HEADER STRUCTURAL PROTEIN 01-JUN-18 6GNY
TITLE CRYSTAL STRUCTURE OF THE MAJIN-TERB2 HETEROTETRAMERIC COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MEMBRANE-ANCHORED JUNCTION PROTEIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TELOMERE REPEATS-BINDING BOUQUET FORMATION PROTEIN 2;
COMPND 7 CHAIN: B, D;
COMPND 8 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: MAJIN, C11ORF85;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: TERB2, C15ORF43;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MEIOSIS, TELOMERES, COMPLEX, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.DUNCE,M.GURUSARAN,L.T.SEN,O.R.DAVIES
REVDAT 4 17-JAN-24 6GNY 1 REMARK
REVDAT 3 22-APR-20 6GNY 1 REMARK
REVDAT 2 02-JAN-19 6GNY 1 JRNL
REVDAT 1 12-DEC-18 6GNY 0
JRNL AUTH J.M.DUNCE,A.E.MILBURN,M.GURUSARAN,I.DA CRUZ,L.T.SEN,
JRNL AUTH 2 R.BENAVENTE,O.R.DAVIES
JRNL TITL STRUCTURAL BASIS OF MEIOTIC TELOMERE ATTACHMENT TO THE
JRNL TITL 2 NUCLEAR ENVELOPE BY MAJIN-TERB2-TERB1.
JRNL REF NAT COMMUN V. 9 5355 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 30559341
JRNL DOI 10.1038/S41467-018-07794-7
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_3126)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.280
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25690
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 2427
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 45.3632 - 4.7553 1.00 2734 148 0.1641 0.1694
REMARK 3 2 4.7553 - 3.7750 1.00 2751 123 0.1369 0.1390
REMARK 3 3 3.7750 - 3.2980 1.00 2775 117 0.1833 0.2349
REMARK 3 4 3.2980 - 2.9965 1.00 2698 173 0.1984 0.2297
REMARK 3 5 2.9965 - 2.7818 1.00 2738 131 0.2100 0.2186
REMARK 3 6 2.7818 - 2.6178 1.00 2747 153 0.2286 0.2119
REMARK 3 7 2.6178 - 2.4867 1.00 2741 122 0.2203 0.2740
REMARK 3 8 2.4867 - 2.3784 1.00 2758 117 0.2114 0.2422
REMARK 3 9 2.3784 - 2.2869 1.00 2744 151 0.2084 0.2403
REMARK 3 10 2.2869 - 2.2080 1.00 2694 152 0.2328 0.2595
REMARK 3 11 2.2080 - 2.1389 1.00 2710 157 0.2298 0.2760
REMARK 3 12 2.1389 - 2.0778 1.00 2729 180 0.2646 0.2661
REMARK 3 13 2.0778 - 2.0231 1.00 2728 146 0.2652 0.2748
REMARK 3 14 2.0231 - 1.9737 1.00 2665 166 0.2718 0.2747
REMARK 3 15 1.9737 - 1.9289 1.00 2770 128 0.3124 0.3572
REMARK 3 16 1.9289 - 1.8878 1.00 2759 141 0.3381 0.3654
REMARK 3 17 1.8878 - 1.8501 1.00 2732 122 0.3587 0.4334
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.57
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 : 0.003 2367
REMARK 3 ANGLE : 0.627 3205
REMARK 3 CHIRALITY : 0.049 336
REMARK 3 PLANARITY : 0.005 404
REMARK 3 DIHEDRAL : 13.763 872
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 6GNY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200009882.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25741
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 45.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6GNX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.12M 1,6-HEXANEDIOL; 0.12M 1-BUTANOL;
REMARK 280 0.12M 1,2-PROPANEDIOL (RACEMIC); 0.12M 2-PROPANOL; 0.12M 1,4-
REMARK 280 BUTANEDIOL; 0.12M 1,3-PROPANEDIOL; 39.1 MM BICINE PH 5.03; 60.9
REMARK 280 MM TRIZMA PH 10.83; 18.3% W/V PEG 1000; 18.3% W/V PEG 3350; 18.3%
REMARK 280 V/V MPD, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.83500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.83500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.98500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.19500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.98500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.19500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 55.83500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.98500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.19500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 55.83500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.98500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 44.19500
REMARK 290 SMTRY3 8 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLY B 165
REMARK 465 SER B 166
REMARK 465 MET B 167
REMARK 465 PRO B 168
REMARK 465 VAL B 169
REMARK 465 ASN B 170
REMARK 465 ASN B 171
REMARK 465 MET B 172
REMARK 465 VAL B 173
REMARK 465 THR B 174
REMARK 465 GLN B 205
REMARK 465 ASN B 206
REMARK 465 GLU B 207
REMARK 465 GLY C -1
REMARK 465 GLY D 165
REMARK 465 SER D 166
REMARK 465 MET D 167
REMARK 465 PRO D 168
REMARK 465 VAL D 169
REMARK 465 ASN D 170
REMARK 465 ASN D 171
REMARK 465 MET D 172
REMARK 465 VAL D 173
REMARK 465 THR D 174
REMARK 465 ASN D 206
REMARK 465 GLU D 207
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 O HOH C 235 O HOH C 236 2.04
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 H GLY B 198 OE2 GLU C 42 6565 1.55
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 THR A 7 43.82 -87.72
REMARK 500 PRO A 9 33.94 -98.83
REMARK 500 ASN A 61 63.89 -155.41
REMARK 500 THR C 7 46.87 -88.42
REMARK 500 PRO C 9 35.31 -97.67
REMARK 500 ASN C 61 62.15 -155.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6GNX RELATED DB: PDB
REMARK 900 6GNX IS THE SELENOMETHIONINE DERIVATIVE OF THE SAME COMPLEX
DBREF 6GNY A 1 106 UNP Q3KP22 MAJIN_HUMAN 1 106
DBREF 6GNY B 168 207 UNP Q8NHR7 TERB2_HUMAN 168 207
DBREF 6GNY C 1 106 UNP Q3KP22 MAJIN_HUMAN 1 106
DBREF 6GNY D 168 207 UNP Q8NHR7 TERB2_HUMAN 168 207
SEQADV 6GNY GLY A -1 UNP Q3KP22 EXPRESSION TAG
SEQADV 6GNY SER A 0 UNP Q3KP22 EXPRESSION TAG
SEQADV 6GNY GLY B 165 UNP Q8NHR7 EXPRESSION TAG
SEQADV 6GNY SER B 166 UNP Q8NHR7 EXPRESSION TAG
SEQADV 6GNY MET B 167 UNP Q8NHR7 EXPRESSION TAG
SEQADV 6GNY GLY C -1 UNP Q3KP22 EXPRESSION TAG
SEQADV 6GNY SER C 0 UNP Q3KP22 EXPRESSION TAG
SEQADV 6GNY GLY D 165 UNP Q8NHR7 EXPRESSION TAG
SEQADV 6GNY SER D 166 UNP Q8NHR7 EXPRESSION TAG
SEQADV 6GNY MET D 167 UNP Q8NHR7 EXPRESSION TAG
SEQRES 1 A 108 GLY SER MET SER LEU LYS PRO PHE THR TYR PRO PHE PRO
SEQRES 2 A 108 GLU THR ARG PHE LEU HIS ALA GLY PRO ASN VAL TYR LYS
SEQRES 3 A 108 PHE LYS ILE ARG TYR GLY LYS SER ILE ARG GLY GLU GLU
SEQRES 4 A 108 ILE GLU ASN LYS GLU VAL ILE THR GLN GLU LEU GLU ASP
SEQRES 5 A 108 SER VAL ARG VAL VAL LEU GLY ASN LEU ASP ASN LEU GLN
SEQRES 6 A 108 PRO PHE ALA THR GLU HIS PHE ILE VAL PHE PRO TYR LYS
SEQRES 7 A 108 SER LYS TRP GLU ARG VAL SER HIS LEU LYS PHE LYS HIS
SEQRES 8 A 108 GLY GLU ILE ILE LEU ILE PRO TYR PRO PHE VAL PHE THR
SEQRES 9 A 108 LEU TYR VAL GLU
SEQRES 1 B 43 GLY SER MET PRO VAL ASN ASN MET VAL THR GLY TYR ILE
SEQRES 2 B 43 SER ILE ASP ALA MET LYS LYS PHE LEU GLY GLU LEU HIS
SEQRES 3 B 43 ASP PHE ILE PRO GLY THR SER GLY TYR LEU ALA TYR HIS
SEQRES 4 B 43 VAL GLN ASN GLU
SEQRES 1 C 108 GLY SER MET SER LEU LYS PRO PHE THR TYR PRO PHE PRO
SEQRES 2 C 108 GLU THR ARG PHE LEU HIS ALA GLY PRO ASN VAL TYR LYS
SEQRES 3 C 108 PHE LYS ILE ARG TYR GLY LYS SER ILE ARG GLY GLU GLU
SEQRES 4 C 108 ILE GLU ASN LYS GLU VAL ILE THR GLN GLU LEU GLU ASP
SEQRES 5 C 108 SER VAL ARG VAL VAL LEU GLY ASN LEU ASP ASN LEU GLN
SEQRES 6 C 108 PRO PHE ALA THR GLU HIS PHE ILE VAL PHE PRO TYR LYS
SEQRES 7 C 108 SER LYS TRP GLU ARG VAL SER HIS LEU LYS PHE LYS HIS
SEQRES 8 C 108 GLY GLU ILE ILE LEU ILE PRO TYR PRO PHE VAL PHE THR
SEQRES 9 C 108 LEU TYR VAL GLU
SEQRES 1 D 43 GLY SER MET PRO VAL ASN ASN MET VAL THR GLY TYR ILE
SEQRES 2 D 43 SER ILE ASP ALA MET LYS LYS PHE LEU GLY GLU LEU HIS
SEQRES 3 D 43 ASP PHE ILE PRO GLY THR SER GLY TYR LEU ALA TYR HIS
SEQRES 4 D 43 VAL GLN ASN GLU
HET TRS B 301 20
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 5 TRS C4 H12 N O3 1+
FORMUL 6 HOH *119(H2 O)
HELIX 1 AA1 GLY A 30 GLU A 36 1 7
HELIX 2 AA2 ASN A 40 ASN A 58 1 19
HELIX 3 AA3 SER B 178 MET B 182 5 5
HELIX 4 AA4 GLY C 30 GLU C 36 1 7
HELIX 5 AA5 ASN C 40 GLY C 57 1 18
HELIX 6 AA6 SER D 178 MET D 182 5 5
SHEET 1 AA1 6 PHE A 65 ALA A 66 0
SHEET 2 AA1 6 ILE A 71 LYS A 78 -1 O VAL A 72 N PHE A 65
SHEET 3 AA1 6 PHE A 99 GLU A 106 -1 O THR A 102 N TYR A 75
SHEET 4 AA1 6 ASN A 21 TYR A 29 1 N ARG A 28 O VAL A 105
SHEET 5 AA1 6 GLU A 12 ALA A 18 -1 N LEU A 16 O TYR A 23
SHEET 6 AA1 6 HIS B 190 ASP B 191 -1 O HIS B 190 N HIS A 17
SHEET 1 AA2 7 PHE A 65 ALA A 66 0
SHEET 2 AA2 7 ILE A 71 LYS A 78 -1 O VAL A 72 N PHE A 65
SHEET 3 AA2 7 PHE A 99 GLU A 106 -1 O THR A 102 N TYR A 75
SHEET 4 AA2 7 ASN A 21 TYR A 29 1 N ARG A 28 O VAL A 105
SHEET 5 AA2 7 ILE A 92 PRO A 96 1 O ILE A 95 N VAL A 22
SHEET 6 AA2 7 LEU A 85 HIS A 89 -1 N HIS A 89 O ILE A 92
SHEET 7 AA2 7 TYR B 199 HIS B 203 -1 O LEU B 200 N LYS A 88
SHEET 1 AA3 6 PHE C 65 ALA C 66 0
SHEET 2 AA3 6 ILE C 71 LYS C 78 -1 O VAL C 72 N PHE C 65
SHEET 3 AA3 6 ILE C 92 GLU C 106 -1 O GLU C 106 N ILE C 71
SHEET 4 AA3 6 ASN C 21 TYR C 29 1 N ARG C 28 O VAL C 105
SHEET 5 AA3 6 GLU C 12 ALA C 18 -1 N ARG C 14 O PHE C 25
SHEET 6 AA3 6 HIS D 190 ASP D 191 -1 O HIS D 190 N HIS C 17
SHEET 1 AA4 5 PHE C 65 ALA C 66 0
SHEET 2 AA4 5 ILE C 71 LYS C 78 -1 O VAL C 72 N PHE C 65
SHEET 3 AA4 5 ILE C 92 GLU C 106 -1 O GLU C 106 N ILE C 71
SHEET 4 AA4 5 LEU C 85 HIS C 89 -1 N HIS C 89 O ILE C 92
SHEET 5 AA4 5 TYR D 199 HIS D 203 -1 O LEU D 200 N LYS C 88
CISPEP 1 TYR A 8 PRO A 9 0 0.51
CISPEP 2 TYR C 8 PRO C 9 0 -1.05
SITE 1 AC1 6 PRO A 20 TYR A 23 LEU A 56 LEU A 59
SITE 2 AC1 6 HOH A 207 PHE B 185
CRYST1 59.970 88.390 111.670 90.00 90.00 90.00 C 2 2 21 16
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 0.016675 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008955 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
