ASN ARG GLU ARG
SEQRES 5 B 655 TRP CYS HIS GLU ILE GLN ILE MET LYS LYS LEU ASN HIS
SEQRES 6 B 655 ALA ASN VAL VAL LYS ALA CYS ASP VAL PRO GLU GLU LEU
SEQRES 7 B 655 ASN ILE LEU ILE HIS ASP VAL PRO LEU LEU ALA MET GLU
SEQRES 8 B 655 TYR CYS SER GLY GLY ASP LEU ARG LYS LEU LEU ASN LYS
SEQRES 9 B 655 PRO GLU ASN CYS CYS GLY LEU LYS GLU SER GLN ILE LEU
SEQRES 10 B 655 SER LEU LEU SER ASP ILE GLY SER GLY ILE ARG TYR LEU
SEQRES 11 B 655 HIS GLU ASN LYS ILE ILE HIS ARG ASP LEU LYS PRO GLU
SEQRES 12 B 655 ASN ILE VAL LEU GLN ASP VAL GLY GLY LYS ILE ILE HIS
SEQRES 13 B 655 LYS ILE ILE ASP LEU GLY TYR ALA LYS ASP VAL ASP GLN
SEQRES 14 B 655 GLY GLU LEU CYS THR GLU PHE VAL GLY THR LEU GLN TYR
SEQRES 15 B 655 LEU ALA PRO GLU LEU PHE GLU ASN LYS PRO TYR THR ALA
SEQRES 16 B 655 THR VAL ASP TYR TRP SER PHE GLY THR MET VAL PHE GLU
SEQRES 17 B 655 CYS ILE ALA GLY TYR ARG PRO PHE LEU HIS HIS LEU GLN
SEQRES 18 B 655 PRO PHE THR TRP HIS GLU LYS ILE LYS LYS LYS ASP PRO
SEQRES 19 B 655 LYS CYS ILE PHE ALA CYS GLU GLU MET SER GLY GLU VAL
SEQRES 20 B 655 ARG PHE SER SER HIS LEU PRO GLN PRO ASN SER LEU CYS
SEQRES 21 B 655 SER LEU ILE VAL GLU PRO MET GLU ASN TRP LEU GLN LEU
SEQRES 22 B 655 MET LEU ASN TRP ASP PRO GLN GLN ARG GLY GLY PRO VAL
SEQRES 23 B 655 ASP LEU THR LEU LYS GLN PRO ARG CYS PHE VAL LEU MET
SEQRES 24 B 655 ASP HIS ILE LEU ASN LEU LYS ILE VAL HIS ILE LEU ASN
SEQRES 25 B 655 MET THR SER ALA LYS ILE ILE SER PHE LEU LEU PRO PRO
SEQRES 26 B 655 ASP GLU SER LEU HIS SER LEU GLN SER ARG ILE GLU ARG
SEQRES 27 B 655 GLU THR GLY ILE ASN THR GLY SER GLN GLU LEU LEU SER
SEQRES 28 B 655 GLU THR GLY ILE SER LEU ASP PRO ARG LYS PRO ALA SER
SEQRES 29 B 655 GLN CYS VAL LEU ASP GLY VAL ARG GLY CYS ASP SER TYR
SEQRES 30 B 655 MET VAL TYR LEU PHE ASP LYS SER LYS THR VAL TYR GLU
SEQRES 31 B 655 GLY PRO PHE ALA SER ARG SER LEU SER ASP CYS VAL ASN
SEQRES 32 B 655 TYR ILE VAL GLN ASP SER LYS ILE GLN LEU PRO ILE ILE
SEQRES 33 B 655 GLN LEU ARG LYS VAL TRP ALA GLU ALA VAL HIS TYR VAL
SEQRES 34 B 655 SER GLY LEU LYS GLU ASP TYR SER ARG LEU PHE GLN GLY
SEQRES 35 B 655 GLN ARG ALA ALA MET LEU SER LEU LEU ARG TYR ASN ALA
SEQRES 36 B 655 ASN LEU THR LYS MET LYS ASN THR LEU ILE SER ALA SER
SEQRES 37 B 655 GLN GLN LEU LYS ALA LYS LEU GLU PHE PHE HIS LYS SER
SEQRES 38 B 655 ILE GLN LEU ASP LEU GLU ARG TYR SER GLU GLN MET THR
SEQRES 39 B 655 TYR GLY ILE SER SER GLU LYS MET LEU LYS ALA TRP LYS
SEQRES 40 B 655 GLU MET GLU GLU LYS ALA ILE HIS TYR ALA GLU VAL GLY
SEQRES 41 B 655 VAL ILE GLY TYR LEU GLU ASP GLN ILE MET SER LEU HIS
SEQRES 42 B 655 ALA GLU ILE MET GLU LEU GLN LYS SER PRO TYR GLY ARG
SEQRES 43 B 655 ARG GLN GLY ASP LEU MET GLU SER LEU GLU GLN ARG ALA
SEQRES 44 B 655 ILE ASP LEU TYR LYS GLN LEU LYS HIS ARG PRO SER ASP
SEQRES 45 B 655 HIS SER TYR SER ASP SER THR GLU MET VAL LYS ILE ILE
SEQRES 46 B 655 VAL HIS THR VAL GLN SER GLN ASP ARG VAL LEU LYS GLU
SEQRES 47 B 655 LEU PHE GLY HIS LEU SER LYS LEU LEU GLY CYS LYS GLN
SEQRES 48 B 655 LYS ILE ILE ASP LEU LEU PRO LYS VAL GLU VAL ALA LEU
SEQRES 49 B 655 SER ASN ILE LYS GLU ALA ASP ASN THR VAL MET PHE MET
SEQRES 50 B 655 GLN GLY LYS ARG GLN LYS GLU ILE TRP HIS LEU LEU LYS
SEQRES 51 B 655 ILE ALA CYS THR GLN
HELIX 1 AA1 SER A 51 LYS A 67 1 17
HELIX 2 AA2 ARG A 104 ASN A 108 1 5
HELIX 3 AA3 GLU A 111 GLY A 115 5 5
HELIX 4 AA4 LYS A 117 ASN A 138 1 22
HELIX 5 AA5 LYS A 146 GLU A 148 5 3
HELIX 6 AA6 ALA A 189 GLU A 194 1 6
HELIX 7 AA7 THR A 199 GLY A 217 1 19
HELIX 8 AA8 GLN A 226 LYS A 235 1 10
HELIX 9 AA9 CYS A 265 LEU A 280 1 16
HELIX 10 AB1 ARG A 299 LEU A 308 1 10
HELIX 11 AB2 SER A 333 GLY A 346 1 14
HELIX 12 AB3 SER A 404 ASP A 413 1 10
HELIX 13 AB4 PRO A 419 TYR A 500 1 82
HELIX 14 AB5 SER A 504 TYR A 521 1 18
HELIX 15 AB6 GLY A 525 LYS A 546 1 22
HELIX 16 AB7 GLY A 550 HIS A 573 1 24
HELIX 17 AB8 PRO A 575 SER A 579 5 5
HELIX 18 AB9 SER A 583 GLN A 660 1 78
HELIX 19 AC1 SER B 51 LYS B 67 1 17
HELIX 20 AC2 ARG B 104 ASN B 108 1 5
HELIX 21 AC3 GLU B 111 GLY B 115 5 5
HELIX 22 AC4 LYS B 117 ASN B 138 1 22
HELIX 23 AC5 LYS B 146 GLU B 148 5 3
HELIX 24 AC6 ALA B 189 GLU B 194 1 6
HELIX 25 AC7 THR B 199 GLY B 217 1 19
HELIX 26 AC8 GLN B 226 LYS B 235 1 10
HELIX 27 AC9 CYS B 265 LEU B 280 1 16
HELIX 28 AD1 ARG B 299 LEU B 308 1 10
HELIX 29 AD2 SER B 333 GLY B 346 1 14
HELIX 30 AD3 SER B 404 ASP B 413 1 10
HELIX 31 AD4 PRO B 419 TYR B 500 1 82
HELIX 32 AD5 SER B 504 TYR B 521 1 18
HELIX 33 AD6 GLY B 525 LYS B 546 1 22
HELIX 34 AD7 GLY B 550 HIS B 573 1 24
HELIX 35 AD8 PRO B 575 SER B 579 5 5
HELIX 36 AD9 SER B 583 GLN B 660 1 78
SHEET 1 AA1 3 GLU A 16 GLY A 22 0
SHEET 2 AA1 3 VAL A 29 GLN A 33 -1 O LEU A 31 N GLU A 19
SHEET 3 AA1 3 ILE A 41 LYS A 44 -1 O ILE A 41 N TYR A 32
SHEET 1 AA2 2 ILE A 150 VAL A 155 0
SHEET 2 AA2 2 LYS A 158 ILE A 163 -1 O ILE A 160 N GLN A 153
SHEET 1 AA3 2 PHE A 243 GLU A 246 0
SHEET 2 AA3 2 VAL A 252 SER A 255 -1 O SER A 255 N PHE A 243
SHEET 1 AA4 2 VAL A 291 ASP A 292 0
SHEET 2 AA4 2 GLN A 297 PRO A 298 -1 O GLN A 297 N ASP A 292
SHEET 1 AA5 4 LYS A 322 LEU A 327 0
SHEET 2 AA5 4 ILE A 312 ASN A 317 -1 N ASN A 317 O LYS A 322
SHEET 3 AA5 4 VAL A 384 ASP A 388 1 O LEU A 386 N LEU A 316
SHEET 4 AA5 4 GLN A 352 LEU A 355 -1 N GLU A 353 O PHE A 387
SHEET 1 AA6 3 GLU B 16 GLY B 22 0
SHEET 2 AA6 3 VAL B 29 GLN B 33 -1 O LEU B 31 N GLU B 19
SHEET 3 AA6 3 ILE B 41 LYS B 44 -1 O ILE B 41 N TYR B 32
SHEET 1 AA7 2 ILE B 150 VAL B 155 0
SHEET 2 AA7 2 LYS B 158 ILE B 163 -1 O ILE B 160 N GLN B 153
SHEET 1 AA8 2 PHE B 243 GLU B 246 0
SHEET 2 AA8 2 VAL B 252 SER B 255 -1 O SER B 255 N PHE B 243
SHEET 1 AA9 2 VAL B 291 ASP B 292 0
SHEET 2 AA9 2 GLN B 297 PRO B 298 -1 O GLN B 297 N ASP B 292
SHEET 1 AB1 4 LYS B 322 LEU B 327 0
SHEET 2 AB1 4 ILE B 312 ASN B 317 -1 N ASN B 317 O LYS B 322
SHEET 3 AB1 4 VAL B 384 ASP B 388 1 O LEU B 386 N LEU B 316
SHEET 4 AB1 4 GLN B 352 LEU B 355 -1 N GLU B 353 O PHE B 387
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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
(ATOM LINES ARE NOT SHOWN.)
END
