HEADER PROTEIN BINDING 10-JUN-14 4TQ1
TITLE CRYSTAL STRUCTURE OF HUMAN ATG5-TECAIR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUTOPHAGY PROTEIN 5;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: APG5-LIKE,APOPTOSIS-SPECIFIC PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TECTONIN BETA-PROPELLER REPEAT-CONTAINING PROTEIN 1;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 503-540;
COMPND 10 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: ATG5, APG5L, ASP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: TECPR1, KIAA1358;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS AUTOPHAGY PROTEIN COMPLEX, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.KIM,S.B.HONG,H.K.SONG
REVDAT 3 20-MAR-24 4TQ1 1 REMARK
REVDAT 2 29-JAN-20 4TQ1 1 SOURCE REMARK
REVDAT 1 11-MAR-15 4TQ1 0
JRNL AUTH J.H.KIM,S.B.HONG,J.K.LEE,S.HAN,K.H.ROH,K.E.LEE,Y.K.KIM,
JRNL AUTH 2 E.J.CHOI,H.K.SONG
JRNL TITL INSIGHTS INTO AUTOPHAGOSOME MATURATION REVEALED BY THE
JRNL TITL 2 STRUCTURES OF ATG5 WITH ITS INTERACTING PARTNERS
JRNL REF AUTOPHAGY V. 11 75 2015
JRNL REFN ESSN 1554-8635
JRNL PMID 25484072
JRNL DOI 10.4161/15548627.2014.984276
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 27641
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1926
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.7870 - 4.3398 1.00 2061 155 0.1768 0.1931
REMARK 3 2 4.3398 - 3.4456 1.00 1944 144 0.1547 0.2132
REMARK 3 3 3.4456 - 3.0103 1.00 1927 145 0.1779 0.2410
REMARK 3 4 3.0103 - 2.7352 0.99 1890 141 0.1794 0.2225
REMARK 3 5 2.7352 - 2.5392 0.98 1878 141 0.1893 0.2172
REMARK 3 6 2.5392 - 2.3896 0.98 1872 141 0.1868 0.2335
REMARK 3 7 2.3896 - 2.2699 0.98 1856 136 0.1799 0.2336
REMARK 3 8 2.2699 - 2.1711 0.98 1825 137 0.1762 0.2443
REMARK 3 9 2.1711 - 2.0875 0.96 1829 134 0.1797 0.2710
REMARK 3 10 2.0875 - 2.0155 0.96 1816 137 0.1829 0.2202
REMARK 3 11 2.0155 - 1.9525 0.95 1769 135 0.1912 0.2021
REMARK 3 12 1.9525 - 1.8967 0.92 1730 134 0.1889 0.2076
REMARK 3 13 1.8967 - 1.8468 0.89 1660 124 0.2080 0.2446
REMARK 3 14 1.8468 - 1.8017 0.87 1658 122 0.2194 0.2772
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2495
REMARK 3 ANGLE : 1.041 3378
REMARK 3 CHIRALITY : 0.072 355
REMARK 3 PLANARITY : 0.004 431
REMARK 3 DIHEDRAL : 14.393 931
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202057.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28746
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.0000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, PEG 1000, PEG 3350, ALCOHOLS, MES
REMARK 280 -IMDAZOLE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.80900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.17700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.95950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.17700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.80900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.95950
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 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: 2480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 MET A -13
REMARK 465 GLY A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 GLU A 26
REMARK 465 ILE A 27
REMARK 465 THR A 28
REMARK 465 GLU A 29
REMARK 465 ARG A 30
REMARK 465 GLU A 31
REMARK 465 ARG A 61
REMARK 465 GLN A 62
REMARK 465 GLU A 63
REMARK 465 ASP A 64
REMARK 465 ILE A 65
REMARK 465 GLN A 272
REMARK 465 PRO A 273
REMARK 465 THR A 274
REMARK 465 ASP A 275
REMARK 465 MET B 572
REMARK 465 ALA B 573
REMARK 465 GLN B 606
REMARK 465 SER B 607
REMARK 465 VAL B 608
REMARK 465 TRP B 609
REMARK 465 VAL B 610
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 58 CG CD CE NZ
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 OG SER A 66 O HOH A 421 2.12
REMARK 500 OE2 GLU A 67 O HOH A 443 2.15
REMARK 500 O HOH A 438 O HOH B 717 2.17
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 OE2 GLU B 595 O HOH A 336 3545 2.17
REMARK 500 O HOH A 454 O HOH A 457 1455 2.19
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 SER A 43 -161.30 -103.12
REMARK 500 GLU A 67 -54.70 -132.32
REMARK 500 THR A 192 -59.80 62.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 400 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH A 425 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH A 454 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH A 459 DISTANCE = 8.07 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TQ0 RELATED DB: PDB
DBREF 4TQ1 A 1 275 UNP Q9H1Y0 ATG5_HUMAN 1 275
DBREF 4TQ1 B 573 610 UNP Q7Z6L1 TCPR1_HUMAN 503 540
SEQADV 4TQ1 MET A -13 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 GLY A -12 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 SER A -11 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 SER A -10 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 HIS A -9 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 HIS A -8 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 HIS A -7 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 HIS A -6 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 HIS A -5 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 HIS A -4 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 SER A -3 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 GLN A -2 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 GLY A -1 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 SER A 0 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ1 MET B 572 UNP Q7Z6L1 EXPRESSION TAG
SEQRES 1 A 289 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN GLY
SEQRES 2 A 289 SER MET THR ASP ASP LYS ASP VAL LEU ARG ASP VAL TRP
SEQRES 3 A 289 PHE GLY ARG ILE PRO THR CYS PHE THR LEU TYR GLN ASP
SEQRES 4 A 289 GLU ILE THR GLU ARG GLU ALA GLU PRO TYR TYR LEU LEU
SEQRES 5 A 289 LEU PRO ARG VAL SER TYR LEU THR LEU VAL THR ASP LYS
SEQRES 6 A 289 VAL LYS LYS HIS PHE GLN LYS VAL MET ARG GLN GLU ASP
SEQRES 7 A 289 ILE SER GLU ILE TRP PHE GLU TYR GLU GLY THR PRO LEU
SEQRES 8 A 289 LYS TRP HIS TYR PRO ILE GLY LEU LEU PHE ASP LEU LEU
SEQRES 9 A 289 ALA SER SER SER ALA LEU PRO TRP ASN ILE THR VAL HIS
SEQRES 10 A 289 PHE LYS SER PHE PRO GLU LYS ASP LEU LEU HIS CYS PRO
SEQRES 11 A 289 SER LYS ASP ALA ILE GLU ALA HIS PHE MET SER CYS MET
SEQRES 12 A 289 LYS GLU ALA ASP ALA LEU LYS HIS LYS SER GLN VAL ILE
SEQRES 13 A 289 ASN GLU MET GLN LYS LYS ASP HIS LYS GLN LEU TRP MET
SEQRES 14 A 289 GLY LEU GLN ASN ASP ARG PHE ASP GLN PHE TRP ALA ILE
SEQRES 15 A 289 ASN ARG LYS LEU MET GLU TYR PRO ALA GLU GLU ASN GLY
SEQRES 16 A 289 PHE ARG TYR ILE PRO PHE ARG ILE TYR GLN THR THR THR
SEQRES 17 A 289 GLU ARG PRO PHE ILE GLN LYS LEU PHE ARG PRO VAL ALA
SEQRES 18 A 289 ALA ASP GLY GLN LEU HIS THR LEU GLY ASP LEU LEU LYS
SEQRES 19 A 289 GLU VAL CYS PRO SER ALA ILE ASP PRO GLU ASP GLY GLU
SEQRES 20 A 289 LYS LYS ASN GLN VAL MET ILE HIS GLY ILE GLU PRO MET
SEQRES 21 A 289 LEU GLU THR PRO LEU GLN TRP LEU SER GLU HIS LEU SER
SEQRES 22 A 289 TYR PRO ASP ASN PHE LEU HIS ILE SER ILE ILE PRO GLN
SEQRES 23 A 289 PRO THR ASP
SEQRES 1 B 39 MET ALA GLN THR ALA ALA TRP ARG LYS GLN ILE PHE GLN
SEQRES 2 B 39 GLN LEU THR GLU ARG THR LYS ARG GLU LEU GLU ASN PHE
SEQRES 3 B 39 ARG HIS TYR GLU GLN ALA VAL GLU GLN SER VAL TRP VAL
FORMUL 3 HOH *190(H2 O)
HELIX 1 AA1 ASP A 3 PHE A 13 1 11
HELIX 2 AA2 TYR A 44 THR A 49 1 6
HELIX 3 AA3 THR A 49 LYS A 58 1 10
HELIX 4 AA4 PRO A 82 SER A 92 1 11
HELIX 5 AA5 SER A 117 LYS A 138 1 22
HELIX 6 AA6 SER A 139 MET A 145 1 7
HELIX 7 AA7 GLN A 146 ASN A 159 1 14
HELIX 8 AA8 ARG A 161 MET A 173 1 13
HELIX 9 AA9 THR A 214 CYS A 223 1 10
HELIX 10 AB1 PRO A 224 ILE A 227 5 4
HELIX 11 AB2 PRO A 250 LEU A 258 1 9
HELIX 12 AB3 ALA B 576 GLU B 595 1 20
SHEET 1 AA1 6 THR A 75 PRO A 76 0
SHEET 2 AA1 6 TRP A 69 TYR A 72 -1 N TYR A 72 O THR A 75
SHEET 3 AA1 6 TRP A 98 HIS A 103 -1 O THR A 101 N GLU A 71
SHEET 4 AA1 6 ARG A 15 LEU A 22 1 N CYS A 19 O TRP A 98
SHEET 5 AA1 6 TYR A 35 PRO A 40 -1 O TYR A 35 N PHE A 20
SHEET 6 AA1 6 GLU B 601 GLN B 602 1 O GLU B 601 N LEU A 38
SHEET 1 AA2 3 PHE A 187 GLN A 191 0
SHEET 2 AA2 3 LEU A 265 ILE A 270 1 O ILE A 267 N TYR A 190
SHEET 3 AA2 3 GLN A 237 MET A 239 -1 N GLN A 237 O ILE A 270
CISPEP 1 LEU A 96 PRO A 97 0 2.37
CRYST1 43.618 71.919 96.354 90.00 90.00 90.00 P 21 21 21 4
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 0.022926 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013905 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010378 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
