HEADER ISOMERASE/PROTEIN BINDING 05-SEP-16 5GVE
TITLE HUMAN TOP3B-TDRD3 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA TOPOISOMERASE 3-BETA-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-612;
COMPND 5 SYNONYM: DNA TOPOISOMERASE III BETA-1;
COMPND 6 EC: 5.99.1.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: TUDOR DOMAIN-CONTAINING PROTEIN 3;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 1-161;
COMPND 12 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: TOP3B, TOP3B1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: TDRD3;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TOPOISOMERASE, SCAFFOLD, ISOMERASE-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GOTO-ITO,A.YAMAGATA,Y.SATO,T.S.TAKAHASHI,S.FUKAI
REVDAT 2 08-NOV-23 5GVE 1 REMARK
REVDAT 1 14-JUN-17 5GVE 0
JRNL AUTH S.GOTO-ITO,A.YAMAGATA,T.S.TAKAHASHI,Y.SATO,S.FUKAI
JRNL TITL STRUCTURAL BASIS OF THE INTERACTION BETWEEN TOPOISOMERASE
JRNL TITL 2 III BETA AND THE TDRD3 AUXILIARY FACTOR
JRNL REF SCI REP V. 7 42123 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28176834
JRNL DOI 10.1038/SREP42123
REMARK 2
REMARK 2 RESOLUTION. 3.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 3.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22208
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1134
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 47.0012 - 7.2039 1.00 2703 132 0.1787 0.1982
REMARK 3 2 7.2039 - 5.7212 1.00 2646 145 0.2200 0.2839
REMARK 3 3 5.7212 - 4.9989 1.00 2624 152 0.1977 0.2913
REMARK 3 4 4.9989 - 4.5423 1.00 2639 142 0.1760 0.2244
REMARK 3 5 4.5423 - 4.2169 1.00 2609 137 0.1705 0.2093
REMARK 3 6 4.2169 - 3.9684 1.00 2620 148 0.2104 0.2582
REMARK 3 7 3.9684 - 3.7698 1.00 2608 143 0.2411 0.2876
REMARK 3 8 3.7698 - 3.6057 1.00 2625 135 0.2719 0.3353
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.920
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 : 0.004 6208
REMARK 3 ANGLE : 1.135 8399
REMARK 3 CHIRALITY : 0.079 938
REMARK 3 PLANARITY : 0.004 1087
REMARK 3 DIHEDRAL : 13.516 2325
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0221 -51.7221 0.4102
REMARK 3 T TENSOR
REMARK 3 T11: 1.5584 T22: 1.0689
REMARK 3 T33: 1.1073 T12: -0.5168
REMARK 3 T13: 0.1120 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.7770 L22: 1.4405
REMARK 3 L33: 1.6832 L12: 0.9220
REMARK 3 L13: 1.2205 L23: 1.6754
REMARK 3 S TENSOR
REMARK 3 S11: -0.1472 S12: 0.3326 S13: -0.0442
REMARK 3 S21: -0.2489 S22: 0.2780 S23: -0.0259
REMARK 3 S31: 0.3492 S32: -0.0163 S33: -0.1279
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 5GVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1300001535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CMOS
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22224
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.66
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5GVC, 5GVD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM NA-CACODYLATE, 10 MM MGSO4, 1.7
REMARK 280 M LI2SO4, PH 6.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.54000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.27000
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 55.90500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 18.63500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 93.17500
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: 1630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 SER A 209
REMARK 465 SER A 612
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 OD2 ASP A 119 OH TYR A 336 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 PRO A 86 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 VAL B 79 CB - CA - C ANGL. DEV. = -15.6 DEGREES
REMARK 500 ALA B 80 CB - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 PRO B 92 C - N - CD ANGL. DEV. = 12.8 DEGREES
REMARK 500 PRO B 92 CB - CA - C ANGL. DEV. = -13.6 DEGREES
REMARK 500 PRO B 92 N - CA - C ANGL. DEV. = 40.0 DEGREES
REMARK 500 ARG B 93 C - N - CA ANGL. DEV. = 27.2 DEGREES
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 VAL A 262 -59.53 64.39
REMARK 500 TRP A 363 17.96 -140.89
REMARK 500 GLU B 86 -120.38 64.23
REMARK 500 ARG B 93 132.10 -36.17
REMARK 500 MET B 94 24.89 81.39
REMARK 500 HIS B 103 -46.99 -135.33
REMARK 500 GLU B 110 86.15 -69.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 88 GLN B 89 -148.78
REMARK 500 PRO B 92 ARG B 93 -122.74
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 MG A 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GVC RELATED DB: PDB
REMARK 900 RELATED ID: 5GVD RELATED DB: PDB
DBREF 5GVE A 1 612 UNP O95985 TOP3B_HUMAN 1 612
DBREF 5GVE B 1 161 UNP Q9H7E2 TDRD3_HUMAN 1 161
SEQADV 5GVE HIS A 0 UNP O95985 EXPRESSION TAG
SEQADV 5GVE GLY B -3 UNP Q9H7E2 EXPRESSION TAG
SEQADV 5GVE PRO B -2 UNP Q9H7E2 EXPRESSION TAG
SEQADV 5GVE GLY B -1 UNP Q9H7E2 EXPRESSION TAG
SEQADV 5GVE HIS B 0 UNP Q9H7E2 EXPRESSION TAG
SEQRES 1 A 613 HIS MET LYS THR VAL LEU MET VAL ALA GLU LYS PRO SER
SEQRES 2 A 613 LEU ALA GLN SER ILE ALA LYS ILE LEU SER ARG GLY SER
SEQRES 3 A 613 LEU SER SER HIS LYS GLY LEU ASN GLY ALA CYS SER VAL
SEQRES 4 A 613 HIS GLU TYR THR GLY THR PHE ALA GLY GLN PRO VAL ARG
SEQRES 5 A 613 PHE LYS MET THR SER VAL CYS GLY HIS VAL MET THR LEU
SEQRES 6 A 613 ASP PHE LEU GLY LYS TYR ASN LYS TRP ASP LYS VAL ASP
SEQRES 7 A 613 PRO ALA GLU LEU PHE SER GLN ALA PRO THR GLU LYS LYS
SEQRES 8 A 613 GLU ALA ASN PRO LYS LEU ASN MET VAL LYS PHE LEU GLN
SEQRES 9 A 613 VAL GLU GLY ARG GLY CYS ASP TYR ILE VAL LEU TRP LEU
SEQRES 10 A 613 ASP CYS ASP LYS GLU GLY GLU ASN ILE CYS PHE GLU VAL
SEQRES 11 A 613 LEU ASP ALA VAL LEU PRO VAL MET ASN LYS ALA HIS GLY
SEQRES 12 A 613 GLY GLU LYS THR VAL PHE ARG ALA ARG PHE SER SER ILE
SEQRES 13 A 613 THR ASP THR ASP ILE CYS ASN ALA MET ALA CYS LEU GLY
SEQRES 14 A 613 GLU PRO ASP HIS ASN GLU ALA LEU SER VAL ASP ALA ARG
SEQRES 15 A 613 GLN GLU LEU ASP LEU ARG ILE GLY CYS ALA PHE THR ARG
SEQRES 16 A 613 PHE GLN THR LYS TYR PHE GLN GLY LYS TYR GLY ASP LEU
SEQRES 17 A 613 ASP SER SER LEU ILE SER PHE GLY PRO CYS GLN THR PRO
SEQRES 18 A 613 THR LEU GLY PHE CYS VAL GLU ARG HIS ASP LYS ILE GLN
SEQRES 19 A 613 SER PHE LYS PRO GLU THR TYR TRP VAL LEU GLN ALA LYS
SEQRES 20 A 613 VAL ASN THR ASP LYS ASP ARG SER LEU LEU LEU ASP TRP
SEQRES 21 A 613 ASP ARG VAL ARG VAL PHE ASP ARG GLU ILE ALA GLN MET
SEQRES 22 A 613 PHE LEU ASN MET THR LYS LEU GLU LYS GLU ALA GLN VAL
SEQRES 23 A 613 GLU ALA THR SER ARG LYS GLU LYS ALA LYS GLN ARG PRO
SEQRES 24 A 613 LEU ALA LEU ASN THR VAL GLU MET LEU ARG VAL ALA SER
SEQRES 25 A 613 SER SER LEU GLY MET GLY PRO GLN HIS ALA MET GLN THR
SEQRES 26 A 613 ALA GLU ARG LEU TYR THR GLN GLY TYR ILE SER TYR PRO
SEQRES 27 A 613 ARG THR GLU THR THR HIS TYR PRO GLU ASN PHE ASP LEU
SEQRES 28 A 613 LYS GLY SER LEU ARG GLN GLN ALA ASN HIS PRO TYR TRP
SEQRES 29 A 613 ALA ASP THR VAL LYS ARG LEU LEU ALA GLU GLY ILE ASN
SEQRES 30 A 613 ARG PRO ARG LYS GLY HIS ASP ALA GLY ASP HIS PRO PRO
SEQRES 31 A 613 ILE THR PRO MET LYS SER ALA THR GLU ALA GLU LEU GLY
SEQRES 32 A 613 GLY ASP ALA TRP ARG LEU TYR GLU TYR ILE THR ARG HIS
SEQRES 33 A 613 PHE ILE ALA THR VAL SER HIS ASP CYS LYS TYR LEU GLN
SEQRES 34 A 613 SER THR ILE SER PHE ARG ILE GLY PRO GLU LEU PHE THR
SEQRES 35 A 613 CYS SER GLY LYS THR VAL LEU SER PRO GLY PHE THR GLU
SEQRES 36 A 613 VAL MET PRO TRP GLN SER VAL PRO LEU GLU GLU SER LEU
SEQRES 37 A 613 PRO THR CYS GLN ARG GLY ASP ALA PHE PRO VAL GLY GLU
SEQRES 38 A 613 VAL LYS MET LEU GLU LYS GLN THR ASN PRO PRO ASP TYR
SEQRES 39 A 613 LEU THR GLU ALA GLU LEU ILE THR LEU MET GLU LYS HIS
SEQRES 40 A 613 GLY ILE GLY THR ASP ALA SER ILE PRO VAL HIS ILE ASN
SEQRES 41 A 613 ASN ILE CYS GLN ARG ASN TYR VAL THR VAL GLU SER GLY
SEQRES 42 A 613 ARG ARG LEU LYS PRO THR ASN LEU GLY ILE VAL LEU VAL
SEQRES 43 A 613 HIS GLY TYR TYR LYS ILE ASP ALA GLU LEU VAL LEU PRO
SEQRES 44 A 613 THR ILE ARG SER ALA VAL GLU LYS GLN LEU ASN LEU ILE
SEQRES 45 A 613 ALA GLN GLY LYS ALA ASP TYR ARG GLN VAL LEU GLY HIS
SEQRES 46 A 613 THR LEU ASP VAL PHE LYS ARG LYS PHE HIS TYR PHE VAL
SEQRES 47 A 613 ASP SER ILE ALA GLY MET ASP GLU LEU MET GLU VAL SER
SEQRES 48 A 613 PHE SER
SEQRES 1 B 165 GLY PRO GLY HIS MET ALA GLN VAL ALA GLY ALA ALA LEU
SEQRES 2 B 165 SER GLN ALA GLY TRP TYR LEU SER ASP GLU GLY ILE GLU
SEQRES 3 B 165 ALA CYS THR SER SER PRO ASP LYS VAL ASN VAL ASN ASP
SEQRES 4 B 165 ILE ILE LEU ILE ALA LEU ASN THR ASP LEU ARG THR ILE
SEQRES 5 B 165 GLY LYS LYS PHE LEU PRO SER ASP ILE ASN SER GLY LYS
SEQRES 6 B 165 VAL GLU LYS LEU GLU GLY PRO CYS VAL LEU GLN ILE GLN
SEQRES 7 B 165 LYS ILE ARG ASN VAL ALA ALA PRO LYS ASP ASN GLU GLU
SEQRES 8 B 165 SER GLN ALA ALA PRO ARG MET LEU ARG LEU GLN MET THR
SEQRES 9 B 165 ASP GLY HIS ILE SER CYS THR ALA VAL GLU PHE SER TYR
SEQRES 10 B 165 MET SER LYS ILE SER LEU ASN THR PRO PRO GLY THR LYS
SEQRES 11 B 165 VAL LYS LEU SER GLY ILE VAL ASP ILE LYS ASN GLY PHE
SEQRES 12 B 165 LEU LEU LEU ASN ASP SER ASN THR THR VAL LEU GLY GLY
SEQRES 13 B 165 GLU VAL GLU HIS LEU ILE GLU LYS TRP
HET MG A 701 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG MG 2+
HELIX 1 AA1 LYS A 10 SER A 22 1 13
HELIX 2 AA2 GLY A 68 LYS A 72 5 5
HELIX 3 AA3 ASP A 77 PHE A 82 5 6
HELIX 4 AA4 ASN A 93 LEU A 96 5 4
HELIX 5 AA5 ASN A 97 ARG A 107 1 11
HELIX 6 AA6 ASP A 119 LEU A 134 1 16
HELIX 7 AA7 PRO A 135 MET A 137 5 3
HELIX 8 AA8 THR A 156 CYS A 166 1 11
HELIX 9 AA9 ASP A 171 PHE A 200 1 30
HELIX 10 AB1 CYS A 217 SER A 234 1 18
HELIX 11 AB2 ASP A 266 MET A 276 1 11
HELIX 12 AB3 ASN A 302 SER A 313 1 12
HELIX 13 AB4 GLY A 317 GLN A 331 1 15
HELIX 14 AB5 ASP A 349 GLN A 356 1 8
HELIX 15 AB6 TRP A 363 GLY A 374 1 12
HELIX 16 AB7 GLY A 402 VAL A 420 1 19
HELIX 17 AB8 PRO A 450 VAL A 455 5 6
HELIX 18 AB9 MET A 456 SER A 460 5 5
HELIX 19 AC1 THR A 495 HIS A 506 1 12
HELIX 20 AC2 SER A 513 ARG A 524 1 12
HELIX 21 AC3 THR A 538 ASP A 552 1 15
HELIX 22 AC4 ALA A 553 VAL A 556 5 4
HELIX 23 AC5 LEU A 557 GLN A 573 1 17
HELIX 24 AC6 ASP A 577 SER A 599 1 23
HELIX 25 AC7 ILE A 600 PHE A 611 1 12
HELIX 26 AC8 GLY B -1 GLY B 13 1 15
HELIX 27 AC9 SER B 17 CYS B 24 1 8
HELIX 28 AD1 ASN B 32 ASN B 42 1 11
HELIX 29 AD2 ASP B 44 GLY B 49 1 6
SHEET 1 AA1 6 SER A 27 LYS A 30 0
SHEET 2 AA1 6 SER A 37 THR A 44 -1 O GLU A 40 N SER A 27
SHEET 3 AA1 6 PRO A 49 SER A 56 -1 O PHE A 52 N TYR A 41
SHEET 4 AA1 6 LYS A 2 ALA A 8 1 N VAL A 4 O ARG A 51
SHEET 5 AA1 6 TYR A 111 TRP A 115 1 O TRP A 115 N VAL A 7
SHEET 6 AA1 6 VAL A 147 ARG A 149 1 O PHE A 148 N ILE A 112
SHEET 1 AA2 2 MET A 62 PHE A 66 0
SHEET 2 AA2 2 THR A 87 GLU A 91 -1 O LYS A 90 N THR A 63
SHEET 1 AA3 7 SER A 254 LEU A 256 0
SHEET 2 AA3 7 THR A 239 ASN A 248 -1 N VAL A 247 O LEU A 255
SHEET 3 AA3 7 ALA A 475 GLN A 487 -1 O GLY A 479 N LYS A 246
SHEET 4 AA3 7 GLU A 282 LYS A 295 -1 N ALA A 283 O PHE A 476
SHEET 5 AA3 7 CYS A 424 ILE A 435 -1 O SER A 432 N GLU A 286
SHEET 6 AA3 7 GLU A 438 SER A 449 -1 O PHE A 440 N PHE A 433
SHEET 7 AA3 7 ASP A 258 TRP A 259 -1 N ASP A 258 O THR A 441
SHEET 1 AA4 2 VAL A 527 GLU A 530 0
SHEET 2 AA4 2 ARG A 534 PRO A 537 -1 O ARG A 534 N GLU A 530
SHEET 1 AA5 8 LYS B 64 GLU B 66 0
SHEET 2 AA5 8 ILE B 132 LYS B 136 -1 O VAL B 133 N LEU B 65
SHEET 3 AA5 8 PHE B 139 LEU B 142 -1 O LEU B 141 N ASP B 134
SHEET 4 AA5 8 SER B 105 GLU B 110 1 N VAL B 109 O LEU B 140
SHEET 5 AA5 8 LEU B 95 THR B 100 -1 N MET B 99 O CYS B 106
SHEET 6 AA5 8 CYS B 69 ASN B 78 -1 N GLN B 74 O GLN B 98
SHEET 7 AA5 8 LYS B 126 LEU B 129 -1 O VAL B 127 N LEU B 71
SHEET 8 AA5 8 THR B 147 GLY B 151 -1 O THR B 148 N LYS B 128
LINK OE1 GLU A 9 MG MG A 701 1555 1555 2.63
CISPEP 1 VAL A 76 ASP A 77 0 7.51
CISPEP 2 GLY A 142 GLY A 143 0 -7.35
CISPEP 3 GLY B 67 PRO B 68 0 0.87
CISPEP 4 ARG B 93 MET B 94 0 12.65
SITE 1 AC1 2 GLU A 9 GLU A 121
CRYST1 173.563 173.563 111.810 90.00 90.00 120.00 P 65 6
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 0.005762 0.003326 0.000000 0.00000
SCALE2 0.000000 0.006653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008944 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
