HEADER TRANSCRIPTION 09-MAR-16 5IP9
TITLE STRUCTURE OF RNA POLYMERASE II-TFIIF COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNA POLYMERASE II SUBUNIT B1,DNA-DIRECTED RNA POLYMERASE III
COMPND 5 LARGEST SUBUNIT,RNA POLYMERASE II SUBUNIT B220;
COMPND 6 EC: 2.7.7.6;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: RNA POLYMERASE II SUBUNIT 2,B150,DNA-DIRECTED RNA POLYMERASE
COMPND 11 II 140 KDA POLYPEPTIDE;
COMPND 12 EC: 2.7.7.6;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3;
COMPND 15 CHAIN: C;
COMPND 16 SYNONYM: RNA POLYMERASE II SUBUNIT B3,B44.5,DNA-DIRECTED RNA
COMPND 17 POLYMERASE II 45 KDA POLYPEPTIDE;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4;
COMPND 20 CHAIN: D;
COMPND 21 SYNONYM: RNA POLYMERASE II SUBUNIT B4,B32,DNA-DIRECTED RNA POLYMERASE
COMPND 22 II 32 KDA POLYPEPTIDE;
COMPND 23 MOL_ID: 5;
COMPND 24 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1;
COMPND 25 CHAIN: E;
COMPND 26 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC1,ABC27,DNA-DIRECTED
COMPND 27 RNA POLYMERASES I,AND III 27 KDA POLYPEPTIDE;
COMPND 28 MOL_ID: 6;
COMPND 29 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2;
COMPND 30 CHAIN: F;
COMPND 31 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC2,ABC23,DNA-DIRECTED
COMPND 32 RNA POLYMERASES I,AND III 23 KDA POLYPEPTIDE;
COMPND 33 MOL_ID: 7;
COMPND 34 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7;
COMPND 35 CHAIN: G;
COMPND 36 SYNONYM: RNA POLYMERASE II SUBUNIT B7,B16;
COMPND 37 MOL_ID: 8;
COMPND 38 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3;
COMPND 39 CHAIN: H;
COMPND 40 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC3,ABC14.4,ABC14.5,
COMPND 41 DNA-DIRECTED RNA POLYMERASES I,AND III 14.5 KDA POLYPEPTIDE;
COMPND 42 MOL_ID: 9;
COMPND 43 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9;
COMPND 44 CHAIN: I;
COMPND 45 SYNONYM: RNA POLYMERASE II SUBUNIT B9,B12.6,DNA-DIRECTED RNA
COMPND 46 POLYMERASE II 14.2 KDA POLYPEPTIDE,DNA-DIRECTED RNA POLYMERASE II
COMPND 47 SUBUNIT 9;
COMPND 48 MOL_ID: 10;
COMPND 49 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5;
COMPND 50 CHAIN: J;
COMPND 51 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC5,ABC10-BETA,ABC8,
COMPND 52 DNA-DIRECTED RNA POLYMERASES I,AND III 8.3 KDA POLYPEPTIDE;
COMPND 53 MOL_ID: 11;
COMPND 54 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11;
COMPND 55 CHAIN: K;
COMPND 56 SYNONYM: RNA POLYMERASE II SUBUNIT B11,B13.6,DNA-DIRECTED RNA
COMPND 57 POLYMERASE II 13.6 KDA POLYPEPTIDE;
COMPND 58 MOL_ID: 12;
COMPND 59 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC4;
COMPND 60 CHAIN: L;
COMPND 61 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC4,ABC10-ALPHA;
COMPND 62 MOL_ID: 13;
COMPND 63 MOLECULE: PHE-ILE-LYS-ARG-ASP-ARG-MET-ARG-ARG-ASN-PHE-LEU-ARG-MET-
COMPND 64 ARG;
COMPND 65 CHAIN: Q;
COMPND 66 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 8 ORGANISM_TAXID: 4932;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 4932;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 15 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 16 ORGANISM_TAXID: 4932;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 4932;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 27 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 28 ORGANISM_TAXID: 4932;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 31 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 32 ORGANISM_TAXID: 4932;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 35 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 36 ORGANISM_TAXID: 4932;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 39 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 40 ORGANISM_TAXID: 4932;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 4932;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 47 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 48 ORGANISM_TAXID: 4932;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 51 ORGANISM_TAXID: 4932;
SOURCE 52 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 53 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.PLASCHKA,M.HANTSCHE,C.DIENEMANN,C.BURZINSKI,J.PLITZKO,P.CRAMER
REVDAT 4 10-JAN-24 5IP9 1 REMARK
REVDAT 3 08-JUN-16 5IP9 1 JRNL
REVDAT 2 25-MAY-16 5IP9 1 JRNL
REVDAT 1 11-MAY-16 5IP9 0
JRNL AUTH C.PLASCHKA,M.HANTSCHE,C.DIENEMANN,C.BURZINSKI,J.PLITZKO,
JRNL AUTH 2 P.CRAMER
JRNL TITL TRANSCRIPTION INITIATION COMPLEX STRUCTURES ELUCIDATE DNA
JRNL TITL 2 OPENING.
JRNL REF NATURE V. 533 353 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 27193681
JRNL DOI 10.1038/NATURE17990
REMARK 2
REMARK 2 RESOLUTION. 3.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 112717
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2265
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 4.00
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 8240
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2283
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8085
REMARK 3 BIN R VALUE (WORKING SET) : 0.2272
REMARK 3 BIN FREE R VALUE : 0.2915
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.88
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 155
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 31330
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 99.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 130.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.84060
REMARK 3 B22 (A**2) : 25.52380
REMARK 3 B33 (A**2) : -29.36440
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.385
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.383
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 31891 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 43050 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 11507 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 859 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 4553 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 31891 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 3 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 4206 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : 38 ; 1.000 ; HARMONIC
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 37326 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.26
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.74
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 23.94
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|3 - A|81 }
REMARK 3 ORIGIN FOR THE GROUP (A): 98.4813 31.7277 -37.8527
REMARK 3 T TENSOR
REMARK 3 T11: -0.3162 T22: 0.1965
REMARK 3 T33: -0.3533 T12: -0.0426
REMARK 3 T13: 0.1301 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 8.6856 L22: 2.3303
REMARK 3 L33: 2.1122 L12: 1.4480
REMARK 3 L13: 0.5532 L23: -0.3512
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: 0.6308 S13: -0.7718
REMARK 3 S21: 0.0160 S22: -0.0786 S23: -0.0890
REMARK 3 S31: 0.4862 S32: -0.3155 S33: 0.0901
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|82 - A|323 }
REMARK 3 ORIGIN FOR THE GROUP (A): 91.5133 59.4881 -40.8573
REMARK 3 T TENSOR
REMARK 3 T11: -0.4878 T22: 0.1720
REMARK 3 T33: -0.0689 T12: 0.1722
REMARK 3 T13: -0.0505 T23: 0.3727
REMARK 3 L TENSOR
REMARK 3 L11: 1.1078 L22: 3.7726
REMARK 3 L33: 1.6918 L12: 0.7408
REMARK 3 L13: 0.2838 L23: -0.7681
REMARK 3 S TENSOR
REMARK 3 S11: -0.0365 S12: 0.3578 S13: 0.3214
REMARK 3 S21: -0.0055 S22: -0.1716 S23: 0.2615
REMARK 3 S31: -0.1290 S32: -0.1963 S33: 0.2081
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|324 - A|659 }
REMARK 3 ORIGIN FOR THE GROUP (A): 125.8290 36.6334 5.1955
REMARK 3 T TENSOR
REMARK 3 T11: -0.1770 T22: -0.0729
REMARK 3 T33: -0.0512 T12: -0.0291
REMARK 3 T13: 0.0095 T23: 0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 0.3186 L22: 0.4974
REMARK 3 L33: 1.2715 L12: 0.2160
REMARK 3 L13: 0.4841 L23: -0.1808
REMARK 3 S TENSOR
REMARK 3 S11: 0.0388 S12: 0.0901 S13: 0.1592
REMARK 3 S21: 0.2445 S22: -0.0949 S23: -0.0970
REMARK 3 S31: 0.1054 S32: 0.0777 S33: 0.0561
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|660 - A|831 }
REMARK 3 ORIGIN FOR THE GROUP (A): 103.5320 69.3658 25.3714
REMARK 3 T TENSOR
REMARK 3 T11: 0.1958 T22: -0.2727
REMARK 3 T33: 0.0029 T12: -0.0695
REMARK 3 T13: 0.2098 T23: -0.2932
REMARK 3 L TENSOR
REMARK 3 L11: 1.2563 L22: 2.6085
REMARK 3 L33: 0.0000 L12: -0.7988
REMARK 3 L13: -0.3539 L23: -0.4075
REMARK 3 S TENSOR
REMARK 3 S11: -0.0709 S12: 0.0712 S13: 0.4447
REMARK 3 S21: 0.7812 S22: -0.1523 S23: 0.1204
REMARK 3 S31: -0.2145 S32: 0.1202 S33: 0.2232
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|832 - A|1127 }
REMARK 3 ORIGIN FOR THE GROUP (A): 140.0720 66.8794 -2.6252
REMARK 3 T TENSOR
REMARK 3 T11: -0.4100 T22: -0.1952
REMARK 3 T33: 0.3081 T12: -0.0899
REMARK 3 T13: 0.0864 T23: 0.1595
REMARK 3 L TENSOR
REMARK 3 L11: 2.2422 L22: 0.9600
REMARK 3 L33: 0.1930 L12: 0.6899
REMARK 3 L13: 0.6766 L23: 0.0998
REMARK 3 S TENSOR
REMARK 3 S11: 0.1942 S12: -0.0491 S13: 0.3381
REMARK 3 S21: 0.1459 S22: -0.1143 S23: -0.1895
REMARK 3 S31: 0.0129 S32: -0.0452 S33: -0.0799
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { A|1128 - A|1329 }
REMARK 3 ORIGIN FOR THE GROUP (A): 101.9540 104.5700 0.3650
REMARK 3 T TENSOR
REMARK 3 T11: -0.4963 T22: -0.4866
REMARK 3 T33: 0.9119 T12: 0.0782
REMARK 3 T13: 0.0295 T23: -0.1737
REMARK 3 L TENSOR
REMARK 3 L11: 5.7121 L22: 1.7538
REMARK 3 L33: 0.5359 L12: -3.8218
REMARK 3 L13: 0.3872 L23: -0.6515
REMARK 3 S TENSOR
REMARK 3 S11: -0.2432 S12: -0.1523 S13: 0.7280
REMARK 3 S21: 0.1176 S22: 0.1192 S23: -0.5719
REMARK 3 S31: 0.0082 S32: -0.0680 S33: 0.1240
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { A|1330 - A|1454 }
REMARK 3 ORIGIN FOR THE GROUP (A): 118.9870 59.1296 -18.4193
REMARK 3 T TENSOR
REMARK 3 T11: -0.3796 T22: -0.0720
REMARK 3 T33: 0.2408 T12: 0.0698
REMARK 3 T13: 0.1375 T23: 0.1985
REMARK 3 L TENSOR
REMARK 3 L11: 0.1209 L22: 1.2923
REMARK 3 L33: 0.3446 L12: 0.1128
REMARK 3 L13: 0.7418 L23: 0.3074
REMARK 3 S TENSOR
REMARK 3 S11: 0.0923 S12: 0.3360 S13: 0.6415
REMARK 3 S21: -0.0812 S22: -0.1882 S23: -0.0539
REMARK 3 S31: 0.1441 S32: -0.0859 S33: 0.0960
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { B|20 - B|234 }
REMARK 3 ORIGIN FOR THE GROUP (A): 66.7656 44.5209 10.4976
REMARK 3 T TENSOR
REMARK 3 T11: -0.4349 T22: -0.1978
REMARK 3 T33: 0.7146 T12: 0.0502
REMARK 3 T13: 0.3111 T23: 0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 0.4066 L22: 0.4765
REMARK 3 L33: 0.0000 L12: -1.2007
REMARK 3 L13: -0.0573 L23: -0.2680
REMARK 3 S TENSOR
REMARK 3 S11: 0.0649 S12: -0.1617 S13: -0.1258
REMARK 3 S21: 0.0911 S22: 0.1157 S23: 1.0227
REMARK 3 S31: -0.0720 S32: -0.1231 S33: -0.1806
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { B|235 - B|392 }
REMARK 3 ORIGIN FOR THE GROUP (A): 66.6463 83.6992 -5.8316
REMARK 3 T TENSOR
REMARK 3 T11: -0.4899 T22: -0.4411
REMARK 3 T33: 0.5365 T12: 0.2308
REMARK 3 T13: 0.1678 T23: -0.1786
REMARK 3 L TENSOR
REMARK 3 L11: 4.6774 L22: 4.9706
REMARK 3 L33: 2.0022 L12: 0.3692
REMARK 3 L13: 1.7798 L23: -1.0392
REMARK 3 S TENSOR
REMARK 3 S11: -0.1021 S12: 0.1098 S13: -0.2219
REMARK 3 S21: -0.1674 S22: 0.2288 S23: 0.2496
REMARK 3 S31: 0.0008 S32: -0.0229 S33: -0.1267
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: { B|393 - B|539 }
REMARK 3 ORIGIN FOR THE GROUP (A): 75.0726 51.6942 1.5771
REMARK 3 T TENSOR
REMARK 3 T11: -0.2016 T22: -0.2132
REMARK 3 T33: 0.3553 T12: 0.0591
REMARK 3 T13: 0.1810 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 1.7099 L22: 0.0000
REMARK 3 L33: 1.0085 L12: -0.2599
REMARK 3 L13: 1.1871 L23: 0.2972
REMARK 3 S TENSOR
REMARK 3 S11: -0.1232 S12: 0.2022 S13: 0.3413
REMARK 3 S21: -0.1947 S22: 0.2860 S23: 0.7447
REMARK 3 S31: -0.0611 S32: 0.2323 S33: -0.1628
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: { B|540 - B|735 }
REMARK 3 ORIGIN FOR THE GROUP (A): 69.3551 68.3513 26.2079
REMARK 3 T TENSOR
REMARK 3 T11: -0.1971 T22: -0.1886
REMARK 3 T33: 0.4438 T12: 0.2622
REMARK 3 T13: 0.4559 T23: -0.1508
REMARK 3 L TENSOR
REMARK 3 L11: 0.0124 L22: 0.6168
REMARK 3 L33: 1.1777 L12: -1.8158
REMARK 3 L13: 0.5295 L23: -1.0387
REMARK 3 S TENSOR
REMARK 3 S11: -0.1397 S12: -0.2839 S13: 0.3909
REMARK 3 S21: 0.3910 S22: -0.0838 S23: 0.4043
REMARK 3 S31: 0.0397 S32: -0.2054 S33: 0.2236
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: { B|736 - B|841 }
REMARK 3 ORIGIN FOR THE GROUP (A): 93.0351 42.3630 23.3411
REMARK 3 T TENSOR
REMARK 3 T11: -0.0265 T22: -0.1470
REMARK 3 T33: -0.0627 T12: -0.0292
REMARK 3 T13: 0.3595 T23: -0.1200
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 1.2727
REMARK 3 L33: 0.2832 L12: -1.1113
REMARK 3 L13: -0.3432 L23: -0.6990
REMARK 3 S TENSOR
REMARK 3 S11: -0.0844 S12: -0.1517 S13: 0.1527
REMARK 3 S21: 0.3967 S22: 0.2443 S23: 0.1331
REMARK 3 S31: 0.0109 S32: -0.0367 S33: -0.1599
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: { B|842 - B|974 }
REMARK 3 ORIGIN FOR THE GROUP (A): 86.7383 17.0139 -0.4611
REMARK 3 T TENSOR
REMARK 3 T11: 0.0393 T22: -0.2229
REMARK 3 T33: -0.0127 T12: -0.2322
REMARK 3 T13: 0.0848 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.0731 L22: 2.9393
REMARK 3 L33: 3.9570 L12: 0.8860
REMARK 3 L13: 1.7346 L23: 0.6106
REMARK 3 S TENSOR
REMARK 3 S11: -0.2268 S12: 0.0563 S13: -0.0141
REMARK 3 S21: -0.6760 S22: 0.5107 S23: 0.6559
REMARK 3 S31: -0.0122 S32: 0.4150 S33: -0.2839
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: { B|975 - B|1224 }
REMARK 3 ORIGIN FOR THE GROUP (A): 108.5410 38.3980 2.0771
REMARK 3 T TENSOR
REMARK 3 T11: -0.0726 T22: -0.0896
REMARK 3 T33: -0.1789 T12: 0.0201
REMARK 3 T13: 0.1315 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.4005 L22: 0.1217
REMARK 3 L33: 1.2961 L12: -0.0610
REMARK 3 L13: 0.0001 L23: -0.2142
REMARK 3 S TENSOR
REMARK 3 S11: 0.0458 S12: 0.1207 S13: 0.2393
REMARK 3 S21: 0.1750 S22: 0.0581 S23: 0.1170
REMARK 3 S31: 0.1720 S32: -0.0242 S33: -0.1039
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: { C|3 - C|268 }
REMARK 3 ORIGIN FOR THE GROUP (A): 110.5580 16.4462 36.2838
REMARK 3 T TENSOR
REMARK 3 T11: 0.3289 T22: -0.0372
REMARK 3 T33: -0.4998 T12: -0.0044
REMARK 3 T13: 0.1892 T23: 0.1795
REMARK 3 L TENSOR
REMARK 3 L11: 1.2011 L22: 1.1303
REMARK 3 L33: 0.1989 L12: -0.0013
REMARK 3 L13: 0.1119 L23: -0.0813
REMARK 3 S TENSOR
REMARK 3 S11: -0.0697 S12: -0.2970 S13: -0.2462
REMARK 3 S21: 0.7572 S22: 0.0507 S23: 0.0566
REMARK 3 S31: 0.2065 S32: 0.0593 S33: 0.0191
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: { D|4 - D|221 }
REMARK 3 ORIGIN FOR THE GROUP (A): 135.8650 29.8736 -65.5017
REMARK 3 T TENSOR
REMARK 3 T11: -0.4082 T22: 0.3883
REMARK 3 T33: -0.3327 T12: 0.1576
REMARK 3 T13: 0.0723 T23: -0.0920
REMARK 3 L TENSOR
REMARK 3 L11: 0.1493 L22: 1.0362
REMARK 3 L33: 4.3608 L12: -0.0894
REMARK 3 L13: -0.1183 L23: -0.1020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0490 S12: 0.3411 S13: -0.0356
REMARK 3 S21: 0.1851 S22: 0.1054 S23: -0.0264
REMARK 3 S31: 0.0613 S32: 0.5630 S33: -0.0564
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: { E|2 - E|215 }
REMARK 3 ORIGIN FOR THE GROUP (A): 126.9350 92.7723 -25.3168
REMARK 3 T TENSOR
REMARK 3 T11: -0.3138 T22: -0.3443
REMARK 3 T33: 0.5299 T12: -0.0698
REMARK 3 T13: 0.0802 T23: 0.4441
REMARK 3 L TENSOR
REMARK 3 L11: 1.2184 L22: 3.8608
REMARK 3 L33: 0.3438 L12: -0.2791
REMARK 3 L13: 0.0276 L23: 0.1160
REMARK 3 S TENSOR
REMARK 3 S11: 0.0579 S12: 0.1803 S13: 0.5267
REMARK 3 S21: -0.4658 S22: -0.1345 S23: -0.1336
REMARK 3 S31: -0.0553 S32: 0.1398 S33: 0.0766
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: { F|72 - F|155 }
REMARK 3 ORIGIN FOR THE GROUP (A): 139.6930 38.7219 -19.8766
REMARK 3 T TENSOR
REMARK 3 T11: -0.4251 T22: 0.1092
REMARK 3 T33: -0.0852 T12: 0.0760
REMARK 3 T13: 0.0670 T23: 0.1417
REMARK 3 L TENSOR
REMARK 3 L11: 1.3690 L22: 5.9984
REMARK 3 L33: 2.5307 L12: -0.1084
REMARK 3 L13: 0.0943 L23: -0.5483
REMARK 3 S TENSOR
REMARK 3 S11: 0.0511 S12: 0.1300 S13: 0.1567
REMARK 3 S21: 0.1530 S22: 0.0540 S23: -0.5106
REMARK 3 S31: 0.2068 S32: 0.2566 S33: -0.1051
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: { G|1 - G|171 }
REMARK 3 ORIGIN FOR THE GROUP (A): 126.3070 23.3184 -59.6886
REMARK 3 T TENSOR
REMARK 3 T11: -0.2775 T22: 0.2478
REMARK 3 T33: -0.1799 T12: 0.2464
REMARK 3 T13: 0.1366 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.2133 L22: 0.9729
REMARK 3 L33: 5.2945 L12: 0.1614
REMARK 3 L13: 1.3987 L23: 1.5536
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.0553 S13: -0.2424
REMARK 3 S21: 0.1371 S22: 0.0915 S23: 0.1147
REMARK 3 S31: 0.4664 S32: 0.3482 S33: -0.0957
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: { H|2 - H|146 }
REMARK 3 ORIGIN FOR THE GROUP (A): 152.2490 52.3540 36.3730
REMARK 3 T TENSOR
REMARK 3 T11: -0.0316 T22: 0.0424
REMARK 3 T33: -0.1398 T12: -0.3091
REMARK 3 T13: -0.4559 T23: -0.0660
REMARK 3 L TENSOR
REMARK 3 L11: 2.2831 L22: 3.9300
REMARK 3 L33: 1.4855 L12: 1.6483
REMARK 3 L13: 1.4426 L23: -1.0010
REMARK 3 S TENSOR
REMARK 3 S11: -0.1879 S12: -0.3275 S13: 0.4172
REMARK 3 S21: 0.5085 S22: -0.1378 S23: -0.6469
REMARK 3 S31: -0.2489 S32: 0.2969 S33: 0.3257
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: { I|2 - I|120 }
REMARK 3 ORIGIN FOR THE GROUP (A): 76.8884 99.3126 14.1705
REMARK 3 T TENSOR
REMARK 3 T11: 0.0117 T22: -0.3725
REMARK 3 T33: 0.6513 T12: 0.2739
REMARK 3 T13: 0.2978 T23: -0.2668
REMARK 3 L TENSOR
REMARK 3 L11: 0.6906 L22: 1.4295
REMARK 3 L33: 2.1602 L12: -1.5106
REMARK 3 L13: 1.4777 L23: -2.2116
REMARK 3 S TENSOR
REMARK 3 S11: -0.1531 S12: 0.1508 S13: 0.4143
REMARK 3 S21: 0.7644 S22: -0.0511 S23: 0.4612
REMARK 3 S31: -0.0218 S32: 0.1834 S33: 0.2041
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: { J|1 - J|65 }
REMARK 3 ORIGIN FOR THE GROUP (A): 91.1648 25.8414 37.5209
REMARK 3 T TENSOR
REMARK 3 T11: 0.2722 T22: -0.1338
REMARK 3 T33: -0.2687 T12: 0.0526
REMARK 3 T13: 0.4208 T23: 0.0531
REMARK 3 L TENSOR
REMARK 3 L11: 3.6668 L22: 0.7265
REMARK 3 L33: 0.5738 L12: 1.0445
REMARK 3 L13: -0.6038 L23: 0.4183
REMARK 3 S TENSOR
REMARK 3 S11: -0.0365 S12: 0.0965 S13: 0.2937
REMARK 3 S21: 0.6101 S22: 0.0852 S23: 0.2883
REMARK 3 S31: 0.1169 S32: 0.2386 S33: -0.0487
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: { K|2 - K|114 }
REMARK 3 ORIGIN FOR THE GROUP (A): 131.9630 17.3981 28.2003
REMARK 3 T TENSOR
REMARK 3 T11: 0.1054 T22: -0.0192
REMARK 3 T33: -0.3388 T12: 0.1733
REMARK 3 T13: -0.0821 T23: 0.1129
REMARK 3 L TENSOR
REMARK 3 L11: 1.1261 L22: 2.0994
REMARK 3 L33: 0.0000 L12: 0.5362
REMARK 3 L13: 0.5808 L23: -1.3593
REMARK 3 S TENSOR
REMARK 3 S11: -0.0662 S12: 0.3737 S13: -0.2548
REMARK 3 S21: 0.4154 S22: -0.1259 S23: -0.3196
REMARK 3 S31: 0.1145 S32: 0.2030 S33: 0.1922
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: { L|25 - L|70 }
REMARK 3 ORIGIN FOR THE GROUP (A): 76.3519 9.6497 9.1671
REMARK 3 T TENSOR
REMARK 3 T11: -0.1156 T22: -0.2557
REMARK 3 T33: 0.4577 T12: -0.2534
REMARK 3 T13: 0.2418 T23: 0.2206
REMARK 3 L TENSOR
REMARK 3 L11: 1.4696 L22: 3.2228
REMARK 3 L33: 3.5459 L12: 1.4449
REMARK 3 L13: 1.2652 L23: 1.1866
REMARK 3 S TENSOR
REMARK 3 S11: 0.1214 S12: 0.0711 S13: -0.4133
REMARK 3 S21: 0.4871 S22: -0.2633 S23: 1.3915
REMARK 3 S31: 0.5542 S32: -0.0450 S33: 0.1419
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5IP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219219.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-12
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91889
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112721
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.450
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.20600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 4.01100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.630
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3PO2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, SODIUM ACETATE, AMMONIUM
REMARK 280 ACETATE, HEPES, TCEP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295K
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 141.71000
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 141.71000
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 111.41000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 196.36500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 111.41000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 196.36500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 141.71000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 111.41000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 196.36500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 141.71000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 111.41000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 196.36500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIDECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 66670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 151010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -326.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, Q
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 VAL A 2
REMARK 465 LYS A 187
REMARK 465 ASP A 188
REMARK 465 ARG A 189
REMARK 465 ALA A 190
REMARK 465 THR A 191
REMARK 465 GLY A 192
REMARK 465 ASP A 193
REMARK 465 ALA A 194
REMARK 465 ALA A 1087
REMARK 465 GLY A 1088
REMARK 465 VAL A 1089
REMARK 465 ALA A 1090
REMARK 465 LEU A 1177
REMARK 465 ASP A 1178
REMARK 465 GLU A 1179
REMARK 465 GLU A 1180
REMARK 465 ALA A 1181
REMARK 465 GLU A 1182
REMARK 465 GLN A 1183
REMARK 465 SER A 1184
REMARK 465 PHE A 1185
REMARK 465 ASP A 1186
REMARK 465 PRO A 1245
REMARK 465 LYS A 1246
REMARK 465 SER A 1247
REMARK 465 LEU A 1248
REMARK 465 ASP A 1249
REMARK 465 ALA A 1250
REMARK 465 GLU A 1251
REMARK 465 THR A 1252
REMARK 465 GLU A 1253
REMARK 465 PRO A 1455
REMARK 465 GLU A 1456
REMARK 465 GLN A 1457
REMARK 465 LYS A 1458
REMARK 465 ILE A 1459
REMARK 465 THR A 1460
REMARK 465 GLU A 1461
REMARK 465 ILE A 1462
REMARK 465 GLU A 1463
REMARK 465 ASP A 1464
REMARK 465 GLY A 1465
REMARK 465 GLN A 1466
REMARK 465 ASP A 1467
REMARK 465 GLY A 1468
REMARK 465 GLY A 1469
REMARK 465 VAL A 1470
REMARK 465 THR A 1471
REMARK 465 PRO A 1472
REMARK 465 TYR A 1473
REMARK 465 SER A 1474
REMARK 465 ASN A 1475
REMARK 465 GLU A 1476
REMARK 465 SER A 1477
REMARK 465 GLY A 1478
REMARK 465 LEU A 1479
REMARK 465 VAL A 1480
REMARK 465 ASN A 1481
REMARK 465 ALA A 1482
REMARK 465 ASP A 1483
REMARK 465 LEU A 1484
REMARK 465 ASP A 1485
REMARK 465 VAL A 1486
REMARK 465 LYS A 1487
REMARK 465 ASP A 1488
REMARK 465 GLU A 1489
REMARK 465 LEU A 1490
REMARK 465 MET A 1491
REMARK 465 PHE A 1492
REMARK 465 SER A 1493
REMARK 465 PRO A 1494
REMARK 465 LEU A 1495
REMARK 465 VAL A 1496
REMARK 465 ASP A 1497
REMARK 465 SER A 1498
REMARK 465 GLY A 1499
REMARK 465 SER A 1500
REMARK 465 ASN A 1501
REMARK 465 ASP A 1502
REMARK 465 ALA A 1503
REMARK 465 MET A 1504
REMARK 465 ALA A 1505
REMARK 465 GLY A 1506
REMARK 465 GLY A 1507
REMARK 465 PHE A 1508
REMARK 465 THR A 1509
REMARK 465 ALA A 1510
REMARK 465 TYR A 1511
REMARK 465 GLY A 1512
REMARK 465 GLY A 1513
REMARK 465 ALA A 1514
REMARK 465 ASP A 1515
REMARK 465 TYR A 1516
REMARK 465 GLY A 1517
REMARK 465 GLU A 1518
REMARK 465 ALA A 1519
REMARK 465 THR A 1520
REMARK 465 SER A 1521
REMARK 465 PRO A 1522
REMARK 465 PHE A 1523
REMARK 465 GLY A 1524
REMARK 465 ALA A 1525
REMARK 465 TYR A 1526
REMARK 465 GLY A 1527
REMARK 465 GLU A 1528
REMARK 465 ALA A 1529
REMARK 465 PRO A 1530
REMARK 465 THR A 1531
REMARK 465 SER A 1532
REMARK 465 PRO A 1533
REMARK 465 GLY A 1534
REMARK 465 PHE A 1535
REMARK 465 GLY A 1536
REMARK 465 VAL A 1537
REMARK 465 SER A 1538
REMARK 465 SER A 1539
REMARK 465 PRO A 1540
REMARK 465 GLY A 1541
REMARK 465 PHE A 1542
REMARK 465 SER A 1543
REMARK 465 PRO A 1544
REMARK 465 THR A 1545
REMARK 465 SER A 1546
REMARK 465 PRO A 1547
REMARK 465 THR A 1548
REMARK 465 TYR A 1549
REMARK 465 SER A 1550
REMARK 465 PRO A 1551
REMARK 465 THR A 1552
REMARK 465 SER A 1553
REMARK 465 PRO A 1554
REMARK 465 ALA A 1555
REMARK 465 TYR A 1556
REMARK 465 SER A 1557
REMARK 465 PRO A 1558
REMARK 465 THR A 1559
REMARK 465 SER A 1560
REMARK 465 PRO A 1561
REMARK 465 SER A 1562
REMARK 465 TYR A 1563
REMARK 465 SER A 1564
REMARK 465 PRO A 1565
REMARK 465 THR A 1566
REMARK 465 SER A 1567
REMARK 465 PRO A 1568
REMARK 465 SER A 1569
REMARK 465 TYR A 1570
REMARK 465 SER A 1571
REMARK 465 PRO A 1572
REMARK 465 THR A 1573
REMARK 465 SER A 1574
REMARK 465 PRO A 1575
REMARK 465 SER A 1576
REMARK 465 TYR A 1577
REMARK 465 SER A 1578
REMARK 465 PRO A 1579
REMARK 465 THR A 1580
REMARK 465 SER A 1581
REMARK 465 PRO A 1582
REMARK 465 SER A 1583
REMARK 465 TYR A 1584
REMARK 465 SER A 1585
REMARK 465 PRO A 1586
REMARK 465 THR A 1587
REMARK 465 SER A 1588
REMARK 465 PRO A 1589
REMARK 465 SER A 1590
REMARK 465 TYR A 1591
REMARK 465 SER A 1592
REMARK 465 PRO A 1593
REMARK 465 THR A 1594
REMARK 465 SER A 1595
REMARK 465 PRO A 1596
REMARK 465 SER A 1597
REMARK 465 TYR A 1598
REMARK 465 SER A 1599
REMARK 465 PRO A 1600
REMARK 465 THR A 1601
REMARK 465 SER A 1602
REMARK 465 PRO A 1603
REMARK 465 SER A 1604
REMARK 465 TYR A 1605
REMARK 465 SER A 1606
REMARK 465 PRO A 1607
REMARK 465 THR A 1608
REMARK 465 SER A 1609
REMARK 465 PRO A 1610
REMARK 465 SER A 1611
REMARK 465 TYR A 1612
REMARK 465 SER A 1613
REMARK 465 PRO A 1614
REMARK 465 THR A 1615
REMARK 465 SER A 1616
REMARK 465 PRO A 1617
REMARK 465 SER A 1618
REMARK 465 TYR A 1619
REMARK 465 SER A 1620
REMARK 465 PRO A 1621
REMARK 465 THR A 1622
REMARK 465 SER A 1623
REMARK 465 PRO A 1624
REMARK 465 SER A 1625
REMARK 465 TYR A 1626
REMARK 465 SER A 1627
REMARK 465 PRO A 1628
REMARK 465 THR A 1629
REMARK 465 SER A 1630
REMARK 465 PRO A 1631
REMARK 465 SER A 1632
REMARK 465 TYR A 1633
REMARK 465 SER A 1634
REMARK 465 PRO A 1635
REMARK 465 THR A 1636
REMARK 465 SER A 1637
REMARK 465 PRO A 1638
REMARK 465 SER A 1639
REMARK 465 TYR A 1640
REMARK 465 SER A 1641
REMARK 465 PRO A 1642
REMARK 465 THR A 1643
REMARK 465 SER A 1644
REMARK 465 PRO A 1645
REMARK 465 SER A 1646
REMARK 465 TYR A 1647
REMARK 465 SER A 1648
REMARK 465 PRO A 1649
REMARK 465 THR A 1650
REMARK 465 SER A 1651
REMARK 465 PRO A 1652
REMARK 465 SER A 1653
REMARK 465 TYR A 1654
REMARK 465 SER A 1655
REMARK 465 PRO A 1656
REMARK 465 THR A 1657
REMARK 465 SER A 1658
REMARK 465 PRO A 1659
REMARK 465 ALA A 1660
REMARK 465 TYR A 1661
REMARK 465 SER A 1662
REMARK 465 PRO A 1663
REMARK 465 THR A 1664
REMARK 465 SER A 1665
REMARK 465 PRO A 1666
REMARK 465 SER A 1667
REMARK 465 TYR A 1668
REMARK 465 SER A 1669
REMARK 465 PRO A 1670
REMARK 465 THR A 1671
REMARK 465 SER A 1672
REMARK 465 PRO A 1673
REMARK 465 SER A 1674
REMARK 465 TYR A 1675
REMARK 465 SER A 1676
REMARK 465 PRO A 1677
REMARK 465 THR A 1678
REMARK 465 SER A 1679
REMARK 465 PRO A 1680
REMARK 465 SER A 1681
REMARK 465 TYR A 1682
REMARK 465 SER A 1683
REMARK 465 PRO A 1684
REMARK 465 THR A 1685
REMARK 465 SER A 1686
REMARK 465 PRO A 1687
REMARK 465 SER A 1688
REMARK 465 TYR A 1689
REMARK 465 SER A 1690
REMARK 465 PRO A 1691
REMARK 465 THR A 1692
REMARK 465 SER A 1693
REMARK 465 PRO A 1694
REMARK 465 ASN A 1695
REMARK 465 TYR A 1696
REMARK 465 SER A 1697
REMARK 465 PRO A 1698
REMARK 465 THR A 1699
REMARK 465 SER A 1700
REMARK 465 PRO A 1701
REMARK 465 SER A 1702
REMARK 465 TYR A 1703
REMARK 465 SER A 1704
REMARK 465 PRO A 1705
REMARK 465 THR A 1706
REMARK 465 SER A 1707
REMARK 465 PRO A 1708
REMARK 465 GLY A 1709
REMARK 465 TYR A 1710
REMARK 465 SER A 1711
REMARK 465 PRO A 1712
REMARK 465 GLY A 1713
REMARK 465 SER A 1714
REMARK 465 PRO A 1715
REMARK 465 ALA A 1716
REMARK 465 TYR A 1717
REMARK 465 SER A 1718
REMARK 465 PRO A 1719
REMARK 465 LYS A 1720
REMARK 465 GLN A 1721
REMARK 465 ASP A 1722
REMARK 465 GLU A 1723
REMARK 465 GLN A 1724
REMARK 465 LYS A 1725
REMARK 465 HIS A 1726
REMARK 465 ASN A 1727
REMARK 465 GLU A 1728
REMARK 465 ASN A 1729
REMARK 465 GLU A 1730
REMARK 465 ASN A 1731
REMARK 465 SER A 1732
REMARK 465 ARG A 1733
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
REMARK 465 ASN B 6
REMARK 465 SER B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 9
REMARK 465 TYR B 10
REMARK 465 TYR B 11
REMARK 465 ASP B 12
REMARK 465 GLU B 13
REMARK 465 ASP B 14
REMARK 465 PRO B 15
REMARK 465 TYR B 16
REMARK 465 GLY B 17
REMARK 465 PHE B 18
REMARK 465 GLU B 19
REMARK 465 LEU B 71
REMARK 465 GLU B 72
REMARK 465 GLN B 73
REMARK 465 LEU B 74
REMARK 465 ALA B 75
REMARK 465 GLN B 76
REMARK 465 HIS B 77
REMARK 465 THR B 78
REMARK 465 THR B 79
REMARK 465 GLU B 80
REMARK 465 SER B 81
REMARK 465 ASP B 82
REMARK 465 ASN B 83
REMARK 465 ILE B 84
REMARK 465 SER B 85
REMARK 465 ARG B 86
REMARK 465 LYS B 87
REMARK 465 TYR B 88
REMARK 465 GLU B 89
REMARK 465 ARG B 135
REMARK 465 THR B 136
REMARK 465 TYR B 137
REMARK 465 GLU B 138
REMARK 465 ALA B 139
REMARK 465 ILE B 140
REMARK 465 ASP B 141
REMARK 465 VAL B 142
REMARK 465 PRO B 143
REMARK 465 GLY B 144
REMARK 465 ARG B 145
REMARK 465 GLU B 146
REMARK 465 LEU B 147
REMARK 465 LYS B 148
REMARK 465 TYR B 149
REMARK 465 GLU B 150
REMARK 465 LEU B 151
REMARK 465 ILE B 152
REMARK 465 ALA B 153
REMARK 465 GLU B 154
REMARK 465 GLU B 155
REMARK 465 SER B 156
REMARK 465 GLU B 157
REMARK 465 ASP B 158
REMARK 465 ASP B 159
REMARK 465 SER B 160
REMARK 465 GLU B 161
REMARK 465 SER B 162
REMARK 465 GLY B 163
REMARK 465 GLU B 438
REMARK 465 ALA B 439
REMARK 465 HIS B 440
REMARK 465 ASP B 441
REMARK 465 PHE B 442
REMARK 465 ASN B 443
REMARK 465 MET B 444
REMARK 465 LYS B 445
REMARK 465 ARG B 504
REMARK 465 ASP B 505
REMARK 465 GLY B 506
REMARK 465 ILE B 669
REMARK 465 GLU B 670
REMARK 465 GLY B 671
REMARK 465 GLY B 672
REMARK 465 PHE B 673
REMARK 465 GLU B 674
REMARK 465 ASP B 675
REMARK 465 VAL B 676
REMARK 465 GLU B 677
REMARK 465 ASN B 716
REMARK 465 GLU B 717
REMARK 465 GLU B 718
REMARK 465 ASN B 719
REMARK 465 ASP B 720
REMARK 465 LEU B 721
REMARK 465 PRO B 920
REMARK 465 ASP B 921
REMARK 465 GLU B 922
REMARK 465 GLU B 923
REMARK 465 GLU B 924
REMARK 465 LEU B 925
REMARK 465 GLY B 926
REMARK 465 GLN B 927
REMARK 465 ARG B 928
REMARK 465 THR B 929
REMARK 465 ALA B 930
REMARK 465 TYR B 931
REMARK 465 HIS B 932
REMARK 465 HIS D 77
REMARK 465 LYS D 78
REMARK 465 LYS D 79
REMARK 465 LYS D 80
REMARK 465 HIS D 81
REMARK 465 LEU D 82
REMARK 465 LYS D 83
REMARK 465 HIS D 84
REMARK 465 GLU D 85
REMARK 465 ASN D 86
REMARK 465 ALA D 87
REMARK 465 ASN D 88
REMARK 465 ASP D 89
REMARK 465 GLU D 90
REMARK 465 THR D 91
REMARK 465 THR D 92
REMARK 465 ALA D 93
REMARK 465 VAL D 94
REMARK 465 GLU D 95
REMARK 465 ASP D 96
REMARK 465 GLU D 97
REMARK 465 ASP D 98
REMARK 465 ASP D 99
REMARK 465 ASP D 100
REMARK 465 LEU D 101
REMARK 465 ASP D 102
REMARK 465 GLU D 103
REMARK 465 ASP D 104
REMARK 465 ASP D 105
REMARK 465 VAL D 106
REMARK 465 ASN D 107
REMARK 465 ALA D 108
REMARK 465 ASP D 109
REMARK 465 ASP D 110
REMARK 465 ASP D 111
REMARK 465 ASP D 112
REMARK 465 PHE D 113
REMARK 465 MET D 114
REMARK 465 HIS D 115
REMARK 465 SER D 116
REMARK 465 GLU D 117
REMARK 465 ASN H 64
REMARK 465 LEU H 65
REMARK 465 GLU H 66
REMARK 465 ASP H 67
REMARK 465 THR H 68
REMARK 465 PRO H 69
REMARK 465 ALA H 70
REMARK 465 ASN H 71
REMARK 465 ASP H 72
REMARK 465 SER H 73
REMARK 465 SER H 74
REMARK 465 ALA H 75
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 B 345 CG CD CE NZ
REMARK 470 ARG D 11 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 17 CG CD CE NZ
REMARK 470 ALA K 115 CA C O CB
REMARK 470 PHE Q 21 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE Q 22 CG1 CG2 CD1
REMARK 470 LYS Q 23 CG CD CE NZ
REMARK 470 ARG Q 24 CG CD NE CZ NH1 NH2
REMARK 470 ASP Q 25 CG OD1 OD2
REMARK 470 ARG Q 26 CG CD NE CZ NH1 NH2
REMARK 470 ARG Q 28 CG CD NE CZ NH1 NH2
REMARK 470 ARG Q 29 CG CD NE CZ NH1 NH2
REMARK 470 ASN Q 30 CG OD1 ND2
REMARK 470 PHE Q 31 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU Q 32 CG CD1 CD2
REMARK 470 ARG Q 33 CG CD NE CZ NH1 NH2
REMARK 470 MET Q 34 CG SD CE
REMARK 470 ARG Q 35 CG CD NE CZ NH1 NH2
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 MET Q 27 CG MET Q 27 SD 0.204
REMARK 500 MET Q 27 SD MET Q 27 CE 0.722
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 ARG A 57 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 HIS A 399 N - CA - CB ANGL. DEV. = 11.6 DEGREES
REMARK 500 ASP A 483 CA - CB - CG ANGL. DEV. = 14.2 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 GLN A 4 -4.22 80.71
REMARK 500 ALA A 9 139.87 -34.19
REMARK 500 MET A 41 -124.87 -164.59
REMARK 500 ASP A 42 24.46 30.39
REMARK 500 GLN A 45 -53.61 94.83
REMARK 500 LYS A 49 129.31 -23.72
REMARK 500 ASN A 54 -97.35 62.49
REMARK 500 ASP A 55 143.47 59.79
REMARK 500 LEU A 65 -34.79 99.94
REMARK 500 THR A 69 -50.68 -125.58
REMARK 500 MET A 108 34.79 -74.64
REMARK 500 HIS A 109 -31.80 -148.43
REMARK 500 LEU A 113 97.17 -61.22
REMARK 500 LEU A 114 -40.34 -28.29
REMARK 500 ASP A 156 -71.33 -67.33
REMARK 500 CYS A 167 -179.67 -60.84
REMARK 500 GLU A 196 130.96 70.40
REMARK 500 PRO A 245 -9.75 -58.59
REMARK 500 ILE A 250 46.84 -79.25
REMARK 500 SER A 251 92.54 -48.53
REMARK 500 ASN A 253 171.58 63.43
REMARK 500 ARG A 257 -125.52 -122.31
REMARK 500 ASN A 282 -153.20 -73.37
REMARK 500 HIS A 286 -35.54 62.93
REMARK 500 ALA A 288 -22.00 -140.76
REMARK 500 ALA A 314 87.62 -68.09
REMARK 500 VAL A 322 114.51 79.28
REMARK 500 LYS A 330 109.67 -58.47
REMARK 500 LYS A 332 -40.57 85.59
REMARK 500 ARG A 335 -58.17 -9.49
REMARK 500 HIS A 399 -72.68 -56.41
REMARK 500 SER A 409 12.54 -64.63
REMARK 500 SER A 418 127.89 -37.39
REMARK 500 TYR A 465 133.34 72.76
REMARK 500 SER A 466 13.93 -61.02
REMARK 500 ASN A 479 12.53 86.47
REMARK 500 ASP A 483 30.29 -65.61
REMARK 500 LEU A 504 -37.25 -135.05
REMARK 500 ASN A 517 19.52 48.40
REMARK 500 GLN A 525 -115.96 44.32
REMARK 500 ASP A 555 34.94 -96.00
REMARK 500 SER A 579 -9.46 -59.30
REMARK 500 GLU A 593 -105.63 45.19
REMARK 500 LEU A 598 63.36 -112.90
REMARK 500 SER A 599 121.54 -34.90
REMARK 500 THR A 621 -65.81 -105.60
REMARK 500 ASN A 700 -1.66 61.09
REMARK 500 LEU A 702 106.95 -49.54
REMARK 500 LYS A 752 145.30 -174.41
REMARK 500 ALA A 763 -76.03 -98.50
REMARK 500
REMARK 500 THIS ENTRY HAS 244 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 67 SG
REMARK 620 2 CYS A 70 SG 87.5
REMARK 620 3 CYS A 77 SG 112.2 99.1
REMARK 620 4 HIS A 80 NE2 130.0 106.3 112.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 107 SG
REMARK 620 2 CYS A 110 SG 116.7
REMARK 620 3 CYS A 148 SG 100.3 116.9
REMARK 620 4 CYS A 167 SG 103.7 99.4 120.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 483 OD1
REMARK 620 2 ASP A 483 OD2 50.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1163 SG
REMARK 620 2 CYS B1166 SG 108.2
REMARK 620 3 CYS B1182 SG 97.4 107.7
REMARK 620 4 CYS B1185 SG 110.8 123.6 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 86 SG
REMARK 620 2 CYS C 88 SG 108.5
REMARK 620 3 CYS C 92 SG 102.6 115.6
REMARK 620 4 CYS C 95 SG 113.3 105.9 111.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 7 SG
REMARK 620 2 CYS I 10 SG 125.7
REMARK 620 3 CYS I 29 SG 100.7 108.9
REMARK 620 4 CYS I 32 SG 104.3 112.2 102.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 75 SG
REMARK 620 2 CYS I 78 SG 125.1
REMARK 620 3 CYS I 103 SG 104.2 90.6
REMARK 620 4 CYS I 106 SG 96.7 124.0 115.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 7 SG
REMARK 620 2 CYS J 10 SG 130.6
REMARK 620 3 CYS J 45 SG 109.8 102.2
REMARK 620 4 CYS J 46 SG 115.1 98.7 93.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 31 SG
REMARK 620 2 CYS L 34 SG 95.1
REMARK 620 3 CYS L 48 SG 99.4 106.7
REMARK 620 4 CYS L 51 SG 113.1 127.8 110.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 101
DBREF 5IP9 A 2 1733 UNP P04050 RPB1_YEAST 2 1733
DBREF 5IP9 B 2 1224 UNP P08518 RPB2_YEAST 2 1224
DBREF 5IP9 C 3 268 UNP P16370 RPB3_YEAST 3 268
DBREF 5IP9 D 1 221 UNP P20433 RPB4_YEAST 1 221
DBREF 5IP9 E 2 215 UNP P20434 RPAB1_YEAST 2 215
DBREF 5IP9 F 69 155 UNP P20435 RPAB2_YEAST 69 155
DBREF 5IP9 G 1 171 UNP P34087 RPB7_YEAST 1 171
DBREF 5IP9 H 2 146 UNP P20436 RPAB3_YEAST 2 146
DBREF 5IP9 I 2 120 UNP P27999 RPB9_YEAST 2 120
DBREF 5IP9 J 1 65 UNP P22139 RPAB5_YEAST 1 65
DBREF 5IP9 K 1 115 UNP P38902 RPB11_YEAST 1 115
DBREF 5IP9 L 25 70 UNP P40422 RPAB4_YEAST 25 70
DBREF 5IP9 Q 21 35 PDB 5IP9 5IP9 21 35
SEQRES 1 A 1732 VAL GLY GLN GLN TYR SER SER ALA PRO LEU ARG THR VAL
SEQRES 2 A 1732 LYS GLU VAL GLN PHE GLY LEU PHE SER PRO GLU GLU VAL
SEQRES 3 A 1732 ARG ALA ILE SER VAL ALA LYS ILE ARG PHE PRO GLU THR
SEQRES 4 A 1732 MET ASP GLU THR GLN THR ARG ALA LYS ILE GLY GLY LEU
SEQRES 5 A 1732 ASN ASP PRO ARG LEU GLY SER ILE ASP ARG ASN LEU LYS
SEQRES 6 A 1732 CYS GLN THR CYS GLN GLU GLY MET ASN GLU CYS PRO GLY
SEQRES 7 A 1732 HIS PHE GLY HIS ILE ASP LEU ALA LYS PRO VAL PHE HIS
SEQRES 8 A 1732 VAL GLY PHE ILE ALA LYS ILE LYS LYS VAL CYS GLU CYS
SEQRES 9 A 1732 VAL CYS MET HIS CYS GLY LYS LEU LEU LEU ASP GLU HIS
SEQRES 10 A 1732 ASN GLU LEU MET ARG GLN ALA LEU ALA ILE LYS ASP SER
SEQRES 11 A 1732 LYS LYS ARG PHE ALA ALA ILE TRP THR LEU CYS LYS THR
SEQRES 12 A 1732 LYS MET VAL CYS GLU THR ASP VAL PRO SER GLU ASP ASP
SEQRES 13 A 1732 PRO THR GLN LEU VAL SER ARG GLY GLY CYS GLY ASN THR
SEQRES 14 A 1732 GLN PRO THR ILE ARG LYS ASP GLY LEU LYS LEU VAL GLY
SEQRES 15 A 1732 SER TRP LYS LYS ASP ARG ALA THR GLY ASP ALA ASP GLU
SEQRES 16 A 1732 PRO GLU LEU ARG VAL LEU SER THR GLU GLU ILE LEU ASN
SEQRES 17 A 1732 ILE PHE LYS HIS ILE SER VAL LYS ASP PHE THR SER LEU
SEQRES 18 A 1732 GLY PHE ASN GLU VAL PHE SER ARG PRO GLU TRP MET ILE
SEQRES 19 A 1732 LEU THR CYS LEU PRO VAL PRO PRO PRO PRO VAL ARG PRO
SEQRES 20 A 1732 SER ILE SER PHE ASN GLU SER GLN ARG GLY GLU ASP ASP
SEQRES 21 A 1732 LEU THR PHE LYS LEU ALA ASP ILE LEU LYS ALA ASN ILE
SEQRES 22 A 1732 SER LEU GLU THR LEU GLU HIS ASN GLY ALA PRO HIS HIS
SEQRES 23 A 1732 ALA ILE GLU GLU ALA GLU SER LEU LEU GLN PHE HIS VAL
SEQRES 24 A 1732 ALA THR TYR MET ASP ASN ASP ILE ALA GLY GLN PRO GLN
SEQRES 25 A 1732 ALA LEU GLN LYS SER GLY ARG PRO VAL LYS SER ILE ARG
SEQRES 26 A 1732 ALA ARG LEU LYS GLY LYS GLU GLY ARG ILE ARG GLY ASN
SEQRES 27 A 1732 LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG THR VAL
SEQRES 28 A 1732 ILE SER GLY ASP PRO ASN LEU GLU LEU ASP GLN VAL GLY
SEQRES 29 A 1732 VAL PRO LYS SER ILE ALA LYS THR LEU THR TYR PRO GLU
SEQRES 30 A 1732 VAL VAL THR PRO TYR ASN ILE ASP ARG LEU THR GLN LEU
SEQRES 31 A 1732 VAL ARG ASN GLY PRO ASN GLU HIS PRO GLY ALA LYS TYR
SEQRES 32 A 1732 VAL ILE ARG ASP SER GLY ASP ARG ILE ASP LEU ARG TYR
SEQRES 33 A 1732 SER LYS ARG ALA GLY ASP ILE GLN LEU GLN TYR GLY TRP
SEQRES 34 A 1732 LYS VAL GLU ARG HIS ILE MET ASP ASN ASP PRO VAL LEU
SEQRES 35 A 1732 PHE ASN ARG GLN PRO SER LEU HIS LYS MET SER MET MET
SEQRES 36 A 1732 ALA HIS ARG VAL LYS VAL ILE PRO TYR SER THR PHE ARG
SEQRES 37 A 1732 LEU ASN LEU SER VAL THR SER PRO TYR ASN ALA ASP PHE
SEQRES 38 A 1732 ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN SER GLU
SEQRES 39 A 1732 GLU THR ARG ALA GLU LEU SER GLN LEU CYS ALA VAL PRO
SEQRES 40 A 1732 LEU GLN ILE VAL SER PRO GLN SER ASN LYS PRO CYS MET
SEQRES 41 A 1732 GLY ILE VAL GLN ASP THR LEU CYS GLY ILE ARG LYS LEU
SEQRES 42 A 1732 THR LEU ARG ASP THR PHE ILE GLU LEU ASP GLN VAL LEU
SEQRES 43 A 1732 ASN MET LEU TYR TRP VAL PRO ASP TRP ASP GLY VAL ILE
SEQRES 44 A 1732 PRO THR PRO ALA ILE ILE LYS PRO LYS PRO LEU TRP SER
SEQRES 45 A 1732 GLY LYS GLN ILE LEU SER VAL ALA ILE PRO ASN GLY ILE
SEQRES 46 A 1732 HIS LEU GLN ARG PHE ASP GLU GLY THR THR LEU LEU SER
SEQRES 47 A 1732 PRO LYS ASP ASN GLY MET LEU ILE ILE ASP GLY GLN ILE
SEQRES 48 A 1732 ILE PHE GLY VAL VAL GLU LYS LYS THR VAL GLY SER SER
SEQRES 49 A 1732 ASN GLY GLY LEU ILE HIS VAL VAL THR ARG GLU LYS GLY
SEQRES 50 A 1732 PRO GLN VAL CYS ALA LYS LEU PHE GLY ASN ILE GLN LYS
SEQRES 51 A 1732 VAL VAL ASN PHE TRP LEU LEU HIS ASN GLY PHE SER THR
SEQRES 52 A 1732 GLY ILE GLY ASP THR ILE ALA ASP GLY PRO THR MET ARG
SEQRES 53 A 1732 GLU ILE THR GLU THR ILE ALA GLU ALA LYS LYS LYS VAL
SEQRES 54 A 1732 LEU ASP VAL THR LYS GLU ALA GLN ALA ASN LEU LEU THR
SEQRES 55 A 1732 ALA LYS HIS GLY MET THR LEU ARG GLU SER PHE GLU ASP
SEQRES 56 A 1732 ASN VAL VAL ARG PHE LEU ASN GLU ALA ARG ASP LYS ALA
SEQRES 57 A 1732 GLY ARG LEU ALA GLU VAL ASN LEU LYS ASP LEU ASN ASN
SEQRES 58 A 1732 VAL LYS GLN MET VAL MET ALA GLY SER LYS GLY SER PHE
SEQRES 59 A 1732 ILE ASN ILE ALA GLN MET SER ALA CYS VAL GLY GLN GLN
SEQRES 60 A 1732 SER VAL GLU GLY LYS ARG ILE ALA PHE GLY PHE VAL ASP
SEQRES 61 A 1732 ARG THR LEU PRO HIS PHE SER LYS ASP ASP TYR SER PRO
SEQRES 62 A 1732 GLU SER LYS GLY PHE VAL GLU ASN SER TYR LEU ARG GLY
SEQRES 63 A 1732 LEU THR PRO GLN GLU PHE PHE PHE HIS ALA MET GLY GLY
SEQRES 64 A 1732 ARG GLU GLY LEU ILE ASP THR ALA VAL LYS THR ALA GLU
SEQRES 65 A 1732 THR GLY TYR ILE GLN ARG ARG LEU VAL LYS ALA LEU GLU
SEQRES 66 A 1732 ASP ILE MET VAL HIS TYR ASP ASN THR THR ARG ASN SER
SEQRES 67 A 1732 LEU GLY ASN VAL ILE GLN PHE ILE TYR GLY GLU ASP GLY
SEQRES 68 A 1732 MET ASP ALA ALA HIS ILE GLU LYS GLN SER LEU ASP THR
SEQRES 69 A 1732 ILE GLY GLY SER ASP ALA ALA PHE GLU LYS ARG TYR ARG
SEQRES 70 A 1732 VAL ASP LEU LEU ASN THR ASP HIS THR LEU ASP PRO SER
SEQRES 71 A 1732 LEU LEU GLU SER GLY SER GLU ILE LEU GLY ASP LEU LYS
SEQRES 72 A 1732 LEU GLN VAL LEU LEU ASP GLU GLU TYR LYS GLN LEU VAL
SEQRES 73 A 1732 LYS ASP ARG LYS PHE LEU ARG GLU VAL PHE VAL ASP GLY
SEQRES 74 A 1732 GLU ALA ASN TRP PRO LEU PRO VAL ASN ILE ARG ARG ILE
SEQRES 75 A 1732 ILE GLN ASN ALA GLN GLN THR PHE HIS ILE ASP HIS THR
SEQRES 76 A 1732 LYS PRO SER ASP LEU THR ILE LYS ASP ILE VAL LEU GLY
SEQRES 77 A 1732 VAL LYS ASP LEU GLN GLU ASN LEU LEU VAL LEU ARG GLY
SEQRES 78 A 1732 LYS ASN GLU ILE ILE GLN ASN ALA GLN ARG ASP ALA VAL
SEQRES 79 A 1732 THR LEU PHE CYS CYS LEU LEU ARG SER ARG LEU ALA THR
SEQRES 80 A 1732 ARG ARG VAL LEU GLN GLU TYR ARG LEU THR LYS GLN ALA
SEQRES 81 A 1732 PHE ASP TRP VAL LEU SER ASN ILE GLU ALA GLN PHE LEU
SEQRES 82 A 1732 ARG SER VAL VAL HIS PRO GLY GLU MET VAL GLY VAL LEU
SEQRES 83 A 1732 ALA ALA GLN SER ILE GLY GLU PRO ALA THR GLN MET THR
SEQRES 84 A 1732 LEU ASN THR PHE HIS PHE ALA GLY VAL ALA SER LYS LYS
SEQRES 85 A 1732 VAL THR SER GLY VAL PRO ARG LEU LYS GLU ILE LEU ASN
SEQRES 86 A 1732 VAL ALA LYS ASN MET LYS THR PRO SER LEU THR VAL TYR
SEQRES 87 A 1732 LEU GLU PRO GLY HIS ALA ALA ASP GLN GLU GLN ALA LYS
SEQRES 88 A 1732 LEU ILE ARG SER ALA ILE GLU HIS THR THR LEU LYS SER
SEQRES 89 A 1732 VAL THR ILE ALA SER GLU ILE TYR TYR ASP PRO ASP PRO
SEQRES 90 A 1732 ARG SER THR VAL ILE PRO GLU ASP GLU GLU ILE ILE GLN
SEQRES 91 A 1732 LEU HIS PHE SER LEU LEU ASP GLU GLU ALA GLU GLN SER
SEQRES 92 A 1732 PHE ASP GLN GLN SER PRO TRP LEU LEU ARG LEU GLU LEU
SEQRES 93 A 1732 ASP ARG ALA ALA MET ASN ASP LYS ASP LEU THR MET GLY
SEQRES 94 A 1732 GLN VAL GLY GLU ARG ILE LYS GLN THR PHE LYS ASN ASP
SEQRES 95 A 1732 LEU PHE VAL ILE TRP SER GLU ASP ASN ASP GLU LYS LEU
SEQRES 96 A 1732 ILE ILE ARG CYS ARG VAL VAL ARG PRO LYS SER LEU ASP
SEQRES 97 A 1732 ALA GLU THR GLU ALA GLU GLU ASP HIS MET LEU LYS LYS
SEQRES 98 A 1732 ILE GLU ASN THR MET LEU GLU ASN ILE THR LEU ARG GLY
SEQRES 99 A 1732 VAL GLU ASN ILE GLU ARG VAL VAL MET MET LYS TYR ASP
SEQRES 100 A 1732 ARG LYS VAL PRO SER PRO THR GLY GLU TYR VAL LYS GLU
SEQRES 101 A 1732 PRO GLU TRP VAL LEU GLU THR ASP GLY VAL ASN LEU SER
SEQRES 102 A 1732 GLU VAL MET THR VAL PRO GLY ILE ASP PRO THR ARG ILE
SEQRES 103 A 1732 TYR THR ASN SER PHE ILE ASP ILE MET GLU VAL LEU GLY
SEQRES 104 A 1732 ILE GLU ALA GLY ARG ALA ALA LEU TYR LYS GLU VAL TYR
SEQRES 105 A 1732 ASN VAL ILE ALA SER ASP GLY SER TYR VAL ASN TYR ARG
SEQRES 106 A 1732 HIS MET ALA LEU LEU VAL ASP VAL MET THR THR GLN GLY
SEQRES 107 A 1732 GLY LEU THR SER VAL THR ARG HIS GLY PHE ASN ARG SER
SEQRES 108 A 1732 ASN THR GLY ALA LEU MET ARG CYS SER PHE GLU GLU THR
SEQRES 109 A 1732 VAL GLU ILE LEU PHE GLU ALA GLY ALA SER ALA GLU LEU
SEQRES 110 A 1732 ASP ASP CYS ARG GLY VAL SER GLU ASN VAL ILE LEU GLY
SEQRES 111 A 1732 GLN MET ALA PRO ILE GLY THR GLY ALA PHE ASP VAL MET
SEQRES 112 A 1732 ILE ASP GLU GLU SER LEU VAL LYS TYR MET PRO GLU GLN
SEQRES 113 A 1732 LYS ILE THR GLU ILE GLU ASP GLY GLN ASP GLY GLY VAL
SEQRES 114 A 1732 THR PRO TYR SER ASN GLU SER GLY LEU VAL ASN ALA ASP
SEQRES 115 A 1732 LEU ASP VAL LYS ASP GLU LEU MET PHE SER PRO LEU VAL
SEQRES 116 A 1732 ASP SER GLY SER ASN ASP ALA MET ALA GLY GLY PHE THR
SEQRES 117 A 1732 ALA TYR GLY GLY ALA ASP TYR GLY GLU ALA THR SER PRO
SEQRES 118 A 1732 PHE GLY ALA TYR GLY GLU ALA PRO THR SER PRO GLY PHE
SEQRES 119 A 1732 GLY VAL SER SER PRO GLY PHE SER PRO THR SER PRO THR
SEQRES 120 A 1732 TYR SER PRO THR SER PRO ALA TYR SER PRO THR SER PRO
SEQRES 121 A 1732 SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER
SEQRES 122 A 1732 PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR
SEQRES 123 A 1732 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 124 A 1732 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 125 A 1732 PRO THR SER PRO SER TYR SER PRO THR SER PRO SER TYR
SEQRES 126 A 1732 SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER
SEQRES 127 A 1732 TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO
SEQRES 128 A 1732 SER TYR SER PRO THR SER PRO ALA TYR SER PRO THR SER
SEQRES 129 A 1732 PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR
SEQRES 130 A 1732 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 131 A 1732 THR SER PRO ASN TYR SER PRO THR SER PRO SER TYR SER
SEQRES 132 A 1732 PRO THR SER PRO GLY TYR SER PRO GLY SER PRO ALA TYR
SEQRES 133 A 1732 SER PRO LYS GLN ASP GLU GLN LYS HIS ASN GLU ASN GLU
SEQRES 134 A 1732 ASN SER ARG
SEQRES 1 B 1223 SER ASP LEU ALA ASN SER GLU LYS TYR TYR ASP GLU ASP
SEQRES 2 B 1223 PRO TYR GLY PHE GLU ASP GLU SER ALA PRO ILE THR ALA
SEQRES 3 B 1223 GLU ASP SER TRP ALA VAL ILE SER ALA PHE PHE ARG GLU
SEQRES 4 B 1223 LYS GLY LEU VAL SER GLN GLN LEU ASP SER PHE ASN GLN
SEQRES 5 B 1223 PHE VAL ASP TYR THR LEU GLN ASP ILE ILE CYS GLU ASP
SEQRES 6 B 1223 SER THR LEU ILE LEU GLU GLN LEU ALA GLN HIS THR THR
SEQRES 7 B 1223 GLU SER ASP ASN ILE SER ARG LYS TYR GLU ILE SER PHE
SEQRES 8 B 1223 GLY LYS ILE TYR VAL THR LYS PRO MET VAL ASN GLU SER
SEQRES 9 B 1223 ASP GLY VAL THR HIS ALA LEU TYR PRO GLN GLU ALA ARG
SEQRES 10 B 1223 LEU ARG ASN LEU THR TYR SER SER GLY LEU PHE VAL ASP
SEQRES 11 B 1223 VAL LYS LYS ARG THR TYR GLU ALA ILE ASP VAL PRO GLY
SEQRES 12 B 1223 ARG GLU LEU LYS TYR GLU LEU ILE ALA GLU GLU SER GLU
SEQRES 13 B 1223 ASP ASP SER GLU SER GLY LYS VAL PHE ILE GLY ARG LEU
SEQRES 14 B 1223 PRO ILE MET LEU ARG SER LYS ASN CYS TYR LEU SER GLU
SEQRES 15 B 1223 ALA THR GLU SER ASP LEU TYR LYS LEU LYS GLU CYS PRO
SEQRES 16 B 1223 PHE ASP MET GLY GLY TYR PHE ILE ILE ASN GLY SER GLU
SEQRES 17 B 1223 LYS VAL LEU ILE ALA GLN GLU ARG SER ALA GLY ASN ILE
SEQRES 18 B 1223 VAL GLN VAL PHE LYS LYS ALA ALA PRO SER PRO ILE SER
SEQRES 19 B 1223 HIS VAL ALA GLU ILE ARG SER ALA LEU GLU LYS GLY SER
SEQRES 20 B 1223 ARG PHE ILE SER THR LEU GLN VAL LYS LEU TYR GLY ARG
SEQRES 21 B 1223 GLU GLY SER SER ALA ARG THR ILE LYS ALA THR LEU PRO
SEQRES 22 B 1223 TYR ILE LYS GLN ASP ILE PRO ILE VAL ILE ILE PHE ARG
SEQRES 23 B 1223 ALA LEU GLY ILE ILE PRO ASP GLY GLU ILE LEU GLU HIS
SEQRES 24 B 1223 ILE CYS TYR ASP VAL ASN ASP TRP GLN MET LEU GLU MET
SEQRES 25 B 1223 LEU LYS PRO CYS VAL GLU ASP GLY PHE VAL ILE GLN ASP
SEQRES 26 B 1223 ARG GLU THR ALA LEU ASP PHE ILE GLY ARG ARG GLY THR
SEQRES 27 B 1223 ALA LEU GLY ILE LYS LYS GLU LYS ARG ILE GLN TYR ALA
SEQRES 28 B 1223 LYS ASP ILE LEU GLN LYS GLU PHE LEU PRO HIS ILE THR
SEQRES 29 B 1223 GLN LEU GLU GLY PHE GLU SER ARG LYS ALA PHE PHE LEU
SEQRES 30 B 1223 GLY TYR MET ILE ASN ARG LEU LEU LEU CYS ALA LEU ASP
SEQRES 31 B 1223 ARG LYS ASP GLN ASP ASP ARG ASP HIS PHE GLY LYS LYS
SEQRES 32 B 1223 ARG LEU ASP LEU ALA GLY PRO LEU LEU ALA GLN LEU PHE
SEQRES 33 B 1223 LYS THR LEU PHE LYS LYS LEU THR LYS ASP ILE PHE ARG
SEQRES 34 B 1223 TYR MET GLN ARG THR VAL GLU GLU ALA HIS ASP PHE ASN
SEQRES 35 B 1223 MET LYS LEU ALA ILE ASN ALA LYS THR ILE THR SER GLY
SEQRES 36 B 1223 LEU LYS TYR ALA LEU ALA THR GLY ASN TRP GLY GLU GLN
SEQRES 37 B 1223 LYS LYS ALA MET SER SER ARG ALA GLY VAL SER GLN VAL
SEQRES 38 B 1223 LEU ASN ARG TYR THR TYR SER SER THR LEU SER HIS LEU
SEQRES 39 B 1223 ARG ARG THR ASN THR PRO ILE GLY ARG ASP GLY LYS LEU
SEQRES 40 B 1223 ALA LYS PRO ARG GLN LEU HIS ASN THR HIS TRP GLY LEU
SEQRES 41 B 1223 VAL CYS PRO ALA GLU THR PRO GLU GLY GLN ALA CYS GLY
SEQRES 42 B 1223 LEU VAL LYS ASN LEU SER LEU MET SER CYS ILE SER VAL
SEQRES 43 B 1223 GLY THR ASP PRO MET PRO ILE ILE THR PHE LEU SER GLU
SEQRES 44 B 1223 TRP GLY MET GLU PRO LEU GLU ASP TYR VAL PRO HIS GLN
SEQRES 45 B 1223 SER PRO ASP ALA THR ARG VAL PHE VAL ASN GLY VAL TRP
SEQRES 46 B 1223 HIS GLY VAL HIS ARG ASN PRO ALA ARG LEU MET GLU THR
SEQRES 47 B 1223 LEU ARG THR LEU ARG ARG LYS GLY ASP ILE ASN PRO GLU
SEQRES 48 B 1223 VAL SER MET ILE ARG ASP ILE ARG GLU LYS GLU LEU LYS
SEQRES 49 B 1223 ILE PHE THR ASP ALA GLY ARG VAL TYR ARG PRO LEU PHE
SEQRES 50 B 1223 ILE VAL GLU ASP ASP GLU SER LEU GLY HIS LYS GLU LEU
SEQRES 51 B 1223 LYS VAL ARG LYS GLY HIS ILE ALA LYS LEU MET ALA THR
SEQRES 52 B 1223 GLU TYR GLN ASP ILE GLU GLY GLY PHE GLU ASP VAL GLU
SEQRES 53 B 1223 GLU TYR THR TRP SER SER LEU LEU ASN GLU GLY LEU VAL
SEQRES 54 B 1223 GLU TYR ILE ASP ALA GLU GLU GLU GLU SER ILE LEU ILE
SEQRES 55 B 1223 ALA MET GLN PRO GLU ASP LEU GLU PRO ALA GLU ALA ASN
SEQRES 56 B 1223 GLU GLU ASN ASP LEU ASP VAL ASP PRO ALA LYS ARG ILE
SEQRES 57 B 1223 ARG VAL SER HIS HIS ALA THR THR PHE THR HIS CYS GLU
SEQRES 58 B 1223 ILE HIS PRO SER MET ILE LEU GLY VAL ALA ALA SER ILE
SEQRES 59 B 1223 ILE PRO PHE PRO ASP HIS ASN GLN SER PRO ARG ASN THR
SEQRES 60 B 1223 TYR GLN SER ALA MET GLY LYS GLN ALA MET GLY VAL PHE
SEQRES 61 B 1223 LEU THR ASN TYR ASN VAL ARG MET ASP THR MET ALA ASN
SEQRES 62 B 1223 ILE LEU TYR TYR PRO GLN LYS PRO LEU GLY THR THR ARG
SEQRES 63 B 1223 ALA MET GLU TYR LEU LYS PHE ARG GLU LEU PRO ALA GLY
SEQRES 64 B 1223 GLN ASN ALA ILE VAL ALA ILE ALA CYS TYR SER GLY TYR
SEQRES 65 B 1223 ASN GLN GLU ASP SER MET ILE MET ASN GLN SER SER ILE
SEQRES 66 B 1223 ASP ARG GLY LEU PHE ARG SER LEU PHE PHE ARG SER TYR
SEQRES 67 B 1223 MET ASP GLN GLU LYS LYS TYR GLY MET SER ILE THR GLU
SEQRES 68 B 1223 THR PHE GLU LYS PRO GLN ARG THR ASN THR LEU ARG MET
SEQRES 69 B 1223 LYS HIS GLY THR TYR ASP LYS LEU ASP ASP ASP GLY LEU
SEQRES 70 B 1223 ILE ALA PRO GLY VAL ARG VAL SER GLY GLU ASP VAL ILE
SEQRES 71 B 1223 ILE GLY LYS THR THR PRO ILE SER PRO ASP GLU GLU GLU
SEQRES 72 B 1223 LEU GLY GLN ARG THR ALA TYR HIS SER LYS ARG ASP ALA
SEQRES 73 B 1223 SER THR PRO LEU ARG SER THR GLU ASN GLY ILE VAL ASP
SEQRES 74 B 1223 GLN VAL LEU VAL THR THR ASN GLN ASP GLY LEU LYS PHE
SEQRES 75 B 1223 VAL LYS VAL ARG VAL ARG THR THR LYS ILE PRO GLN ILE
SEQRES 76 B 1223 GLY ASP LYS PHE ALA SER ARG HIS GLY GLN LYS GLY THR
SEQRES 77 B 1223 ILE GLY ILE THR TYR ARG ARG GLU ASP MET PRO PHE THR
SEQRES 78 B 1223 ALA GLU GLY ILE VAL PRO ASP LEU ILE ILE ASN PRO HIS
SEQRES 79 B 1223 ALA ILE PRO SER ARG MET THR VAL ALA HIS LEU ILE GLU
SEQRES 80 B 1223 CYS LEU LEU SER LYS VAL ALA ALA LEU SER GLY ASN GLU
SEQRES 81 B 1223 GLY ASP ALA SER PRO PHE THR ASP ILE THR VAL GLU GLY
SEQRES 82 B 1223 ILE SER LYS LEU LEU ARG GLU HIS GLY TYR GLN SER ARG
SEQRES 83 B 1223 GLY PHE GLU VAL MET TYR ASN GLY HIS THR GLY LYS LYS
SEQRES 84 B 1223 LEU MET ALA GLN ILE PHE PHE GLY PRO THR TYR TYR GLN
SEQRES 85 B 1223 ARG LEU ARG HIS MET VAL ASP ASP LYS ILE HIS ALA ARG
SEQRES 86 B 1223 ALA ARG GLY PRO MET GLN VAL LEU THR ARG GLN PRO VAL
SEQRES 87 B 1223 GLU GLY ARG SER ARG ASP GLY GLY LEU ARG PHE GLY GLU
SEQRES 88 B 1223 MET GLU ARG ASP CYS MET ILE ALA HIS GLY ALA ALA SER
SEQRES 89 B 1223 PHE LEU LYS GLU ARG LEU MET GLU ALA SER ASP ALA PHE
SEQRES 90 B 1223 ARG VAL HIS ILE CYS GLY ILE CYS GLY LEU MET THR VAL
SEQRES 91 B 1223 ILE ALA LYS LEU ASN HIS ASN GLN PHE GLU CYS LYS GLY
SEQRES 92 B 1223 CYS ASP ASN LYS ILE ASP ILE TYR GLN ILE HIS ILE PRO
SEQRES 93 B 1223 TYR ALA ALA LYS LEU LEU PHE GLN GLU LEU MET ALA MET
SEQRES 94 B 1223 ASN ILE THR PRO ARG LEU TYR THR ASP ARG SER ARG ASP
SEQRES 95 B 1223 PHE
SEQRES 1 C 266 GLU GLU GLY PRO GLN VAL LYS ILE ARG GLU ALA SER LYS
SEQRES 2 C 266 ASP ASN VAL ASP PHE ILE LEU SER ASN VAL ASP LEU ALA
SEQRES 3 C 266 MET ALA ASN SER LEU ARG ARG VAL MET ILE ALA GLU ILE
SEQRES 4 C 266 PRO THR LEU ALA ILE ASP SER VAL GLU VAL GLU THR ASN
SEQRES 5 C 266 THR THR VAL LEU ALA ASP GLU PHE ILE ALA HIS ARG LEU
SEQRES 6 C 266 GLY LEU ILE PRO LEU GLN SER MET ASP ILE GLU GLN LEU
SEQRES 7 C 266 GLU TYR SER ARG ASP CYS PHE CYS GLU ASP HIS CYS ASP
SEQRES 8 C 266 LYS CYS SER VAL VAL LEU THR LEU GLN ALA PHE GLY GLU
SEQRES 9 C 266 SER GLU SER THR THR ASN VAL TYR SER LYS ASP LEU VAL
SEQRES 10 C 266 ILE VAL SER ASN LEU MET GLY ARG ASN ILE GLY HIS PRO
SEQRES 11 C 266 ILE ILE GLN ASP LYS GLU GLY ASN GLY VAL LEU ILE CYS
SEQRES 12 C 266 LYS LEU ARG LYS GLY GLN GLU LEU LYS LEU THR CYS VAL
SEQRES 13 C 266 ALA LYS LYS GLY ILE ALA LYS GLU HIS ALA LYS TRP GLY
SEQRES 14 C 266 PRO ALA ALA ALA ILE GLU PHE GLU TYR ASP PRO TRP ASN
SEQRES 15 C 266 LYS LEU LYS HIS THR ASP TYR TRP TYR GLU GLN ASP SER
SEQRES 16 C 266 ALA LYS GLU TRP PRO GLN SER LYS ASN CYS GLU TYR GLU
SEQRES 17 C 266 ASP PRO PRO ASN GLU GLY ASP PRO PHE ASP TYR LYS ALA
SEQRES 18 C 266 GLN ALA ASP THR PHE TYR MET ASN VAL GLU SER VAL GLY
SEQRES 19 C 266 SER ILE PRO VAL ASP GLN VAL VAL VAL ARG GLY ILE ASP
SEQRES 20 C 266 THR LEU GLN LYS LYS VAL ALA SER ILE LEU LEU ALA LEU
SEQRES 21 C 266 THR GLN MET ASP GLN ASP
SEQRES 1 D 221 MET ASN VAL SER THR SER THR PHE GLN THR ARG ARG ARG
SEQRES 2 D 221 ARG LEU LYS LYS VAL GLU GLU GLU GLU ASN ALA ALA THR
SEQRES 3 D 221 LEU GLN LEU GLY GLN GLU PHE GLN LEU LYS GLN ILE ASN
SEQRES 4 D 221 HIS GLN GLY GLU GLU GLU GLU LEU ILE ALA LEU ASN LEU
SEQRES 5 D 221 SER GLU ALA ARG LEU VAL ILE LYS GLU ALA LEU VAL GLU
SEQRES 6 D 221 ARG ARG ARG ALA PHE LYS ARG SER GLN LYS LYS HIS LYS
SEQRES 7 D 221 LYS LYS HIS LEU LYS HIS GLU ASN ALA ASN ASP GLU THR
SEQRES 8 D 221 THR ALA VAL GLU ASP GLU ASP ASP ASP LEU ASP GLU ASP
SEQRES 9 D 221 ASP VAL ASN ALA ASP ASP ASP ASP PHE MET HIS SER GLU
SEQRES 10 D 221 THR ARG GLU LYS GLU LEU GLU SER ILE ASP VAL LEU LEU
SEQRES 11 D 221 GLU GLN THR THR GLY GLY ASN ASN LYS ASP LEU LYS ASN
SEQRES 12 D 221 THR MET GLN TYR LEU THR ASN PHE SER ARG PHE ARG ASP
SEQRES 13 D 221 GLN GLU THR VAL GLY ALA VAL ILE GLN LEU LEU LYS SER
SEQRES 14 D 221 THR GLY LEU HIS PRO PHE GLU VAL ALA GLN LEU GLY SER
SEQRES 15 D 221 LEU ALA CYS ASP THR ALA ASP GLU ALA LYS THR LEU ILE
SEQRES 16 D 221 PRO SER LEU ASN ASN LYS ILE SER ASP ASP GLU LEU GLU
SEQRES 17 D 221 ARG ILE LEU LYS GLU LEU SER ASN LEU GLU THR LEU TYR
SEQRES 1 E 214 ASP GLN GLU ASN GLU ARG ASN ILE SER ARG LEU TRP ARG
SEQRES 2 E 214 ALA PHE ARG THR VAL LYS GLU MET VAL LYS ASP ARG GLY
SEQRES 3 E 214 TYR PHE ILE THR GLN GLU GLU VAL GLU LEU PRO LEU GLU
SEQRES 4 E 214 ASP PHE LYS ALA LYS TYR CYS ASP SER MET GLY ARG PRO
SEQRES 5 E 214 GLN ARG LYS MET MET SER PHE GLN ALA ASN PRO THR GLU
SEQRES 6 E 214 GLU SER ILE SER LYS PHE PRO ASP MET GLY SER LEU TRP
SEQRES 7 E 214 VAL GLU PHE CYS ASP GLU PRO SER VAL GLY VAL LYS THR
SEQRES 8 E 214 MET LYS THR PHE VAL ILE HIS ILE GLN GLU LYS ASN PHE
SEQRES 9 E 214 GLN THR GLY ILE PHE VAL TYR GLN ASN ASN ILE THR PRO
SEQRES 10 E 214 SER ALA MET LYS LEU VAL PRO SER ILE PRO PRO ALA THR
SEQRES 11 E 214 ILE GLU THR PHE ASN GLU ALA ALA LEU VAL VAL ASN ILE
SEQRES 12 E 214 THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU SER
SEQRES 13 E 214 SER ASP GLU LYS ARG GLU LEU LEU LYS ARG TYR ARG LEU
SEQRES 14 E 214 LYS GLU SER GLN LEU PRO ARG ILE GLN ARG ALA ASP PRO
SEQRES 15 E 214 VAL ALA LEU TYR LEU GLY LEU LYS ARG GLY GLU VAL VAL
SEQRES 16 E 214 LYS ILE ILE ARG LYS SER GLU THR SER GLY ARG TYR ALA
SEQRES 17 E 214 SER TYR ARG ILE CYS MET
SEQRES 1 F 87 LEU LYS GLU LYS ALA ILE PRO LYS ASP GLN ARG ALA THR
SEQRES 2 F 87 THR PRO TYR MET THR LYS TYR GLU ARG ALA ARG ILE LEU
SEQRES 3 F 87 GLY THR ARG ALA LEU GLN ILE SER MET ASN ALA PRO VAL
SEQRES 4 F 87 PHE VAL ASP LEU GLU GLY GLU THR ASP PRO LEU ARG ILE
SEQRES 5 F 87 ALA MET LYS GLU LEU ALA GLU LYS LYS ILE PRO LEU VAL
SEQRES 6 F 87 ILE ARG ARG TYR LEU PRO ASP GLY SER PHE GLU ASP TRP
SEQRES 7 F 87 SER VAL GLU GLU LEU ILE VAL ASP LEU
SEQRES 1 G 171 MET PHE PHE ILE LYS ASP LEU SER LEU ASN ILE THR LEU
SEQRES 2 G 171 HIS PRO SER PHE PHE GLY PRO ARG MET LYS GLN TYR LEU
SEQRES 3 G 171 LYS THR LYS LEU LEU GLU GLU VAL GLU GLY SER CYS THR
SEQRES 4 G 171 GLY LYS PHE GLY TYR ILE LEU CYS VAL LEU ASP TYR ASP
SEQRES 5 G 171 ASN ILE ASP ILE GLN ARG GLY ARG ILE LEU PRO THR ASP
SEQRES 6 G 171 GLY SER ALA GLU PHE ASN VAL LYS TYR ARG ALA VAL VAL
SEQRES 7 G 171 PHE LYS PRO PHE LYS GLY GLU VAL VAL ASP GLY THR VAL
SEQRES 8 G 171 VAL SER CYS SER GLN HIS GLY PHE GLU VAL GLN VAL GLY
SEQRES 9 G 171 PRO MET LYS VAL PHE VAL THR LYS HIS LEU MET PRO GLN
SEQRES 10 G 171 ASP LEU THR PHE ASN ALA GLY SER ASN PRO PRO SER TYR
SEQRES 11 G 171 GLN SER SER GLU ASP VAL ILE THR ILE LYS SER ARG ILE
SEQRES 12 G 171 ARG VAL LYS ILE GLU GLY CYS ILE SER GLN VAL SER SER
SEQRES 13 G 171 ILE HIS ALA ILE GLY SER ILE LYS GLU ASP TYR LEU GLY
SEQRES 14 G 171 ALA ILE
SEQRES 1 H 145 SER ASN THR LEU PHE ASP ASP ILE PHE GLN VAL SER GLU
SEQRES 2 H 145 VAL ASP PRO GLY ARG TYR ASN LYS VAL CYS ARG ILE GLU
SEQRES 3 H 145 ALA ALA SER THR THR GLN ASP GLN CYS LYS LEU THR LEU
SEQRES 4 H 145 ASP ILE ASN VAL GLU LEU PHE PRO VAL ALA ALA GLN ASP
SEQRES 5 H 145 SER LEU THR VAL THR ILE ALA SER SER LEU ASN LEU GLU
SEQRES 6 H 145 ASP THR PRO ALA ASN ASP SER SER ALA THR ARG SER TRP
SEQRES 7 H 145 ARG PRO PRO GLN ALA GLY ASP ARG SER LEU ALA ASP ASP
SEQRES 8 H 145 TYR ASP TYR VAL MET TYR GLY THR ALA TYR LYS PHE GLU
SEQRES 9 H 145 GLU VAL SER LYS ASP LEU ILE ALA VAL TYR TYR SER PHE
SEQRES 10 H 145 GLY GLY LEU LEU MET ARG LEU GLU GLY ASN TYR ARG ASN
SEQRES 11 H 145 LEU ASN ASN LEU LYS GLN GLU ASN ALA TYR LEU LEU ILE
SEQRES 12 H 145 ARG ARG
SEQRES 1 I 119 THR THR PHE ARG PHE CYS ARG ASP CYS ASN ASN MET LEU
SEQRES 2 I 119 TYR PRO ARG GLU ASP LYS GLU ASN ASN ARG LEU LEU PHE
SEQRES 3 I 119 GLU CYS ARG THR CYS SER TYR VAL GLU GLU ALA GLY SER
SEQRES 4 I 119 PRO LEU VAL TYR ARG HIS GLU LEU ILE THR ASN ILE GLY
SEQRES 5 I 119 GLU THR ALA GLY VAL VAL GLN ASP ILE GLY SER ASP PRO
SEQRES 6 I 119 THR LEU PRO ARG SER ASP ARG GLU CYS PRO LYS CYS HIS
SEQRES 7 I 119 SER ARG GLU ASN VAL PHE PHE GLN SER GLN GLN ARG ARG
SEQRES 8 I 119 LYS ASP THR SER MET VAL LEU PHE PHE VAL CYS LEU SER
SEQRES 9 I 119 CYS SER HIS ILE PHE THR SER ASP GLN LYS ASN LYS ARG
SEQRES 10 I 119 THR GLN
SEQRES 1 J 65 MET ILE VAL PRO VAL ARG CYS PHE SER CYS GLY LYS VAL
SEQRES 2 J 65 VAL GLY ASP LYS TRP GLU SER TYR LEU ASN LEU LEU GLN
SEQRES 3 J 65 GLU ASP GLU LEU ASP GLU GLY THR ALA LEU SER ARG LEU
SEQRES 4 J 65 GLY LEU LYS ARG TYR CYS CYS ARG ARG MET ILE LEU THR
SEQRES 5 J 65 HIS VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO
SEQRES 1 K 115 MET ASN ALA PRO ASP ARG PHE GLU LEU PHE LEU LEU GLY
SEQRES 2 K 115 GLU GLY GLU SER LYS LEU LYS ILE ASP PRO ASP THR LYS
SEQRES 3 K 115 ALA PRO ASN ALA VAL VAL ILE THR PHE GLU LYS GLU ASP
SEQRES 4 K 115 HIS THR LEU GLY ASN LEU ILE ARG ALA GLU LEU LEU ASN
SEQRES 5 K 115 ASP ARG LYS VAL LEU PHE ALA ALA TYR LYS VAL GLU HIS
SEQRES 6 K 115 PRO PHE PHE ALA ARG PHE LYS LEU ARG ILE GLN THR THR
SEQRES 7 K 115 GLU GLY TYR ASP PRO LYS ASP ALA LEU LYS ASN ALA CYS
SEQRES 8 K 115 ASN SER ILE ILE ASN LYS LEU GLY ALA LEU LYS THR ASN
SEQRES 9 K 115 PHE GLU THR GLU TRP ASN LEU GLN THR LEU ALA
SEQRES 1 L 46 ALA THR LEU LYS TYR ILE CYS ALA GLU CYS SER SER LYS
SEQRES 2 L 46 LEU SER LEU SER ARG THR ASP ALA VAL ARG CYS LYS ASP
SEQRES 3 L 46 CYS GLY HIS ARG ILE LEU LEU LYS ALA ARG THR LYS ARG
SEQRES 4 L 46 LEU VAL GLN PHE GLU ALA ARG
SEQRES 1 Q 15 PHE ILE LYS ARG ASP ARG MET ARG ARG ASN PHE LEU ARG
SEQRES 2 Q 15 MET ARG
HET ZN A1801 1
HET ZN A1802 1
HET MG A1803 1
HET ZN B1301 1
HET ZN C 301 1
HET ZN I 201 1
HET ZN I 202 1
HET ZN J 101 1
HET ZN L 101 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 14 ZN 8(ZN 2+)
FORMUL 16 MG MG 2+
HELIX 1 AA1 SER A 23 SER A 31 1 9
HELIX 2 AA2 ASN A 54 GLY A 59 1 6
HELIX 3 AA3 PHE A 95 VAL A 106 1 12
HELIX 4 AA4 ASN A 119 ILE A 128 1 10
HELIX 5 AA5 ASP A 130 LYS A 143 1 14
HELIX 6 AA6 SER A 203 HIS A 213 1 11
HELIX 7 AA7 SER A 215 LEU A 222 1 8
HELIX 8 AA8 ARG A 230 TRP A 233 5 4
HELIX 9 AA9 PRO A 243 ARG A 247 5 5
HELIX 10 AB1 ASP A 260 ASN A 282 1 23
HELIX 11 AB2 ALA A 288 ASP A 305 1 18
HELIX 12 AB3 SER A 324 LYS A 330 1 7
HELIX 13 AB4 GLY A 334 LEU A 340 1 7
HELIX 14 AB5 LYS A 368 LYS A 372 1 5
HELIX 15 AB6 THR A 381 GLY A 395 1 15
HELIX 16 AB7 VAL A 474 ASN A 479 1 6
HELIX 17 AB8 SER A 494 CYS A 505 1 12
HELIX 18 AB9 ALA A 506 ILE A 511 1 6
HELIX 19 AC1 GLN A 525 THR A 535 1 11
HELIX 20 AC2 LEU A 543 VAL A 553 1 11
HELIX 21 AC3 GLY A 574 SER A 579 1 6
HELIX 22 AC4 GLU A 618 GLY A 623 1 6
HELIX 23 AC5 GLY A 628 GLY A 638 1 11
HELIX 24 AC6 GLY A 638 GLY A 661 1 24
HELIX 25 AC7 GLY A 665 THR A 669 5 5
HELIX 26 AC8 ASP A 672 ALA A 699 1 28
HELIX 27 AC9 THR A 709 LEU A 737 1 29
HELIX 28 AD1 ASN A 741 GLY A 750 1 10
HELIX 29 AD2 SER A 754 ALA A 763 1 10
HELIX 30 AD3 SER A 793 GLY A 798 1 6
HELIX 31 AD4 THR A 809 GLU A 846 1 38
HELIX 32 AD5 ILE A 867 ASP A 871 5 5
HELIX 33 AD6 ASP A 874 ILE A 878 5 5
HELIX 34 AD7 SER A 889 ARG A 898 1 10
HELIX 35 AD8 SER A 915 LEU A 920 1 6
HELIX 36 AD9 ASP A 922 PHE A 947 1 26
HELIX 37 AE1 ASN A 959 HIS A 972 1 14
HELIX 38 AE2 THR A 982 LEU A 997 1 16
HELIX 39 AE3 ASN A 1004 VAL A 1015 1 12
HELIX 40 AE4 VAL A 1015 LEU A 1026 1 12
HELIX 41 AE5 ALA A 1027 GLU A 1034 1 8
HELIX 42 AE6 THR A 1038 VAL A 1057 1 20
HELIX 43 AE7 MET A 1063 GLN A 1078 1 16
HELIX 44 AE8 GLY A 1097 VAL A 1107 1 11
HELIX 45 AE9 GLU A 1121 ALA A 1125 5 5
HELIX 46 AF1 ASP A 1127 GLU A 1139 1 13
HELIX 47 AF2 LEU A 1143 VAL A 1146 1 4
HELIX 48 AF3 ASP A 1166 HIS A 1173 1 8
HELIX 49 AF4 ASP A 1198 LYS A 1205 1 8
HELIX 50 AF5 THR A 1208 LYS A 1221 1 14
HELIX 51 AF6 GLU A 1256 GLU A 1269 1 14
HELIX 52 AF7 ASN A 1312 MET A 1317 1 6
HELIX 53 AF8 SER A 1331 GLY A 1340 1 10
HELIX 54 AF9 GLY A 1340 ALA A 1357 1 18
HELIX 55 AG1 ASN A 1364 GLN A 1378 1 15
HELIX 56 AG2 GLY A 1388 SER A 1392 5 5
HELIX 57 AG3 GLY A 1395 SER A 1401 1 7
HELIX 58 AG4 THR A 1405 SER A 1415 1 11
HELIX 59 AG5 GLY A 1423 GLY A 1431 1 9
HELIX 60 AG6 ILE A 1436 GLY A 1439 5 4
HELIX 61 AG7 ASP A 1446 MET A 1454 1 9
HELIX 62 AG8 GLU B 28 LYS B 41 1 14
HELIX 63 AG9 VAL B 44 TYR B 57 1 14
HELIX 64 AH1 TYR B 57 CYS B 64 1 8
HELIX 65 AH2 TYR B 113 ARG B 120 1 8
HELIX 66 AH3 THR B 185 LEU B 192 1 8
HELIX 67 AH4 ILE B 282 LEU B 289 1 8
HELIX 68 AH5 GLY B 295 HIS B 300 1 6
HELIX 69 AH6 ASP B 307 MET B 313 1 7
HELIX 70 AH7 LEU B 314 PHE B 322 1 9
HELIX 71 AH8 ASP B 326 THR B 339 1 14
HELIX 72 AH9 LYS B 347 GLU B 359 1 13
HELIX 73 AI1 PHE B 370 LEU B 390 1 21
HELIX 74 AI2 HIS B 400 GLY B 402 5 3
HELIX 75 AI3 LEU B 408 THR B 435 1 28
HELIX 76 AI4 ALA B 450 GLY B 464 1 15
HELIX 77 AI5 THR B 487 ARG B 496 1 10
HELIX 78 AI6 HIS B 515 TRP B 519 5 5
HELIX 79 AI7 GLU B 529 CYS B 533 5 5
HELIX 80 AI8 PRO B 551 GLU B 560 1 10
HELIX 81 AI9 GLU B 567 TYR B 569 5 3
HELIX 82 AJ1 ASN B 592 GLY B 607 1 16
HELIX 83 AJ2 ARG B 654 GLN B 667 1 14
HELIX 84 AJ3 TRP B 681 GLU B 687 1 7
HELIX 85 AJ4 ALA B 695 GLU B 699 1 5
HELIX 86 AJ5 PRO B 707 GLU B 711 5 5
HELIX 87 AJ6 HIS B 744 LEU B 749 5 6
HELIX 88 AJ7 GLY B 750 ILE B 755 1 6
HELIX 89 AJ8 PHE B 758 ASN B 762 5 5
HELIX 90 AJ9 GLN B 763 GLY B 774 1 12
HELIX 91 AK1 LEU B 782 VAL B 787 5 6
HELIX 92 AK2 THR B 806 TYR B 811 5 6
HELIX 93 AK3 GLN B 843 ARG B 848 1 6
HELIX 94 AK4 THR B 889 LEU B 893 5 5
HELIX 95 AK5 THR B 1022 GLY B 1039 1 18
HELIX 96 AK6 THR B 1051 GLY B 1063 1 13
HELIX 97 AK7 MET B 1098 ILE B 1103 1 6
HELIX 98 AK8 GLY B 1131 GLY B 1142 1 12
HELIX 99 AK9 ALA B 1143 MET B 1152 1 10
HELIX 100 AL1 TYR B 1198 ALA B 1209 1 12
HELIX 101 AL2 ASP C 26 GLU C 40 1 15
HELIX 102 AL3 ALA C 59 ILE C 70 1 12
HELIX 103 AL4 ASP C 76 LEU C 80 5 5
HELIX 104 AL5 TYR C 82 CYS C 86 5 5
HELIX 105 AL6 HIS C 167 GLY C 171 5 5
HELIX 106 AL7 ASP C 196 TRP C 201 1 6
HELIX 107 AL8 SER C 204 GLU C 208 5 5
HELIX 108 AL9 PRO C 239 ASP C 266 1 28
HELIX 109 AM1 ASN D 51 LYS D 76 1 26
HELIX 110 AM2 GLU D 120 THR D 134 1 15
HELIX 111 AM3 ASN D 138 SER D 152 1 15
HELIX 112 AM4 ASP D 156 SER D 169 1 14
HELIX 113 AM5 HIS D 173 LEU D 183 1 11
HELIX 114 AM6 THR D 187 ILE D 195 1 9
HELIX 115 AM7 SER D 203 GLU D 218 1 16
HELIX 116 AM8 GLU E 4 GLY E 27 1 24
HELIX 117 AM9 THR E 31 GLU E 36 1 6
HELIX 118 AN1 PRO E 38 CYS E 47 1 10
HELIX 119 AN2 GLN E 54 SER E 59 1 6
HELIX 120 AN3 THR E 65 PHE E 72 1 8
HELIX 121 AN4 GLY E 89 LYS E 103 1 15
HELIX 122 AN5 THR E 117 LYS E 122 1 6
HELIX 123 AN6 ALA E 138 VAL E 142 5 5
HELIX 124 AN7 ASN E 143 HIS E 147 5 5
HELIX 125 AN8 SER E 157 ARG E 169 1 13
HELIX 126 AN9 ASP E 182 LEU E 188 1 7
HELIX 127 AO1 THR F 86 MET F 103 1 18
HELIX 128 AO2 ASP F 116 GLU F 127 1 12
HELIX 129 AO3 HIS G 14 PHE G 18 5 5
HELIX 130 AO4 ARG G 21 GLU G 35 1 15
HELIX 131 AO5 ASP G 50 ILE G 54 5 5
HELIX 132 AO6 HIS G 113 MET G 115 5 3
HELIX 133 AO7 VAL I 59 ASP I 65 5 7
HELIX 134 AO8 LYS J 17 GLU J 27 1 11
HELIX 135 AO9 ASP J 31 LEU J 39 1 9
HELIX 136 AP1 ARG J 43 THR J 52 1 10
HELIX 137 AP2 LEU J 56 ARG J 62 1 7
HELIX 138 AP3 ASP K 5 PHE K 10 5 6
HELIX 139 AP4 ASP K 39 ASP K 53 1 15
HELIX 140 AP5 ASP K 82 GLN K 112 1 31
HELIX 141 AP6 ARG Q 26 ARG Q 35 1 10
SHEET 1 AA1 3 LEU A1418 ASP A1419 0
SHEET 2 AA1 3 GLU A 16 LEU A 21 -1 N VAL A 17 O ASP A1419
SHEET 3 AA1 3 ILE B1212 TYR B1217 -1 O ARG B1215 N GLN A 18
SHEET 1 AA2 2 GLY A 82 PHE A 91 0
SHEET 2 AA2 2 ILE A 235 VAL A 241 -1 O LEU A 236 N VAL A 90
SHEET 1 AA3 3 ARG A 175 ASP A 177 0
SHEET 2 AA3 3 LYS A 180 TRP A 185 -1 O LYS A 180 N ASP A 177
SHEET 3 AA3 3 GLU A 198 LEU A 202 -1 O LEU A 202 N LEU A 181
SHEET 1 AA4 2 LYS A 343 VAL A 345 0
SHEET 2 AA4 2 LEU B1128 PHE B1130 -1 O PHE B1130 N LYS A 343
SHEET 1 AA5 8 HIS B1104 ARG B1106 0
SHEET 2 AA5 8 SER A 348 ASP A 356 -1 N ARG A 350 O HIS B1104
SHEET 3 AA5 8 GLU A 486 HIS A 490 -1 O LEU A 489 N ALA A 349
SHEET 4 AA5 8 PRO A 441 ASN A 445 -1 N ASN A 445 O ASN A 488
SHEET 5 AA5 8 MET A 455 ILE A 463 -1 O MET A 456 N PHE A 444
SHEET 6 AA5 8 GLN A 363 PRO A 367 1 N VAL A 366 O ILE A 463
SHEET 7 AA5 8 PHE A 468 ASN A 471 -1 O ARG A 469 N GLY A 365
SHEET 8 AA5 8 SER A 348 ASP A 356 1 N SER A 354 O PHE A 468
SHEET 1 AA6 4 THR A 375 VAL A 379 0
SHEET 2 AA6 4 LYS A 431 HIS A 435 -1 O VAL A 432 N GLU A 378
SHEET 3 AA6 4 ALA A 402 ARG A 407 -1 N TYR A 404 O GLU A 433
SHEET 4 AA6 4 ASP A 411 ASP A 414 -1 O ILE A 413 N VAL A 405
SHEET 1 AA7 2 VAL A 512 SER A 513 0
SHEET 2 AA7 2 LYS A 518 PRO A 519 -1 O LYS A 518 N SER A 513
SHEET 1 AA8 2 PHE A 540 GLU A 542 0
SHEET 2 AA8 2 LEU A 571 SER A 573 -1 O TRP A 572 N ILE A 541
SHEET 1 AA9 3 LEU A 588 ARG A 590 0
SHEET 2 AA9 3 MET A 605 ILE A 608 -1 O ILE A 607 N LEU A 588
SHEET 3 AA9 3 GLN A 611 PHE A 614 -1 O ILE A 613 N LEU A 606
SHEET 1 AB1 8 PHE A 662 SER A 663 0
SHEET 2 AB1 8 GLN B 821 CYS B 829 -1 O CYS B 829 N PHE A 662
SHEET 3 AB1 8 PRO B1089 ARG B1094 -1 O THR B1090 N ALA B 823
SHEET 4 AB1 8 LYS B 979 SER B 982 -1 N ALA B 981 O GLN B1093
SHEET 5 AB1 8 LYS B 987 TYR B 994 -1 O GLY B 988 N PHE B 980
SHEET 6 AB1 8 SER B 838 ASN B 842 1 N MET B 841 O ILE B 992
SHEET 7 AB1 8 LEU B1010 ILE B1012 -1 O ILE B1011 N ILE B 840
SHEET 8 AB1 8 GLN B 821 CYS B 829 1 N ALA B 826 O LEU B1010
SHEET 1 AB2 2 GLY A 766 GLN A 767 0
SHEET 2 AB2 2 PHE A 799 VAL A 800 -1 O VAL A 800 N GLY A 766
SHEET 1 AB3 2 MET A 849 VAL A 850 0
SHEET 2 AB3 2 THR A 856 ARG A 857 -1 O ARG A 857 N MET A 849
SHEET 1 AB4 2 GLU A 879 SER A 882 0
SHEET 2 AB4 2 ASN A 953 LEU A 956 -1 O TRP A 954 N GLN A 881
SHEET 1 AB5 4 VAL A1283 TYR A1287 0
SHEET 2 AB5 4 GLU A1303 GLU A1307 -1 O VAL A1305 N MET A1285
SHEET 3 AB5 4 LEU A1116 TYR A1119 -1 N VAL A1118 O LEU A1306
SHEET 4 AB5 4 TYR A1328 THR A1329 -1 O TYR A1328 N THR A1117
SHEET 1 AB6 2 THR A1141 THR A1142 0
SHEET 2 AB6 2 THR A1272 ARG A1274 -1 O ARG A1274 N THR A1141
SHEET 1 AB7 5 LEU A1224 TRP A1228 0
SHEET 2 AB7 5 LEU A1236 VAL A1243 -1 O ARG A1241 N PHE A1225
SHEET 3 AB7 5 GLN A1188 LEU A1197 -1 N LEU A1195 O ILE A1238
SHEET 4 AB7 5 THR A1147 TYR A1154 -1 N ILE A1148 O GLU A1196
SHEET 5 AB7 5 LEU I 42 ARG I 45 -1 O VAL I 43 N ILE A1152
SHEET 1 AB8 2 LYS A1290 PRO A1292 0
SHEET 2 AB8 2 TYR A1298 LYS A1300 -1 O VAL A1299 N VAL A1291
SHEET 1 AB9 7 THR D 5 THR D 7 0
SHEET 2 AB9 7 PHE G 3 LEU G 13 -1 O SER G 8 N SER D 6
SHEET 3 AB9 7 ALA G 68 PHE G 79 -1 O TYR G 74 N LEU G 7
SHEET 4 AB9 7 GLY G 59 ILE G 61 -1 N ARG G 60 O GLU G 69
SHEET 5 AB9 7 PHE A1441 ILE A1445 -1 N VAL A1443 O ILE G 61
SHEET 6 AB9 7 LEU F 132 TYR F 137 -1 O ARG F 135 N ASP A1442
SHEET 7 AB9 7 PHE F 143 SER F 147 -1 O TRP F 146 N ILE F 134
SHEET 1 AC1 4 ILE D 48 ALA D 49 0
SHEET 2 AC1 4 PHE G 3 LEU G 13 -1 O ILE G 4 N ILE D 48
SHEET 3 AC1 4 ALA G 68 PHE G 79 -1 O TYR G 74 N LEU G 7
SHEET 4 AC1 4 TYR G 44 LEU G 49 -1 N LEU G 49 O ARG G 75
SHEET 1 AC2 3 PHE B 92 PRO B 100 0
SHEET 2 AC2 3 SER B 125 VAL B 132 -1 O PHE B 129 N TYR B 96
SHEET 3 AC2 3 VAL B 165 PRO B 171 -1 O ILE B 167 N LEU B 128
SHEET 1 AC3 3 PHE B 203 ILE B 205 0
SHEET 2 AC3 3 SER B 208 LEU B 212 -1 O LYS B 210 N PHE B 203
SHEET 3 AC3 3 SER B 480 VAL B 482 -1 O GLN B 481 N VAL B 211
SHEET 1 AC4 3 LYS B 404 ASP B 407 0
SHEET 2 AC4 3 ALA B 214 SER B 218 -1 N ARG B 217 O ARG B 405
SHEET 3 AC4 3 THR B 498 ASN B 499 1 O ASN B 499 N GLU B 216
SHEET 1 AC5 5 VAL B 223 LYS B 227 0
SHEET 2 AC5 5 ILE B 234 SER B 242 -1 O GLU B 239 N GLN B 224
SHEET 3 AC5 5 SER B 252 TYR B 259 -1 O LEU B 258 N SER B 235
SHEET 4 AC5 5 ILE B 269 ALA B 271 -1 O LYS B 270 N LYS B 257
SHEET 5 AC5 5 ILE B 280 PRO B 281 -1 O ILE B 280 N ALA B 271
SHEET 1 AC6 2 ASN B 465 TRP B 466 0
SHEET 2 AC6 2 ARG B 476 ALA B 477 -1 O ARG B 476 N TRP B 466
SHEET 1 AC7 3 CYS B 544 ILE B 545 0
SHEET 2 AC7 3 VAL B 633 ILE B 639 -1 O TYR B 634 N CYS B 544
SHEET 3 AC7 3 VAL B 690 ASP B 694 -1 O ILE B 693 N ARG B 635
SHEET 1 AC8 4 CYS B 544 ILE B 545 0
SHEET 2 AC8 4 VAL B 633 ILE B 639 -1 O TYR B 634 N CYS B 544
SHEET 3 AC8 4 HIS B 740 CYS B 741 -1 O CYS B 741 N PHE B 638
SHEET 4 AC8 4 ILE B 703 ALA B 704 1 N ALA B 704 O HIS B 740
SHEET 1 AC9 5 GLU B 564 PRO B 565 0
SHEET 2 AC9 5 VAL B 585 HIS B 590 -1 O VAL B 589 N GLU B 564
SHEET 3 AC9 5 THR B 578 VAL B 582 -1 N THR B 578 O HIS B 590
SHEET 4 AC9 5 GLU B 623 PHE B 627 1 O LEU B 624 N PHE B 581
SHEET 5 AC9 5 SER B 614 ASP B 618 -1 N ILE B 616 O LYS B 625
SHEET 1 AD1 5 MET B 792 LEU B 796 0
SHEET 2 AD1 5 SER B 853 GLN B 862 -1 O LEU B 854 N ILE B 795
SHEET 3 AD1 5 LYS B 962 LYS B 972 -1 O VAL B 966 N TYR B 859
SHEET 4 AD1 5 GLY B 947 THR B 956 -1 N GLN B 951 O ARG B 967
SHEET 5 AD1 5 ARG B 904 VAL B 905 -1 N VAL B 905 O GLY B 947
SHEET 1 AD2 6 MET B 792 LEU B 796 0
SHEET 2 AD2 6 SER B 853 GLN B 862 -1 O LEU B 854 N ILE B 795
SHEET 3 AD2 6 LYS B 962 LYS B 972 -1 O VAL B 966 N TYR B 859
SHEET 4 AD2 6 GLY B 947 THR B 956 -1 N GLN B 951 O ARG B 967
SHEET 5 AD2 6 LEU L 56 LYS L 58 -1 O LYS L 58 N VAL B 952
SHEET 6 AD2 6 TYR L 29 CYS L 31 -1 N ILE L 30 O LEU L 57
SHEET 1 AD3 2 GLY B 804 THR B 805 0
SHEET 2 AD3 2 GLY B1042 ASP B1043 1 O GLY B1042 N THR B 805
SHEET 1 AD4 3 THR B 873 PHE B 874 0
SHEET 2 AD4 3 LYS B 914 PRO B 917 -1 O THR B 915 N THR B 873
SHEET 3 AD4 3 LYS B 934 ASP B 936 -1 O ARG B 935 N THR B 916
SHEET 1 AD5 2 VAL B 910 ILE B 912 0
SHEET 2 AD5 2 THR B 939 PRO B 940 -1 O THR B 939 N ILE B 912
SHEET 1 AD6 3 PHE B1001 THR B1002 0
SHEET 2 AD6 3 PHE B1069 TYR B1073 -1 O TYR B1073 N PHE B1001
SHEET 3 AD6 3 LYS B1080 PHE B1086 -1 O LEU B1081 N MET B1072
SHEET 1 AD7 2 ALA B1157 CYS B1163 0
SHEET 2 AD7 2 ILE B1191 PRO B1197 -1 O TYR B1192 N ILE B1162
SHEET 1 AD8 2 ILE B1172 LYS B1174 0
SHEET 2 AD8 2 GLN B1179 GLU B1181 -1 O GLU B1181 N ILE B1172
SHEET 1 AD9 4 GLN C 7 ALA C 13 0
SHEET 2 AD9 4 ASN C 17 SER C 23 -1 O ASP C 19 N ARG C 11
SHEET 3 AD9 4 PHE C 228 GLU C 233 -1 O MET C 230 N PHE C 20
SHEET 4 AD9 4 GLU C 177 TYR C 180 -1 N GLU C 177 O ASN C 231
SHEET 1 AE1 5 LEU C 118 ILE C 120 0
SHEET 2 AE1 5 SER C 96 PHE C 104 -1 N THR C 100 O VAL C 119
SHEET 3 AE1 5 GLU C 152 GLY C 162 -1 O ALA C 159 N VAL C 97
SHEET 4 AE1 5 THR C 43 ASN C 54 -1 N THR C 53 O LYS C 154
SHEET 5 AE1 5 VAL L 65 GLU L 68 -1 O PHE L 67 N VAL C 49
SHEET 1 AE2 2 THR C 111 TYR C 114 0
SHEET 2 AE2 2 LEU C 143 LEU C 147 -1 O LEU C 147 N THR C 111
SHEET 1 AE3 2 LYS D 36 ILE D 38 0
SHEET 2 AE3 2 GLU D 44 GLU D 46 -1 O GLU D 45 N GLN D 37
SHEET 1 AE4 4 PHE E 60 ALA E 62 0
SHEET 2 AE4 4 LEU E 78 PHE E 82 -1 O VAL E 80 N PHE E 60
SHEET 3 AE4 4 THR E 107 TYR E 112 1 O VAL E 111 N GLU E 81
SHEET 4 AE4 4 THR E 131 ASN E 136 1 O PHE E 135 N PHE E 110
SHEET 1 AE5 2 SER E 87 VAL E 88 0
SHEET 2 AE5 2 ASN E 115 ILE E 116 1 O ASN E 115 N VAL E 88
SHEET 1 AE6 4 LYS E 152 ARG E 155 0
SHEET 2 AE6 4 VAL E 195 LYS E 201 -1 O LYS E 197 N ILE E 154
SHEET 3 AE6 4 ARG E 207 CYS E 214 -1 O ARG E 212 N VAL E 196
SHEET 4 AE6 4 ARG E 177 ILE E 178 1 N ILE E 178 O ILE E 213
SHEET 1 AE7 7 GLY G 169 ALA G 170 0
SHEET 2 AE7 7 ARG G 142 GLN G 153 -1 N ARG G 144 O GLY G 169
SHEET 3 AE7 7 SER G 156 SER G 162 -1 O SER G 156 N GLN G 153
SHEET 4 AE7 7 MET G 106 THR G 111 1 N PHE G 109 O ALA G 159
SHEET 5 AE7 7 GLY G 98 VAL G 103 -1 N VAL G 101 O VAL G 108
SHEET 6 AE7 7 VAL G 86 SER G 95 -1 N THR G 90 O GLN G 102
SHEET 7 AE7 7 ARG G 142 GLN G 153 -1 O ILE G 143 N GLY G 89
SHEET 1 AE8 3 THR G 120 ASN G 122 0
SHEET 2 AE8 3 SER G 129 GLN G 131 -1 O GLN G 131 N THR G 120
SHEET 3 AE8 3 VAL G 136 ILE G 137 -1 O ILE G 137 N TYR G 130
SHEET 1 AE9 9 TYR H 95 TYR H 98 0
SHEET 2 AE9 9 TYR H 141 ARG H 145 -1 O LEU H 142 N MET H 97
SHEET 3 AE9 9 SER H 54 ALA H 60 -1 N ALA H 60 O TYR H 141
SHEET 4 AE9 9 THR H 4 ASP H 16 -1 N PHE H 10 O LEU H 55
SHEET 5 AE9 9 VAL H 23 SER H 30 -1 O ARG H 25 N ASP H 16
SHEET 6 AE9 9 LYS H 37 ASN H 43 -1 O LEU H 40 N ILE H 26
SHEET 7 AE9 9 LEU H 121 GLY H 127 -1 O ARG H 124 N THR H 39
SHEET 8 AE9 9 ILE H 112 PHE H 118 -1 N PHE H 118 O LEU H 121
SHEET 9 AE9 9 THR H 100 GLU H 106 -1 N TYR H 102 O TYR H 115
SHEET 1 AF1 3 LEU I 14 GLU I 18 0
SHEET 2 AF1 3 LEU I 25 CYS I 29 -1 O GLU I 28 N TYR I 15
SHEET 3 AF1 3 VAL I 35 GLU I 37 -1 O GLU I 36 N PHE I 27
SHEET 1 AF2 4 ARG I 70 SER I 71 0
SHEET 2 AF2 4 ASN I 83 PHE I 86 -1 O ASN I 83 N SER I 71
SHEET 3 AF2 4 PHE I 100 CYS I 103 -1 O VAL I 102 N VAL I 84
SHEET 4 AF2 4 ILE I 109 THR I 111 -1 O PHE I 110 N PHE I 101
SHEET 1 AF3 4 LEU K 19 PRO K 23 0
SHEET 2 AF3 4 ALA K 30 GLU K 36 -1 O VAL K 32 N ASP K 22
SHEET 3 AF3 4 ARG K 70 THR K 77 -1 O PHE K 71 N PHE K 35
SHEET 4 AF3 4 VAL K 56 LYS K 62 -1 N ALA K 60 O ARG K 74
LINK SG CYS A 67 ZN ZN A1802 1555 1555 2.17
LINK SG CYS A 70 ZN ZN A1802 1555 1555 2.50
LINK SG CYS A 77 ZN ZN A1802 1555 1555 2.20
LINK NE2 HIS A 80 ZN ZN A1802 1555 1555 2.03
LINK SG CYS A 107 ZN ZN A1801 1555 1555 2.29
LINK SG CYS A 110 ZN ZN A1801 1555 1555 2.32
LINK SG CYS A 148 ZN ZN A1801 1555 1555 2.42
LINK SG CYS A 167 ZN ZN A1801 1555 1555 2.43
LINK OD1 ASP A 483 MG MG A1803 1555 1555 1.94
LINK OD2 ASP A 483 MG MG A1803 1555 1555 2.87
LINK SG CYS B1163 ZN ZN B1301 1555 1555 2.22
LINK SG CYS B1166 ZN ZN B1301 1555 1555 2.23
LINK SG CYS B1182 ZN ZN B1301 1555 1555 2.35
LINK SG CYS B1185 ZN ZN B1301 1555 1555 2.27
LINK SG CYS C 86 ZN ZN C 301 1555 1555 2.18
LINK SG CYS C 88 ZN ZN C 301 1555 1555 2.25
LINK SG CYS C 92 ZN ZN C 301 1555 1555 2.28
LINK SG CYS C 95 ZN ZN C 301 1555 1555 2.28
LINK SG CYS I 7 ZN ZN I 201 1555 1555 2.32
LINK SG CYS I 10 ZN ZN I 201 1555 1555 2.31
LINK SG CYS I 29 ZN ZN I 201 1555 1555 2.35
LINK SG CYS I 32 ZN ZN I 201 1555 1555 2.30
LINK SG CYS I 75 ZN ZN I 202 1555 1555 2.44
LINK SG CYS I 78 ZN ZN I 202 1555 1555 2.34
LINK SG CYS I 103 ZN ZN I 202 1555 1555 2.50
LINK SG CYS I 106 ZN ZN I 202 1555 1555 2.33
LINK SG CYS J 7 ZN ZN J 101 1555 1555 2.36
LINK SG CYS J 10 ZN ZN J 101 1555 1555 2.26
LINK SG CYS J 45 ZN ZN J 101 1555 1555 2.34
LINK SG CYS J 46 ZN ZN J 101 1555 1555 2.23
LINK SG CYS L 31 ZN ZN L 101 1555 1555 2.48
LINK SG CYS L 34 ZN ZN L 101 1555 1555 2.31
LINK SG CYS L 48 ZN ZN L 101 1555 1555 2.29
LINK SG CYS L 51 ZN ZN L 101 1555 1555 2.36
CISPEP 1 GLN A 447 PRO A 448 0 3.58
CISPEP 2 LEU A 1081 ASN A 1082 0 9.58
CISPEP 3 ILE B 343 LYS B 344 0 2.06
CISPEP 4 GLU B 468 GLN B 469 0 -2.50
CISPEP 5 MET B 473 SER B 474 0 2.67
CISPEP 6 PRO E 128 PRO E 129 0 3.41
CISPEP 7 ASN G 126 PRO G 127 0 3.11
SITE 1 AC1 4 CYS A 107 CYS A 110 CYS A 148 CYS A 167
SITE 1 AC2 4 CYS A 67 CYS A 70 CYS A 77 HIS A 80
SITE 1 AC3 3 ASP A 481 ASP A 483 ASP A 485
SITE 1 AC4 4 CYS B1163 CYS B1166 CYS B1182 CYS B1185
SITE 1 AC5 4 CYS C 86 CYS C 88 CYS C 92 CYS C 95
SITE 1 AC6 4 CYS I 7 CYS I 10 CYS I 29 CYS I 32
SITE 1 AC7 4 CYS I 75 CYS I 78 CYS I 103 CYS I 106
SITE 1 AC8 4 CYS J 7 CYS J 10 CYS J 45 CYS J 46
SITE 1 AC9 4 CYS L 31 CYS L 34 CYS L 48 CYS L 51
CRYST1 222.820 392.730 283.420 90.00 90.00 90.00 C 2 2 21 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 0.004488 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002546 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003528 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
