HEADER PROTEIN BINDING 17-FEB-18 5ZCJ
TITLE CRYSTAL STRUCTURE OF COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUDOR-INTERACTING REPAIR REGULATOR PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NUDT16-LIKE PROTEIN 1,PROTEIN SYNDESMOS;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TP53-BINDING PROTEIN 1;
COMPND 8 CHAIN: C;
COMPND 9 SYNONYM: P53BP1;
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: NUDT16L1, SDOS, TIRR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: TP53BP1;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS COMPLEX, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WANG,Z.YUAN,Y.CUI,R.XIE,M.WANG,Y.MA,X.YU,X.LIU
REVDAT 1 27-JUN-18 5ZCJ 0
JRNL AUTH J.WANG,Z.YUAN,Y.CUI,R.XIE,M.WANG,Y.MA,X.YU,X.LIU
JRNL TITL CRYSTAL STRUCTURE OF COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2932)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.150
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 45400
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.330
REMARK 3 FREE R VALUE TEST SET COUNT : 1966
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 19.9178 - 4.8088 0.98 3161 143 0.2029 0.1914
REMARK 3 2 4.8088 - 3.8258 0.99 3158 143 0.1530 0.1854
REMARK 3 3 3.8258 - 3.3448 0.99 3178 144 0.1647 0.2067
REMARK 3 4 3.3448 - 3.0401 0.98 3105 141 0.1725 0.2133
REMARK 3 5 3.0401 - 2.8229 0.97 3098 142 0.1815 0.1961
REMARK 3 6 2.8229 - 2.6568 0.98 3141 142 0.1903 0.2260
REMARK 3 7 2.6568 - 2.5241 0.99 3132 143 0.1938 0.2466
REMARK 3 8 2.5241 - 2.4144 0.99 3142 141 0.2010 0.2310
REMARK 3 9 2.4144 - 2.3216 0.99 3130 143 0.2044 0.2293
REMARK 3 10 2.3216 - 2.2416 0.98 3105 138 0.2020 0.2520
REMARK 3 11 2.2416 - 2.1716 0.98 3110 141 0.2074 0.2537
REMARK 3 12 2.1716 - 2.1096 0.95 3004 139 0.2270 0.2355
REMARK 3 13 2.1096 - 2.0541 0.94 2953 133 0.2420 0.2844
REMARK 3 14 2.0541 - 2.0040 0.95 3017 133 0.2549 0.2889
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.810
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 : 0.002 4221
REMARK 3 ANGLE : 0.509 5698
REMARK 3 CHIRALITY : 0.038 624
REMARK 3 PLANARITY : 0.003 732
REMARK 3 DIHEDRAL : 4.933 3278
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 5ZCJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006809.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 308418
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 19.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7 M AMMONIUM TARTRATE, 0.1 M SODIUM
REMARK 280 ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 55.57200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.96100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 55.57200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 51.96100
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: TRIMERIC
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 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 2
REMARK 465 PRO A 3
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 LYS A 205
REMARK 465 LEU A 206
REMARK 465 LEU A 207
REMARK 465 PRO A 208
REMARK 465 ALA A 209
REMARK 465 SER A 210
REMARK 465 SER A 211
REMARK 465 GLY B 2
REMARK 465 PRO B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 PRO B 208
REMARK 465 ALA B 209
REMARK 465 SER B 210
REMARK 465 SER B 211
REMARK 465 GLY C 1455
REMARK 465 PRO C 1456
REMARK 465 GLY C 1457
REMARK 465 SER C 1458
REMARK 465 ARG C 1459
REMARK 465 SER C 1460
REMARK 465 ASP C 1461
REMARK 465 SER C 1462
REMARK 465 PRO C 1463
REMARK 465 GLU C 1464
REMARK 465 ILE C 1465
REMARK 465 PRO C 1466
REMARK 465 PHE C 1467
REMARK 465 GLN C 1468
REMARK 465 ALA C 1469
REMARK 465 ALA C 1470
REMARK 465 ALA C 1471
REMARK 465 GLY C 1472
REMARK 465 PRO C 1473
REMARK 465 SER C 1474
REMARK 465 ASP C 1475
REMARK 465 GLY C 1476
REMARK 465 LEU C 1477
REMARK 465 ASP C 1478
REMARK 465 ALA C 1479
REMARK 465 SER C 1480
REMARK 465 SER C 1481
REMARK 465 PRO C 1482
REMARK 465 GLY C 1483
REMARK 465 ASN C 1484
REMARK 465 SER C 1485
REMARK 465 ALA C 1607
REMARK 465 VAL C 1608
REMARK 465 THR C 1609
REMARK 465 PRO C 1610
REMARK 465 LEU C 1611
REMARK 465 THR C 1612
REMARK 465 LYS C 1613
REMARK 465 ALA C 1614
REMARK 465 ALA C 1615
REMARK 465 ASP C 1616
REMARK 465 ILE C 1617
REMARK 465 SER C 1618
REMARK 465 LEU C 1619
REMARK 465 ASP C 1620
REMARK 465 ASN C 1621
REMARK 465 LEU C 1622
REMARK 465 VAL C 1623
REMARK 465 GLU C 1624
REMARK 465 GLY C 1625
REMARK 465 LYS C 1626
REMARK 465 ARG C 1627
REMARK 465 LYS C 1628
REMARK 465 ARG C 1629
REMARK 465 ARG C 1630
REMARK 465 SER C 1631
REMARK 465 ASN C 1632
REMARK 465 VAL C 1633
REMARK 465 SER C 1634
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 GLY A 83 NH2 ARG A 133 2.12
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 PHE A 41 16.92 57.78
REMARK 500 ARG A 47 -72.10 63.71
REMARK 500 LEU A 89 132.06 70.86
REMARK 500 LEU A 137 -87.61 -122.22
REMARK 500 VAL A 154 -30.87 -131.30
REMARK 500 ARG B 43 -40.69 -149.58
REMARK 500 ARG B 47 -66.15 65.58
REMARK 500 CYS B 88 24.86 -70.60
REMARK 500 LEU B 137 -98.08 -117.61
REMARK 500 VAL B 154 -30.40 -131.47
REMARK 500 GLU C1551 17.60 86.76
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5ZCJ A 6 211 UNP Q9BRJ7 TIRR_HUMAN 6 211
DBREF 5ZCJ B 6 211 UNP Q9BRJ7 TIRR_HUMAN 6 211
DBREF 5ZCJ C 1459 1634 UNP Q12888 TP53B_HUMAN 1459 1634
SEQADV 5ZCJ GLY A 2 UNP Q9BRJ7 EXPRESSION TAG
SEQADV 5ZCJ PRO A 3 UNP Q9BRJ7 EXPRESSION TAG
SEQADV 5ZCJ GLY A 4 UNP Q9BRJ7 EXPRESSION TAG
SEQADV 5ZCJ SER A 5 UNP Q9BRJ7 EXPRESSION TAG
SEQADV 5ZCJ GLY B 2 UNP Q9BRJ7 EXPRESSION TAG
SEQADV 5ZCJ PRO B 3 UNP Q9BRJ7 EXPRESSION TAG
SEQADV 5ZCJ GLY B 4 UNP Q9BRJ7 EXPRESSION TAG
SEQADV 5ZCJ SER B 5 UNP Q9BRJ7 EXPRESSION TAG
SEQADV 5ZCJ GLY C 1455 UNP Q12888 EXPRESSION TAG
SEQADV 5ZCJ PRO C 1456 UNP Q12888 EXPRESSION TAG
SEQADV 5ZCJ GLY C 1457 UNP Q12888 EXPRESSION TAG
SEQADV 5ZCJ SER C 1458 UNP Q12888 EXPRESSION TAG
SEQRES 1 A 210 GLY PRO GLY SER VAL PRO GLU LEU LYS GLN ILE SER ARG
SEQRES 2 A 210 VAL GLU ALA MET ARG LEU GLY PRO GLY TRP SER HIS SER
SEQRES 3 A 210 CYS HIS ALA MET LEU TYR ALA ALA ASN PRO GLY GLN LEU
SEQRES 4 A 210 PHE GLY ARG ILE PRO MET ARG PHE SER VAL LEU MET GLN
SEQRES 5 A 210 MET ARG PHE ASP GLY LEU LEU GLY PHE PRO GLY GLY PHE
SEQRES 6 A 210 VAL ASP ARG ARG PHE TRP SER LEU GLU ASP GLY LEU ASN
SEQRES 7 A 210 ARG VAL LEU GLY LEU GLY LEU GLY CYS LEU ARG LEU THR
SEQRES 8 A 210 GLU ALA ASP TYR LEU SER SER HIS LEU THR GLU GLY PRO
SEQRES 9 A 210 HIS ARG VAL VAL ALA HIS LEU TYR ALA ARG GLN LEU THR
SEQRES 10 A 210 LEU GLU GLN LEU HIS ALA VAL GLU ILE SER ALA VAL HIS
SEQRES 11 A 210 SER ARG ASP HIS GLY LEU GLU VAL LEU GLY LEU VAL ARG
SEQRES 12 A 210 VAL PRO LEU TYR THR GLN LYS ASP ARG VAL GLY GLY PHE
SEQRES 13 A 210 PRO ASN PHE LEU SER ASN ALA PHE VAL SER THR ALA LYS
SEQRES 14 A 210 CYS GLN LEU LEU PHE ALA LEU LYS VAL LEU ASN MET MET
SEQRES 15 A 210 PRO GLU GLU LYS LEU VAL GLU ALA LEU ALA ALA ALA THR
SEQRES 16 A 210 GLU LYS GLN LYS LYS ALA LEU GLU LYS LEU LEU PRO ALA
SEQRES 17 A 210 SER SER
SEQRES 1 B 210 GLY PRO GLY SER VAL PRO GLU LEU LYS GLN ILE SER ARG
SEQRES 2 B 210 VAL GLU ALA MET ARG LEU GLY PRO GLY TRP SER HIS SER
SEQRES 3 B 210 CYS HIS ALA MET LEU TYR ALA ALA ASN PRO GLY GLN LEU
SEQRES 4 B 210 PHE GLY ARG ILE PRO MET ARG PHE SER VAL LEU MET GLN
SEQRES 5 B 210 MET ARG PHE ASP GLY LEU LEU GLY PHE PRO GLY GLY PHE
SEQRES 6 B 210 VAL ASP ARG ARG PHE TRP SER LEU GLU ASP GLY LEU ASN
SEQRES 7 B 210 ARG VAL LEU GLY LEU GLY LEU GLY CYS LEU ARG LEU THR
SEQRES 8 B 210 GLU ALA ASP TYR LEU SER SER HIS LEU THR GLU GLY PRO
SEQRES 9 B 210 HIS ARG VAL VAL ALA HIS LEU TYR ALA ARG GLN LEU THR
SEQRES 10 B 210 LEU GLU GLN LEU HIS ALA VAL GLU ILE SER ALA VAL HIS
SEQRES 11 B 210 SER ARG ASP HIS GLY LEU GLU VAL LEU GLY LEU VAL ARG
SEQRES 12 B 210 VAL PRO LEU TYR THR GLN LYS ASP ARG VAL GLY GLY PHE
SEQRES 13 B 210 PRO ASN PHE LEU SER ASN ALA PHE VAL SER THR ALA LYS
SEQRES 14 B 210 CYS GLN LEU LEU PHE ALA LEU LYS VAL LEU ASN MET MET
SEQRES 15 B 210 PRO GLU GLU LYS LEU VAL GLU ALA LEU ALA ALA ALA THR
SEQRES 16 B 210 GLU LYS GLN LYS LYS ALA LEU GLU LYS LEU LEU PRO ALA
SEQRES 17 B 210 SER SER
SEQRES 1 C 180 GLY PRO GLY SER ARG SER ASP SER PRO GLU ILE PRO PHE
SEQRES 2 C 180 GLN ALA ALA ALA GLY PRO SER ASP GLY LEU ASP ALA SER
SEQRES 3 C 180 SER PRO GLY ASN SER PHE VAL GLY LEU ARG VAL VAL ALA
SEQRES 4 C 180 LYS TRP SER SER ASN GLY TYR PHE TYR SER GLY LYS ILE
SEQRES 5 C 180 THR ARG ASP VAL GLY ALA GLY LYS TYR LYS LEU LEU PHE
SEQRES 6 C 180 ASP ASP GLY TYR GLU CYS ASP VAL LEU GLY LYS ASP ILE
SEQRES 7 C 180 LEU LEU CYS ASP PRO ILE PRO LEU ASP THR GLU VAL THR
SEQRES 8 C 180 ALA LEU SER GLU ASP GLU TYR PHE SER ALA GLY VAL VAL
SEQRES 9 C 180 LYS GLY HIS ARG LYS GLU SER GLY GLU LEU TYR TYR SER
SEQRES 10 C 180 ILE GLU LYS GLU GLY GLN ARG LYS TRP TYR LYS ARG MET
SEQRES 11 C 180 ALA VAL ILE LEU SER LEU GLU GLN GLY ASN ARG LEU ARG
SEQRES 12 C 180 GLU GLN TYR GLY LEU GLY PRO TYR GLU ALA VAL THR PRO
SEQRES 13 C 180 LEU THR LYS ALA ALA ASP ILE SER LEU ASP ASN LEU VAL
SEQRES 14 C 180 GLU GLY LYS ARG LYS ARG ARG SER ASN VAL SER
FORMUL 4 HOH *393(H2 O)
HELIX 1 AA1 SER A 13 MET A 18 1 6
HELIX 2 AA2 PHE A 41 ARG A 43 5 3
HELIX 3 AA3 SER A 73 LEU A 86 1 14
HELIX 4 AA4 THR A 92 ALA A 94 5 3
HELIX 5 AA5 THR A 118 VAL A 130 1 13
HELIX 6 AA6 GLY A 156 SER A 162 1 7
HELIX 7 AA7 VAL A 166 LEU A 180 1 15
HELIX 8 AA8 PRO A 184 LEU A 203 1 20
HELIX 9 AA9 SER B 13 MET B 18 1 6
HELIX 10 AB1 PHE B 41 ARG B 43 5 3
HELIX 11 AB2 SER B 73 LEU B 86 1 14
HELIX 12 AB3 THR B 92 ALA B 94 5 3
HELIX 13 AB4 THR B 118 HIS B 131 1 14
HELIX 14 AB5 GLY B 156 SER B 162 1 7
HELIX 15 AB6 VAL B 166 LEU B 180 1 15
HELIX 16 AB7 PRO B 184 GLU B 204 1 21
HELIX 17 AB8 SER C 1589 ARG C 1595 1 7
HELIX 18 AB9 LEU C 1596 GLY C 1601 1 6
SHEET 1 AA1 6 LYS A 10 GLN A 11 0
SHEET 2 AA1 6 TYR A 96 LEU A 101 -1 O LEU A 101 N LYS A 10
SHEET 3 AA1 6 VAL A 108 LEU A 117 -1 O ALA A 110 N HIS A 100
SHEET 4 AA1 6 SER A 25 LEU A 40 1 N MET A 31 O TYR A 113
SHEET 5 AA1 6 ILE A 44 ARG A 55 -1 O ARG A 47 N ASN A 36
SHEET 6 AA1 6 GLY A 64 VAL A 67 0
SHEET 1 AA2 4 LEU A 60 GLY A 61 0
SHEET 2 AA2 4 ILE A 44 ARG A 55 -1 N GLN A 53 O GLY A 61
SHEET 3 AA2 4 SER A 25 LEU A 40 -1 N ASN A 36 O ARG A 47
SHEET 4 AA2 4 VAL A 139 VAL A 145 0
SHEET 1 AA3 6 LYS B 10 GLN B 11 0
SHEET 2 AA3 6 TYR B 96 LEU B 101 -1 O LEU B 101 N LYS B 10
SHEET 3 AA3 6 VAL B 108 LEU B 117 -1 O ALA B 110 N HIS B 100
SHEET 4 AA3 6 SER B 25 LEU B 40 1 N SER B 27 O HIS B 111
SHEET 5 AA3 6 ILE B 44 ARG B 55 -1 O ILE B 44 N LEU B 40
SHEET 6 AA3 6 GLY B 64 VAL B 67 0
SHEET 1 AA4 4 LEU B 60 GLY B 61 0
SHEET 2 AA4 4 ILE B 44 ARG B 55 -1 N GLN B 53 O GLY B 61
SHEET 3 AA4 4 SER B 25 LEU B 40 -1 N LEU B 40 O ILE B 44
SHEET 4 AA4 4 VAL B 139 ARG B 144 0
SHEET 1 AA5 5 GLU C1524 LEU C1528 0
SHEET 2 AA5 5 LYS C1514 PHE C1519 -1 N TYR C1515 O VAL C1527
SHEET 3 AA5 5 TYR C1502 GLY C1511 -1 N THR C1507 O LYS C1516
SHEET 4 AA5 5 ARG C1490 ALA C1493 -1 N ALA C1493 O TYR C1502
SHEET 5 AA5 5 ILE C1532 LEU C1533 -1 O LEU C1533 N VAL C1492
SHEET 1 AA6 5 GLN C1577 LYS C1582 0
SHEET 2 AA6 5 GLU C1567 LYS C1574 -1 N TYR C1570 O TYR C1581
SHEET 3 AA6 5 PHE C1553 GLU C1564 -1 N LYS C1559 O SER C1571
SHEET 4 AA6 5 GLU C1543 LEU C1547 -1 N ALA C1546 O SER C1554
SHEET 5 AA6 5 VAL C1586 ILE C1587 -1 O ILE C1587 N THR C1545
CISPEP 1 GLY A 104 PRO A 105 0 4.11
CISPEP 2 GLY B 104 PRO B 105 0 -3.10
CISPEP 3 LEU B 206 LEU B 207 0 1.78
CISPEP 4 ASP C 1536 PRO C 1537 0 -1.87
CISPEP 5 GLY C 1603 PRO C 1604 0 2.98
CRYST1 111.144 103.922 61.470 90.00 95.46 90.00 C 1 2 1 8
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 0.008997 0.000000 0.000860 0.00000
SCALE2 0.000000 0.009623 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016342 0.00000
(ATOM LINES ARE NOT SHOWN.)
END