HEADER DNA BINDING PROTEIN/DNA 28-OCT-13 4NDY
TITLE HUMAN MHF1-MHF2 DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (26-MER);
COMPND 3 CHAIN: E, O;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (26-MER);
COMPND 7 CHAIN: F, P;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: CENTROMERE PROTEIN S;
COMPND 11 CHAIN: C, G, A, I, J, K, Q, R, S, T;
COMPND 12 SYNONYM: CENP-S, APOPTOSIS-INDUCING TAF9-LIKE DOMAIN-CONTAINING
COMPND 13 PROTEIN 1, FANCM-INTERACTING HISTONE FOLD PROTEIN 1, FANCONI ANEMIA-
COMPND 14 ASSOCIATED POLYPEPTIDE OF 16 KDA;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: CENTROMERE PROTEIN X;
COMPND 18 CHAIN: D, H, B, L, M, N, U, V, W, X;
COMPND 19 SYNONYM: CENP-X, FANCM-INTERACTING HISTONE FOLD PROTEIN 2, FANCONI
COMPND 20 ANEMIA-ASSOCIATED POLYPEPTIDE OF 10 KDA, RETINOIC ACID-INDUCIBLE GENE
COMPND 21 D9 PROTEIN HOMOLOG, STIMULATED BY RETINOIC ACID GENE 13 PROTEIN
COMPND 22 HOMOLOG;
COMPND 23 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC DNA;
SOURCE 4 ORGANISM_TAXID: 32630;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: SYNTHETIC DNA;
SOURCE 8 ORGANISM_TAXID: 32630;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: APITD1, CENPS, FAAP16, MHF1;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 ROSSETTA 2;
SOURCE 17 MOL_ID: 4;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 GENE: STRA13, CENPX, FAAP10, MHF2;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 24 EXPRESSION_SYSTEM_STRAIN: BL21 ROSSETTA 2
KEYWDS HISTONE FOLD, DNA REPAIR, GENOME MAINTENANCE, CENTROMERE
KEYWDS 2 CONSTRUCTION, FANCONI ANEMIA, FANCM, NUCLEUS, DNA BINDING PROTEIN-
KEYWDS 3 DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.ZHAO,D.SARO,A.SACHPATZIDIS,P.SUNG,Y.XIONG
REVDAT 2 28-FEB-24 4NDY 1 SEQADV
REVDAT 1 22-JAN-14 4NDY 0
JRNL AUTH Q.ZHAO,D.SARO,A.SACHPATZIDIS,T.R.SINGH,D.SCHLINGMAN,
JRNL AUTH 2 X.F.ZHENG,A.MACK,M.S.TSAI,S.MOCHRIE,L.REGAN,A.R.MEETEI,
JRNL AUTH 3 P.SUNG,Y.XIONG
JRNL TITL THE MHF COMPLEX SENSES BRANCHED DNA BY BINDING A PAIR OF
JRNL TITL 2 CROSSOVER DNA DUPLEXES.
JRNL REF NAT COMMUN V. 5 2987 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 24390579
JRNL DOI 10.1038/NCOMMS3987
REMARK 2
REMARK 2 RESOLUTION. 7.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 7.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 108.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 7171
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.100
REMARK 3 FREE R VALUE TEST SET COUNT : 439
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 7.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 7.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 436
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13734
REMARK 3 NUCLEIC ACID ATOMS : 2132
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 310.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -20.27000
REMARK 3 B22 (A**2) : -20.27000
REMARK 3 B33 (A**2) : 40.53000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.648
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 2.308
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 613.494
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.894
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.848
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 4
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.461
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -K, -H, -L
REMARK 3 TWIN FRACTION : 0.046
REMARK 3 TWIN DOMAIN : 3
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.045
REMARK 3 TWIN DOMAIN : 4
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.449
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 26
REMARK 3 ORIGIN FOR THE GROUP (A): 114.7505 28.2498 46.1394
REMARK 3 T TENSOR
REMARK 3 T11: 2.1500 T22: 2.3090
REMARK 3 T33: 2.5105 T12: 0.0987
REMARK 3 T13: 0.0333 T23: 0.0806
REMARK 3 L TENSOR
REMARK 3 L11: 4.8151 L22: 2.0470
REMARK 3 L33: 2.3070 L12: -2.3805
REMARK 3 L13: -2.2120 L23: 0.9989
REMARK 3 S TENSOR
REMARK 3 S11: -1.7541 S12: 1.0124 S13: 1.3530
REMARK 3 S21: 1.3798 S22: 0.8261 S23: -0.7524
REMARK 3 S31: 1.2365 S32: -0.4702 S33: 0.9280
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 26
REMARK 3 ORIGIN FOR THE GROUP (A): 115.3394 27.2135 44.6338
REMARK 3 T TENSOR
REMARK 3 T11: 2.5561 T22: 2.2623
REMARK 3 T33: 2.1311 T12: -0.4293
REMARK 3 T13: -0.1132 T23: -0.0529
REMARK 3 L TENSOR
REMARK 3 L11: 15.3798 L22: 4.1410
REMARK 3 L33: 3.8032 L12: -6.0000
REMARK 3 L13: -4.7021 L23: 2.3859
REMARK 3 S TENSOR
REMARK 3 S11: -3.0175 S12: 1.8093 S13: 1.4585
REMARK 3 S21: 1.4993 S22: 1.2909 S23: -0.6245
REMARK 3 S31: 1.4702 S32: -0.1905 S33: 1.7265
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 26
REMARK 3 ORIGIN FOR THE GROUP (A): 113.8809 -29.3212 16.6400
REMARK 3 T TENSOR
REMARK 3 T11: 2.8603 T22: 2.5835
REMARK 3 T33: 2.5563 T12: 0.1124
REMARK 3 T13: 0.2470 T23: 0.0811
REMARK 3 L TENSOR
REMARK 3 L11: 1.8749 L22: 0.8145
REMARK 3 L33: 1.3162 L12: 0.4201
REMARK 3 L13: 0.4584 L23: 0.3933
REMARK 3 S TENSOR
REMARK 3 S11: -1.2183 S12: -1.6108 S13: -0.8368
REMARK 3 S21: -1.3385 S22: 0.3567 S23: -0.6402
REMARK 3 S31: -1.3959 S32: -0.5709 S33: 0.8616
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 26
REMARK 3 ORIGIN FOR THE GROUP (A): 114.0304 -28.4083 17.5782
REMARK 3 T TENSOR
REMARK 3 T11: 3.8277 T22: 2.9352
REMARK 3 T33: 2.4540 T12: 0.3765
REMARK 3 T13: 0.4712 T23: -0.1388
REMARK 3 L TENSOR
REMARK 3 L11: 30.6491 L22: 10.3368
REMARK 3 L33: 3.7425 L12: 15.5059
REMARK 3 L13: 9.4072 L23: 5.8210
REMARK 3 S TENSOR
REMARK 3 S11: -0.3268 S12: -0.4123 S13: 0.8081
REMARK 3 S21: -0.3515 S22: -0.2018 S23: 0.5117
REMARK 3 S31: -0.7600 S32: -0.2561 S33: 0.5286
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 14 C 106
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0341 -34.0163 -11.2021
REMARK 3 T TENSOR
REMARK 3 T11: 3.0881 T22: 4.0821
REMARK 3 T33: 2.4825 T12: -0.1712
REMARK 3 T13: -1.0632 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 3.5687 L22: 9.5115
REMARK 3 L33: 6.3166 L12: 1.1023
REMARK 3 L13: -3.6041 L23: -5.9563
REMARK 3 S TENSOR
REMARK 3 S11: 1.1998 S12: -0.0380 S13: -0.0421
REMARK 3 S21: -0.0241 S22: -1.1860 S23: 1.0776
REMARK 3 S31: -1.1671 S32: 1.2802 S33: -0.0138
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 8 D 81
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3070 -38.8681 -11.8733
REMARK 3 T TENSOR
REMARK 3 T11: 3.8726 T22: 3.6474
REMARK 3 T33: 4.3777 T12: -0.2327
REMARK 3 T13: -1.0942 T23: -0.2450
REMARK 3 L TENSOR
REMARK 3 L11: 0.1937 L22: 1.0777
REMARK 3 L33: 2.9957 L12: 0.1982
REMARK 3 L13: -0.3504 L23: 0.8022
REMARK 3 S TENSOR
REMARK 3 S11: -0.1272 S12: 0.0326 S13: -0.3139
REMARK 3 S21: 0.7983 S22: -0.8019 S23: -0.0840
REMARK 3 S31: 0.7105 S32: 0.7295 S33: 0.9291
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 14 G 106
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2310 -53.2284 -6.9962
REMARK 3 T TENSOR
REMARK 3 T11: 2.7068 T22: 2.8345
REMARK 3 T33: 3.5443 T12: 0.1787
REMARK 3 T13: 0.2570 T23: -0.3396
REMARK 3 L TENSOR
REMARK 3 L11: 2.8973 L22: 13.3923
REMARK 3 L33: 1.0218 L12: 4.9625
REMARK 3 L13: 0.1717 L23: -1.8364
REMARK 3 S TENSOR
REMARK 3 S11: 0.3301 S12: 0.2252 S13: 0.0823
REMARK 3 S21: 1.7694 S22: -1.2499 S23: -0.6790
REMARK 3 S31: -0.9477 S32: 0.5205 S33: 0.9198
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 8 H 81
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4537 -56.4200 -6.6125
REMARK 3 T TENSOR
REMARK 3 T11: 2.1070 T22: 1.9957
REMARK 3 T33: 2.8494 T12: 0.0607
REMARK 3 T13: 0.1885 T23: 0.2102
REMARK 3 L TENSOR
REMARK 3 L11: 11.4608 L22: 15.6697
REMARK 3 L33: 8.6945 L12: -9.9289
REMARK 3 L13: -6.8862 L23: 11.6166
REMARK 3 S TENSOR
REMARK 3 S11: 0.3740 S12: 0.3316 S13: -0.8840
REMARK 3 S21: 0.6399 S22: -1.0900 S23: 0.4732
REMARK 3 S31: 0.4587 S32: -1.0082 S33: 0.7160
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 14 A 106
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9908 -94.8477 -5.7006
REMARK 3 T TENSOR
REMARK 3 T11: 1.5853 T22: 1.5127
REMARK 3 T33: 1.6119 T12: -0.1922
REMARK 3 T13: 0.2530 T23: 0.1096
REMARK 3 L TENSOR
REMARK 3 L11: 2.0129 L22: 4.3860
REMARK 3 L33: 10.0543 L12: 0.0446
REMARK 3 L13: -3.1885 L23: 4.4994
REMARK 3 S TENSOR
REMARK 3 S11: 0.2370 S12: 0.4174 S13: -0.0988
REMARK 3 S21: 0.5680 S22: -0.1600 S23: 0.1781
REMARK 3 S31: 0.3092 S32: -0.4973 S33: -0.0771
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 8 B 81
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0903 -90.7021 -5.1509
REMARK 3 T TENSOR
REMARK 3 T11: 2.0594 T22: 2.3900
REMARK 3 T33: 3.2474 T12: -0.0806
REMARK 3 T13: -0.0113 T23: -0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 1.2758 L22: 6.4812
REMARK 3 L33: 9.8067 L12: 0.1417
REMARK 3 L13: -2.2625 L23: 4.3930
REMARK 3 S TENSOR
REMARK 3 S11: -0.2092 S12: -1.4815 S13: 1.0418
REMARK 3 S21: -1.6638 S22: 0.0330 S23: 0.2228
REMARK 3 S31: 0.5710 S32: 3.4100 S33: 0.1762
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 14 I 118
REMARK 3 ORIGIN FOR THE GROUP (A): 80.9554 50.0764 41.5295
REMARK 3 T TENSOR
REMARK 3 T11: 2.0095 T22: 2.2154
REMARK 3 T33: 1.1255 T12: 0.3731
REMARK 3 T13: -0.1359 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 12.4546 L22: 10.4161
REMARK 3 L33: 0.9945 L12: -0.0466
REMARK 3 L13: -3.3323 L23: 0.2704
REMARK 3 S TENSOR
REMARK 3 S11: -0.7218 S12: -1.6084 S13: -0.3578
REMARK 3 S21: -0.5664 S22: 0.5128 S23: -1.4071
REMARK 3 S31: 0.6266 S32: 0.4645 S33: 0.2089
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 14 J 106
REMARK 3 ORIGIN FOR THE GROUP (A): 68.6359 45.1164 13.7696
REMARK 3 T TENSOR
REMARK 3 T11: 2.4283 T22: 2.0023
REMARK 3 T33: 2.3697 T12: 0.2363
REMARK 3 T13: -0.1077 T23: -0.1252
REMARK 3 L TENSOR
REMARK 3 L11: 5.2819 L22: 6.0220
REMARK 3 L33: 0.3663 L12: 5.6387
REMARK 3 L13: 1.2130 L23: 1.2844
REMARK 3 S TENSOR
REMARK 3 S11: 0.6114 S12: -0.1924 S13: 0.1611
REMARK 3 S21: 0.6549 S22: -0.3068 S23: 0.2059
REMARK 3 S31: 0.1191 S32: 0.2801 S33: -0.3046
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 14 K 118
REMARK 3 ORIGIN FOR THE GROUP (A): 100.5551 16.2598 30.8073
REMARK 3 T TENSOR
REMARK 3 T11: 2.5146 T22: 2.6248
REMARK 3 T33: 2.1977 T12: 0.0063
REMARK 3 T13: -0.2940 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.4360 L22: 4.8092
REMARK 3 L33: 3.8849 L12: -0.6218
REMARK 3 L13: 0.6048 L23: 2.2898
REMARK 3 S TENSOR
REMARK 3 S11: -0.8040 S12: -0.1766 S13: 0.2667
REMARK 3 S21: -0.2023 S22: 0.5396 S23: -0.2993
REMARK 3 S31: -1.3009 S32: -0.3799 S33: 0.2644
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 8 L 81
REMARK 3 ORIGIN FOR THE GROUP (A): 94.0593 12.7849 30.9018
REMARK 3 T TENSOR
REMARK 3 T11: 2.7241 T22: 3.2831
REMARK 3 T33: 3.2837 T12: -0.2515
REMARK 3 T13: -0.3984 T23: -0.5433
REMARK 3 L TENSOR
REMARK 3 L11: 0.9262 L22: 4.8141
REMARK 3 L33: 0.5985 L12: -1.8468
REMARK 3 L13: 0.0611 L23: -0.9104
REMARK 3 S TENSOR
REMARK 3 S11: -0.5960 S12: 0.1902 S13: -0.9271
REMARK 3 S21: 0.0110 S22: 0.3880 S23: 1.1256
REMARK 3 S31: 0.1934 S32: -0.8269 S33: 0.2080
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 8 M 81
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6428 52.3645 40.4145
REMARK 3 T TENSOR
REMARK 3 T11: 2.2710 T22: 2.4395
REMARK 3 T33: 0.0457 T12: -0.4379
REMARK 3 T13: 0.1522 T23: 0.0647
REMARK 3 L TENSOR
REMARK 3 L11: 15.2162 L22: 13.6551
REMARK 3 L33: 4.0888 L12: -5.1848
REMARK 3 L13: 2.0971 L23: 1.1060
REMARK 3 S TENSOR
REMARK 3 S11: 0.4077 S12: 0.1274 S13: -0.4455
REMARK 3 S21: -0.2812 S22: -0.4868 S23: 0.3158
REMARK 3 S31: -1.1151 S32: 0.2137 S33: 0.0791
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 8 N 81
REMARK 3 ORIGIN FOR THE GROUP (A): 64.6757 47.8259 14.0699
REMARK 3 T TENSOR
REMARK 3 T11: 2.1765 T22: 1.9735
REMARK 3 T33: 2.1316 T12: 0.0510
REMARK 3 T13: 0.1136 T23: -0.2043
REMARK 3 L TENSOR
REMARK 3 L11: 0.1757 L22: 3.9338
REMARK 3 L33: 1.0572 L12: -0.6579
REMARK 3 L13: 0.3777 L23: -1.7628
REMARK 3 S TENSOR
REMARK 3 S11: -0.3267 S12: -0.3521 S13: 0.1660
REMARK 3 S21: 0.3170 S22: -0.0594 S23: -0.2741
REMARK 3 S31: 0.2539 S32: -0.5554 S33: 0.3862
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 14 Q 118
REMARK 3 ORIGIN FOR THE GROUP (A): 80.2185 -51.3587 20.1870
REMARK 3 T TENSOR
REMARK 3 T11: 2.2540 T22: 1.8392
REMARK 3 T33: 1.1894 T12: 0.1731
REMARK 3 T13: 0.0216 T23: -0.1527
REMARK 3 L TENSOR
REMARK 3 L11: 20.0646 L22: 5.1594
REMARK 3 L33: 2.4836 L12: 5.6294
REMARK 3 L13: 2.3725 L23: -1.9904
REMARK 3 S TENSOR
REMARK 3 S11: -0.8425 S12: -1.0301 S13: -1.1141
REMARK 3 S21: -0.0440 S22: 0.0869 S23: -1.0967
REMARK 3 S31: -0.7663 S32: -0.2185 S33: 0.7555
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 14 R 106
REMARK 3 ORIGIN FOR THE GROUP (A): 69.9504 -45.6633 46.0937
REMARK 3 T TENSOR
REMARK 3 T11: 2.3448 T22: 1.6691
REMARK 3 T33: 2.1774 T12: -0.0925
REMARK 3 T13: -0.5236 T23: -0.1082
REMARK 3 L TENSOR
REMARK 3 L11: 8.0721 L22: 7.9288
REMARK 3 L33: 8.7795 L12: 0.6657
REMARK 3 L13: -2.0424 L23: -8.1223
REMARK 3 S TENSOR
REMARK 3 S11: 1.4234 S12: -0.3469 S13: -1.0674
REMARK 3 S21: 0.1655 S22: -0.3551 S23: 1.0112
REMARK 3 S31: 0.2610 S32: 0.5218 S33: -1.0684
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 14 S 106
REMARK 3 ORIGIN FOR THE GROUP (A): 61.7408 -82.0521 1.6818
REMARK 3 T TENSOR
REMARK 3 T11: 0.9288 T22: 2.0885
REMARK 3 T33: 1.9454 T12: -0.4300
REMARK 3 T13: 0.6040 T23: 0.3893
REMARK 3 L TENSOR
REMARK 3 L11: 10.4724 L22: 9.2801
REMARK 3 L33: 17.3710 L12: -9.3138
REMARK 3 L13: 12.2676 L23: -9.2659
REMARK 3 S TENSOR
REMARK 3 S11: -0.0392 S12: 0.2926 S13: -0.1673
REMARK 3 S21: 0.6144 S22: 0.1984 S23: 0.3791
REMARK 3 S31: 0.8682 S32: 0.3713 S33: -0.1593
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 14 T 118
REMARK 3 ORIGIN FOR THE GROUP (A): 101.4448 -16.6182 29.8638
REMARK 3 T TENSOR
REMARK 3 T11: 2.6379 T22: 4.2674
REMARK 3 T33: 3.0502 T12: -0.3704
REMARK 3 T13: 0.5624 T23: 0.1524
REMARK 3 L TENSOR
REMARK 3 L11: 7.8322 L22: 1.3465
REMARK 3 L33: 13.2518 L12: 2.7284
REMARK 3 L13: -2.1690 L23: 0.8575
REMARK 3 S TENSOR
REMARK 3 S11: -0.5134 S12: 3.1023 S13: -0.3586
REMARK 3 S21: 0.2498 S22: 0.3937 S23: 0.4177
REMARK 3 S31: 0.7219 S32: -0.3659 S33: 0.1197
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 8 U 81
REMARK 3 ORIGIN FOR THE GROUP (A): 94.8687 -12.4921 29.3940
REMARK 3 T TENSOR
REMARK 3 T11: 4.1220 T22: 4.4901
REMARK 3 T33: 4.5923 T12: -0.4065
REMARK 3 T13: -0.1003 T23: -0.3790
REMARK 3 L TENSOR
REMARK 3 L11: 3.8576 L22: 7.1249
REMARK 3 L33: 0.2191 L12: 5.0552
REMARK 3 L13: -0.0266 L23: -0.3046
REMARK 3 S TENSOR
REMARK 3 S11: -1.0872 S12: 0.8706 S13: 1.0709
REMARK 3 S21: 0.0013 S22: 1.3549 S23: 0.2953
REMARK 3 S31: 0.0500 S32: -0.9238 S33: -0.2677
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 8 V 81
REMARK 3 ORIGIN FOR THE GROUP (A): 73.1514 -53.2149 21.1782
REMARK 3 T TENSOR
REMARK 3 T11: 3.2052 T22: 2.0256
REMARK 3 T33: 1.6893 T12: 0.1473
REMARK 3 T13: 0.2751 T23: -0.3298
REMARK 3 L TENSOR
REMARK 3 L11: 8.1662 L22: 6.0477
REMARK 3 L33: 4.4381 L12: 1.5432
REMARK 3 L13: -0.2180 L23: -4.9804
REMARK 3 S TENSOR
REMARK 3 S11: -0.6302 S12: 1.3562 S13: -0.1106
REMARK 3 S21: 0.8077 S22: 1.1302 S23: 0.1773
REMARK 3 S31: -0.2160 S32: -0.5451 S33: -0.5000
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 8 W 81
REMARK 3 ORIGIN FOR THE GROUP (A): 66.6386 -47.4258 44.8748
REMARK 3 T TENSOR
REMARK 3 T11: 1.9203 T22: 2.0540
REMARK 3 T33: 2.0863 T12: 0.0881
REMARK 3 T13: -0.1157 T23: 0.1241
REMARK 3 L TENSOR
REMARK 3 L11: 0.8666 L22: 4.4481
REMARK 3 L33: 10.4896 L12: 1.0019
REMARK 3 L13: 0.0549 L23: 5.5279
REMARK 3 S TENSOR
REMARK 3 S11: -0.5530 S12: -0.2240 S13: 0.5443
REMARK 3 S21: -0.1512 S22: -0.2390 S23: 0.9116
REMARK 3 S31: -0.3015 S32: -0.9298 S33: 0.7921
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 8 X 81
REMARK 3 ORIGIN FOR THE GROUP (A): 58.9597 -78.7737 1.3104
REMARK 3 T TENSOR
REMARK 3 T11: 1.7395 T22: 2.0751
REMARK 3 T33: 2.5987 T12: -0.1449
REMARK 3 T13: 0.2556 T23: 0.1220
REMARK 3 L TENSOR
REMARK 3 L11: 3.8712 L22: 3.5904
REMARK 3 L33: 3.9237 L12: 2.0493
REMARK 3 L13: 1.8943 L23: -0.0170
REMARK 3 S TENSOR
REMARK 3 S11: -0.7118 S12: 1.0975 S13: 0.5322
REMARK 3 S21: 0.7959 S22: -0.6778 S23: -0.5131
REMARK 3 S31: -0.6633 S32: 1.7011 S33: 1.3896
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.30
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4NDY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083081.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : APS
REMARK 200 BEAMLINE : 24-ID-E
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 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7171
REMARK 200 RESOLUTION RANGE HIGH (A) : 6.990
REMARK 200 RESOLUTION RANGE LOW (A) : 108.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 6.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 100.0
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 (%): 75.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1-0.3M AMMONIUM PHOSPHATE, MICRO
REMARK 280 -BATCH UNDER OIL, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, I, J, M, N
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, O, P, K, L, T, U
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P, Q, R, V, W
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, S, X
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H
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 ASN C 107
REMARK 465 LEU C 108
REMARK 465 GLU C 109
REMARK 465 ARG C 110
REMARK 465 LYS C 111
REMARK 465 ALA C 112
REMARK 465 GLN C 113
REMARK 465 LYS C 114
REMARK 465 LYS C 115
REMARK 465 LYS C 116
REMARK 465 LYS C 117
REMARK 465 SER C 118
REMARK 465 ASN G 107
REMARK 465 LEU G 108
REMARK 465 GLU G 109
REMARK 465 ARG G 110
REMARK 465 LYS G 111
REMARK 465 ALA G 112
REMARK 465 GLN G 113
REMARK 465 LYS G 114
REMARK 465 LYS G 115
REMARK 465 LYS G 116
REMARK 465 LYS G 117
REMARK 465 SER G 118
REMARK 465 ASN A 107
REMARK 465 LEU A 108
REMARK 465 GLU A 109
REMARK 465 ARG A 110
REMARK 465 LYS A 111
REMARK 465 ALA A 112
REMARK 465 GLN A 113
REMARK 465 LYS A 114
REMARK 465 LYS A 115
REMARK 465 LYS A 116
REMARK 465 LYS A 117
REMARK 465 SER A 118
REMARK 465 ASN J 107
REMARK 465 LEU J 108
REMARK 465 GLU J 109
REMARK 465 ARG J 110
REMARK 465 LYS J 111
REMARK 465 ALA J 112
REMARK 465 GLN J 113
REMARK 465 LYS J 114
REMARK 465 LYS J 115
REMARK 465 LYS J 116
REMARK 465 LYS J 117
REMARK 465 SER J 118
REMARK 465 ASN R 107
REMARK 465 LEU R 108
REMARK 465 GLU R 109
REMARK 465 ARG R 110
REMARK 465 LYS R 111
REMARK 465 ALA R 112
REMARK 465 GLN R 113
REMARK 465 LYS R 114
REMARK 465 LYS R 115
REMARK 465 LYS R 116
REMARK 465 LYS R 117
REMARK 465 SER R 118
REMARK 465 ASN S 107
REMARK 465 LEU S 108
REMARK 465 GLU S 109
REMARK 465 ARG S 110
REMARK 465 LYS S 111
REMARK 465 ALA S 112
REMARK 465 GLN S 113
REMARK 465 LYS S 114
REMARK 465 LYS S 115
REMARK 465 LYS S 116
REMARK 465 LYS S 117
REMARK 465 SER S 118
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 OE1 GLN Q 41 CD2 HIS S 24 1.65
REMARK 500 O ASP H 61 CE LYS A 44 1.73
REMARK 500 C2 DA E 11 O2 DT F 17 1.86
REMARK 500 OP1 DT F 22 N VAL M 30 1.97
REMARK 500 NH1 ARG Q 87 OD2 ASP R 64 1.99
REMARK 500 OP1 DT P 14 NE2 HIS U 20 2.07
REMARK 500 CD1 LEU Q 36 OH TYR S 25 2.08
REMARK 500 OP1 DT P 14 CD2 HIS U 20 2.09
REMARK 500 N6 DA O 21 O4 DT P 6 2.10
REMARK 500 CE1 HIS A 71 CE1 HIS S 71 2.13
REMARK 500 O ASP H 61 NZ LYS A 44 2.16
REMARK 500 C2 DA E 17 O2 DT F 11 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CB ALA G 48 OE2 GLU J 32 3555 2.00
REMARK 500 OD2 ASP H 61 NH1 ARG M 64 3554 2.04
REMARK 500 OD1 ASP B 61 NE2 GLN J 45 3555 2.10
REMARK 500 OP2 DA E 1 OE1 GLU N 13 1556 2.11
REMARK 500
REMARK 500 REMARK: NULL
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 DA E 24 O3' DA E 25 P 0.078
REMARK 500 DT P 1 P DT P 1 OP2 0.116
REMARK 500 GLU G 33 CD GLU G 33 OE1 0.070
REMARK 500 GLU I 32 CD GLU I 32 OE2 0.118
REMARK 500 GLU I 33 CG GLU I 33 CD 0.272
REMARK 500 GLU I 33 CD GLU I 33 OE1 0.085
REMARK 500 SER I 118 CB SER I 118 OG -0.089
REMARK 500 SER I 118 C SER I 118 O 0.123
REMARK 500 GLU J 66 CG GLU J 66 CD 0.111
REMARK 500 GLU J 66 CD GLU J 66 OE1 0.088
REMARK 500 GLU Q 32 CD GLU Q 32 OE2 0.122
REMARK 500 GLU R 32 CD GLU R 32 OE1 0.140
REMARK 500 GLU R 33 CD GLU R 33 OE1 0.080
REMARK 500 GLU R 59 CD GLU R 59 OE1 0.073
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 DA O 23 C3' - C2' - C1' ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG I 18 CG - CD - NE ANGL. DEV. = -17.2 DEGREES
REMARK 500 GLU I 33 OE1 - CD - OE2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 CYS J 29 CA - CB - SG ANGL. DEV. = 10.0 DEGREES
REMARK 500 CYS K 29 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG Q 110 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 HIS S 71 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 CYS T 29 CA - CB - SG ANGL. DEV. = 7.4 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 TYR A 15 -56.50 45.50
REMARK 500 ARG A 70 -70.82 -88.96
REMARK 500 HIS A 71 -59.95 -0.60
REMARK 500 ASP U 26 1.50 -69.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 70 HIS A 71 144.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NE1 RELATED DB: PDB
DBREF 4NDY C 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY D 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY G 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY H 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY A 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY B 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY I 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY J 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY K 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY L 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY M 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY N 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY Q 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY R 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY S 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY T 14 105 UNP Q8N2Z9 CENPS_HUMAN 14 105
DBREF 4NDY U 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY V 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY W 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY X 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NDY E 1 26 PDB 4NDY 4NDY 1 26
DBREF 4NDY O 1 26 PDB 4NDY 4NDY 1 26
DBREF 4NDY F 1 26 PDB 4NDY 4NDY 1 26
DBREF 4NDY P 1 26 PDB 4NDY 4NDY 1 26
SEQADV 4NDY ALA C 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA C 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN C 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU C 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU C 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG C 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS C 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA C 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN C 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS C 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS C 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS C 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS C 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER C 118 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA G 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA G 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN G 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU G 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU G 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG G 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS G 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA G 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN G 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS G 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS G 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS G 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS G 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER G 118 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA A 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA A 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN A 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU A 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU A 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG A 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS A 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA A 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN A 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS A 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS A 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS A 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS A 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER A 118 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA I 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA I 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN I 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU I 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU I 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG I 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS I 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA I 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN I 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS I 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS I 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS I 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS I 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER I 118 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA J 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA J 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN J 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU J 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU J 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG J 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS J 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA J 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN J 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS J 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS J 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS J 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS J 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER J 118 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA K 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA K 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN K 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU K 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU K 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG K 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS K 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA K 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN K 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS K 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS K 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS K 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS K 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER K 118 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA Q 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA Q 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN Q 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU Q 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU Q 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG Q 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS Q 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA Q 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN Q 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS Q 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS Q 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS Q 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS Q 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER Q 118 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA R 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA R 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN R 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU R 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU R 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG R 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS R 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA R 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN R 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS R 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS R 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS R 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS R 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER R 118 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA S 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA S 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN S 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU S 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU S 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG S 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS S 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA S 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN S 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS S 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS S 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS S 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS S 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER S 118 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA T 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NDY ALA T 106 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ASN T 107 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LEU T 108 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLU T 109 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ARG T 110 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS T 111 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY ALA T 112 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY GLN T 113 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS T 114 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS T 115 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS T 116 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY LYS T 117 UNP Q8N2Z9 EXPRESSION TAG
SEQADV 4NDY SER T 118 UNP Q8N2Z9 EXPRESSION TAG
SEQRES 1 E 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 2 E 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 1 F 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 2 F 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 1 O 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 2 O 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 1 P 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 2 P 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 1 C 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 C 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 C 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 C 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 C 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 C 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 C 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 C 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 C 105 SER
SEQRES 1 D 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 D 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 D 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 D 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 D 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 D 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 G 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 G 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 G 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 G 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 G 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 G 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 G 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 G 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 G 105 SER
SEQRES 1 H 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 H 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 H 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 H 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 H 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 H 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 A 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 A 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 A 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 A 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 A 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 A 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 A 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 A 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 A 105 SER
SEQRES 1 B 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 B 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 B 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 B 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 B 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 B 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 I 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 I 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 I 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 I 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 I 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 I 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 I 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 I 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 I 105 SER
SEQRES 1 J 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 J 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 J 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 J 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 J 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 J 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 J 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 J 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 J 105 SER
SEQRES 1 K 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 K 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 K 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 K 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 K 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 K 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 K 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 K 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 K 105 SER
SEQRES 1 L 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 L 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 L 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 L 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 L 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 L 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 M 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 M 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 M 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 M 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 M 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 M 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 N 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 N 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 N 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 N 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 N 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 N 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 Q 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 Q 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 Q 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 Q 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 Q 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 Q 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 Q 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 Q 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 Q 105 SER
SEQRES 1 R 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 R 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 R 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 R 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 R 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 R 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 R 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 R 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 R 105 SER
SEQRES 1 S 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 S 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 S 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 S 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 S 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 S 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 S 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 S 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 S 105 SER
SEQRES 1 T 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 T 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 T 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 T 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 T 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 T 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 T 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 T 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 T 105 SER
SEQRES 1 U 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 U 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 U 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 U 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 U 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 U 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 V 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 V 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 V 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 V 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 V 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 V 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 W 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 W 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 W 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 W 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 W 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 W 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 X 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 X 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 X 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 X 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 X 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 X 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
HELIX 1 1 SER C 14 ALA C 39 1 26
HELIX 2 2 SER C 43 ALA C 72 1 30
HELIX 3 3 ASN C 78 ALA C 86 1 9
HELIX 4 4 SER C 89 ALA C 106 1 18
HELIX 5 5 ARG D 11 LEU D 21 1 11
HELIX 6 6 SER D 31 GLU D 60 1 30
HELIX 7 7 ASP D 66 PHE D 81 1 16
HELIX 8 8 TYR G 15 ALA G 39 1 25
HELIX 9 9 SER G 43 ALA G 72 1 30
HELIX 10 10 ASN G 78 ALA G 86 1 9
HELIX 11 11 SER G 89 ALA G 106 1 18
HELIX 12 12 ARG H 11 LEU H 21 1 11
HELIX 13 13 SER H 31 GLU H 60 1 30
HELIX 14 14 ASP H 66 PHE H 81 1 16
HELIX 15 15 TYR A 15 ALA A 39 1 25
HELIX 16 16 SER A 43 ALA A 72 1 30
HELIX 17 17 ASN A 78 ALA A 86 1 9
HELIX 18 18 SER A 89 ALA A 106 1 18
HELIX 19 19 ARG B 11 LEU B 21 1 11
HELIX 20 20 SER B 31 GLU B 60 1 30
HELIX 21 21 ASP B 66 PHE B 81 1 16
HELIX 22 22 TYR I 15 ALA I 39 1 25
HELIX 23 23 SER I 43 ALA I 72 1 30
HELIX 24 24 ASN I 78 ALA I 86 1 9
HELIX 25 25 SER I 89 LYS I 114 1 26
HELIX 26 26 TYR J 15 ALA J 39 1 25
HELIX 27 27 SER J 43 ALA J 72 1 30
HELIX 28 28 ASN J 78 ALA J 86 1 9
HELIX 29 29 SER J 89 ALA J 106 1 18
HELIX 30 30 TYR K 15 ALA K 39 1 25
HELIX 31 31 SER K 43 ALA K 72 1 30
HELIX 32 32 ASN K 78 ALA K 86 1 9
HELIX 33 33 SER K 89 LYS K 114 1 26
HELIX 34 34 ARG L 11 LEU L 21 1 11
HELIX 35 35 SER L 31 ASP L 61 1 31
HELIX 36 36 ASP L 66 PHE L 81 1 16
HELIX 37 37 ARG M 11 LEU M 21 1 11
HELIX 38 38 SER M 31 GLU M 60 1 30
HELIX 39 39 ASP M 66 PHE M 81 1 16
HELIX 40 40 ARG N 11 LEU N 21 1 11
HELIX 41 41 SER N 31 GLU N 60 1 30
HELIX 42 42 ASP N 66 PHE N 81 1 16
HELIX 43 43 TYR Q 15 ALA Q 39 1 25
HELIX 44 44 SER Q 43 ALA Q 72 1 30
HELIX 45 45 ASN Q 78 ALA Q 86 1 9
HELIX 46 46 SER Q 89 LYS Q 114 1 26
HELIX 47 47 TYR R 15 ALA R 39 1 25
HELIX 48 48 SER R 43 ALA R 72 1 30
HELIX 49 49 ASN R 78 ALA R 86 1 9
HELIX 50 50 SER R 89 ALA R 106 1 18
HELIX 51 51 TYR S 15 ALA S 39 1 25
HELIX 52 52 SER S 43 ALA S 72 1 30
HELIX 53 53 ASN S 78 ALA S 86 1 9
HELIX 54 54 SER S 89 ALA S 106 1 18
HELIX 55 55 TYR T 15 ALA T 39 1 25
HELIX 56 56 SER T 43 ALA T 72 1 30
HELIX 57 57 ASN T 78 ALA T 86 1 9
HELIX 58 58 SER T 89 LYS T 114 1 26
HELIX 59 59 ARG U 11 LEU U 21 1 11
HELIX 60 60 SER U 31 GLU U 60 1 30
HELIX 61 61 ASP U 66 PHE U 81 1 16
HELIX 62 62 ARG V 11 LEU V 21 1 11
HELIX 63 63 SER V 31 GLU V 60 1 30
HELIX 64 64 ASP V 66 PHE V 81 1 16
HELIX 65 65 ARG W 11 LEU W 21 1 11
HELIX 66 66 SER W 31 GLU W 60 1 30
HELIX 67 67 ASP W 66 PHE W 81 1 16
HELIX 68 68 ARG X 11 LEU X 21 1 11
HELIX 69 69 SER X 31 GLU X 60 1 30
HELIX 70 70 ASP X 66 PHE X 81 1 16
SHEET 1 A 2 THR C 76 ILE C 77 0
SHEET 2 A 2 LYS D 29 VAL D 30 1 O LYS D 29 N ILE C 77
SHEET 1 B 2 THR G 76 ILE G 77 0
SHEET 2 B 2 LYS H 29 VAL H 30 1 O LYS H 29 N ILE G 77
SHEET 1 C 2 THR A 76 ILE A 77 0
SHEET 2 C 2 LYS B 29 VAL B 30 1 O LYS B 29 N ILE A 77
SHEET 1 D 2 GLN I 41 PHE I 42 0
SHEET 2 D 2 ARG M 64 VAL M 65 1 O VAL M 65 N GLN I 41
SHEET 1 E 2 THR I 76 ILE I 77 0
SHEET 2 E 2 LYS M 29 VAL M 30 1 O LYS M 29 N ILE I 77
SHEET 1 F 2 THR K 76 ILE K 77 0
SHEET 2 F 2 LYS L 29 VAL L 30 1 O LYS L 29 N ILE K 77
SHEET 1 G 2 THR Q 76 ILE Q 77 0
SHEET 2 G 2 LYS V 29 VAL V 30 1 O LYS V 29 N ILE Q 77
SHEET 1 H 2 THR R 76 ILE R 77 0
SHEET 2 H 2 LYS W 29 VAL W 30 1 O LYS W 29 N ILE R 77
SHEET 1 I 2 GLN S 41 PHE S 42 0
SHEET 2 I 2 ARG X 64 VAL X 65 1 O VAL X 65 N GLN S 41
SHEET 1 J 2 THR S 76 ILE S 77 0
SHEET 2 J 2 LYS X 29 VAL X 30 1 O LYS X 29 N ILE S 77
SHEET 1 K 2 THR T 76 ILE T 77 0
SHEET 2 K 2 LYS U 29 VAL U 30 1 O LYS U 29 N ILE T 77
CRYST1 250.098 250.098 65.561 90.00 90.00 120.00 P 3 30
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 0.003998 0.002308 0.000000 0.00000
SCALE2 0.000000 0.004617 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015253 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
