HEADER LIGASE/LIGASE INHIBITOR 20-APR-17 5VK0
TITLE CRYSTAL STRUCTURE OF HUMAN MDM2 IN COMPLEX WITH A 12-MER LYSINE-
TITLE 2 CYSTEINE SIDE CHAIN DITHIOCARBAMATE STAPLED PEPTIDE INHIBITOR PMI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2;
COMPND 3 CHAIN: A, C, E, G, I, K, M, O, Q, S, U, W;
COMPND 4 FRAGMENT: RESIDUES 25-109;
COMPND 5 SYNONYM: DOUBLE MINUTE 2 PROTEIN,HDM2,ONCOPROTEIN MDM2,RING-TYPE E3
COMPND 6 UBIQUITIN TRANSFERASE MDM2,P53-BINDING PROTEIN MDM2;
COMPND 7 EC: 2.3.2.27;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: LYSINE-CYSTEINE SIDE CHAIN DITHIOCARBAMATE STAPLED PEPTIDE
COMPND 11 INHIBITOR PMI;
COMPND 12 CHAIN: B, D, F, H, J, L, N, P, R, T, V, X;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 9 ORGANISM_TAXID: 32630
KEYWDS MDM2-PEPTIDE INHIBITOR COMPLEX, ONCOPROTEIN, HOST-VIRUS INTERACTION,
KEYWDS 2 LIGASE, METAL-BINDING, NUCLEUS, PHOSPHOPROTEIN, PROTO-ONCOGENE, UBL
KEYWDS 3 CONJUGATION PATHWAY, ZINC-FINGER, STAPLED PEPTIDE, LIGASE-LIGASE
KEYWDS 4 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.D.TOLBERT,N.GOHAIN,M.PAZGIER
REVDAT 5 04-OCT-23 5VK0 1 REMARK
REVDAT 4 11-DEC-19 5VK0 1 REMARK
REVDAT 3 13-MAR-19 5VK0 1 JRNL
REVDAT 2 30-JAN-19 5VK0 1 SOURCE JRNL
REVDAT 1 25-APR-18 5VK0 0
JRNL AUTH X.LI,W.D.TOLBERT,H.G.HU,N.GOHAIN,Y.ZOU,F.NIU,W.X.HE,W.YUAN,
JRNL AUTH 2 J.C.SU,M.PAZGIER,W.LU
JRNL TITL DITHIOCARBAMATE-INSPIRED SIDE CHAIN STAPLING CHEMISTRY FOR
JRNL TITL 2 PEPTIDE DRUG DESIGN.
JRNL REF CHEM SCI V. 10 1522 2019
JRNL REFN ISSN 2041-6520
JRNL PMID 30809370
JRNL DOI 10.1039/C8SC03275K
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 116968
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 6374
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8459
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.1850
REMARK 3 BIN FREE R VALUE SET COUNT : 517
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9689
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 418
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.80000
REMARK 3 B22 (A**2) : 5.31000
REMARK 3 B33 (A**2) : -16.11000
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): 0.028
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.029
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.755
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9948 ; 0.020 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 9777 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13252 ; 2.495 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22567 ; 1.372 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1118 ; 9.274 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 406 ;43.171 ;23.202
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1872 ;20.576 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;20.436 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1504 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10282 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2042 ; 0.004 ; 0.020
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): 4661 ; 0.976 ; 1.931
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4659 ; 0.976 ; 1.931
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5676 ; 1.348 ; 2.873
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5677 ; 1.348 ; 2.873
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5286 ; 0.848 ; 1.986
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5287 ; 0.848 ; 1.986
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7575 ; 1.184 ; 2.955
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 41030 ; 3.091 ;36.514
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 41028 ; 3.091 ;36.514
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 : 3
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.338
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : 1/2H+1/2K, 3/2H-1/2K, -L
REMARK 3 TWIN FRACTION : 0.320
REMARK 3 TWIN DOMAIN : 3
REMARK 3 TWIN OPERATOR : -1/2H+1/2K, 3/2H+1/2K, -L
REMARK 3 TWIN FRACTION : 0.343
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 : A 25 A 109
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6307 -20.1555 -27.7916
REMARK 3 T TENSOR
REMARK 3 T11: 0.0444 T22: 0.0243
REMARK 3 T33: 0.0219 T12: 0.0019
REMARK 3 T13: 0.0234 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.6328 L22: 3.3814
REMARK 3 L33: 1.1028 L12: -0.8575
REMARK 3 L13: 0.0574 L23: -0.3780
REMARK 3 S TENSOR
REMARK 3 S11: 0.0371 S12: 0.0415 S13: -0.0538
REMARK 3 S21: 0.2354 S22: 0.0102 S23: 0.2453
REMARK 3 S31: -0.0285 S32: 0.0554 S33: -0.0473
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 : C 25 C 109
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7900 19.1983 -27.8852
REMARK 3 T TENSOR
REMARK 3 T11: 0.0231 T22: 0.0147
REMARK 3 T33: 0.0047 T12: 0.0041
REMARK 3 T13: 0.0072 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.8466 L22: 3.4754
REMARK 3 L33: 1.1189 L12: -0.4677
REMARK 3 L13: -0.0771 L23: -0.2125
REMARK 3 S TENSOR
REMARK 3 S11: 0.0399 S12: 0.0594 S13: 0.0001
REMARK 3 S21: 0.2031 S22: -0.0184 S23: 0.0943
REMARK 3 S31: 0.0267 S32: 0.0780 S33: -0.0214
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 : E 26 E 108
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7361 -22.9086 -27.1111
REMARK 3 T TENSOR
REMARK 3 T11: 0.0502 T22: 0.1001
REMARK 3 T33: 0.0585 T12: 0.0121
REMARK 3 T13: -0.0062 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.4218 L22: 2.6617
REMARK 3 L33: 1.0204 L12: -0.1985
REMARK 3 L13: -0.0754 L23: 0.1338
REMARK 3 S TENSOR
REMARK 3 S11: -0.0022 S12: 0.0203 S13: -0.0100
REMARK 3 S21: 0.2022 S22: -0.0228 S23: 0.0490
REMARK 3 S31: -0.0762 S32: -0.0323 S33: 0.0250
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 : G 25 G 109
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6930 -33.2233 -60.6782
REMARK 3 T TENSOR
REMARK 3 T11: 0.0706 T22: 0.0373
REMARK 3 T33: 0.0270 T12: 0.0331
REMARK 3 T13: 0.0349 T23: 0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 2.3221 L22: 0.6929
REMARK 3 L33: 2.0374 L12: 0.2788
REMARK 3 L13: -0.4931 L23: 0.0936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0366 S12: 0.1449 S13: 0.0425
REMARK 3 S21: -0.2061 S22: -0.0956 S23: -0.1135
REMARK 3 S31: -0.1295 S32: 0.0756 S33: 0.0590
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 : I 26 I 109
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2439 6.7174 -37.9134
REMARK 3 T TENSOR
REMARK 3 T11: 0.0407 T22: 0.0153
REMARK 3 T33: 0.0354 T12: -0.0057
REMARK 3 T13: 0.0134 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 1.9429 L22: 1.9129
REMARK 3 L33: 1.8922 L12: -0.0890
REMARK 3 L13: -0.1518 L23: -0.0756
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: -0.1120 S13: 0.0946
REMARK 3 S21: 0.2402 S22: -0.0981 S23: 0.1942
REMARK 3 S31: -0.1487 S32: -0.0653 S33: 0.1220
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 : K 27 K 109
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7255 -13.2251 -4.8078
REMARK 3 T TENSOR
REMARK 3 T11: 0.0906 T22: 0.0903
REMARK 3 T33: 0.1225 T12: -0.0105
REMARK 3 T13: 0.0023 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.9462 L22: 1.4243
REMARK 3 L33: 1.5730 L12: 0.1488
REMARK 3 L13: -0.2543 L23: 0.0713
REMARK 3 S TENSOR
REMARK 3 S11: -0.0672 S12: -0.1938 S13: 0.0339
REMARK 3 S21: 0.0861 S22: 0.0460 S23: -0.0070
REMARK 3 S31: -0.0257 S32: -0.0033 S33: 0.0212
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 : M 25 M 109
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8470 -12.4535 -5.1783
REMARK 3 T TENSOR
REMARK 3 T11: 0.0773 T22: 0.0728
REMARK 3 T33: 0.0957 T12: -0.0280
REMARK 3 T13: -0.0032 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.6712 L22: 1.0095
REMARK 3 L33: 1.6043 L12: -0.2696
REMARK 3 L13: -0.3289 L23: 0.0273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0205 S12: -0.1418 S13: 0.0616
REMARK 3 S21: 0.0591 S22: -0.0204 S23: -0.0141
REMARK 3 S31: -0.0443 S32: 0.1150 S33: -0.0000
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 : O 26 O 108
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0286 -26.5527 5.8769
REMARK 3 T TENSOR
REMARK 3 T11: 0.1063 T22: 0.0934
REMARK 3 T33: 0.0878 T12: 0.0167
REMARK 3 T13: -0.0019 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.0141 L22: 1.0544
REMARK 3 L33: 1.1291 L12: 0.1670
REMARK 3 L13: 0.4649 L23: 0.3477
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.1047 S13: -0.0502
REMARK 3 S21: -0.0868 S22: 0.0291 S23: 0.0368
REMARK 3 S31: -0.0752 S32: -0.0455 S33: -0.0246
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 : Q 26 Q 108
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9104 -35.4843 -38.8081
REMARK 3 T TENSOR
REMARK 3 T11: 0.0452 T22: 0.0157
REMARK 3 T33: 0.0128 T12: 0.0042
REMARK 3 T13: 0.0206 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 2.3716 L22: 1.0573
REMARK 3 L33: 1.8551 L12: -0.3921
REMARK 3 L13: -0.6671 L23: -0.1313
REMARK 3 S TENSOR
REMARK 3 S11: -0.0368 S12: -0.1819 S13: -0.1009
REMARK 3 S21: 0.2110 S22: 0.0273 S23: 0.1084
REMARK 3 S31: 0.0220 S32: 0.1041 S33: 0.0094
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 : S 25 S 109
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4170 -62.8870 -26.6420
REMARK 3 T TENSOR
REMARK 3 T11: 0.0225 T22: 0.0596
REMARK 3 T33: 0.0614 T12: 0.0152
REMARK 3 T13: 0.0049 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.0772 L22: 3.0328
REMARK 3 L33: 1.3374 L12: -0.2099
REMARK 3 L13: -0.0620 L23: -0.0303
REMARK 3 S TENSOR
REMARK 3 S11: -0.0287 S12: 0.0484 S13: -0.0266
REMARK 3 S21: 0.1365 S22: 0.0387 S23: 0.0935
REMARK 3 S31: -0.0451 S32: -0.0623 S33: -0.0100
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 : U 25 U 108
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0818 -52.3736 -5.9983
REMARK 3 T TENSOR
REMARK 3 T11: 0.1135 T22: 0.0999
REMARK 3 T33: 0.1198 T12: -0.0256
REMARK 3 T13: 0.0059 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 1.3724 L22: 1.2111
REMARK 3 L33: 1.0098 L12: -0.7227
REMARK 3 L13: -0.1047 L23: -0.1157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: -0.1654 S13: 0.0011
REMARK 3 S21: 0.1633 S22: 0.0192 S23: 0.1156
REMARK 3 S31: 0.0171 S32: -0.0472 S33: -0.0104
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 : W 25 W 108
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6271 2.7405 -38.6800
REMARK 3 T TENSOR
REMARK 3 T11: 0.0502 T22: 0.0300
REMARK 3 T33: 0.0211 T12: -0.0079
REMARK 3 T13: 0.0213 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 2.6103 L22: 1.3953
REMARK 3 L33: 2.2447 L12: 0.0618
REMARK 3 L13: -0.1045 L23: -0.3519
REMARK 3 S TENSOR
REMARK 3 S11: 0.0123 S12: -0.2350 S13: 0.0773
REMARK 3 S21: 0.2639 S22: -0.0380 S23: 0.1035
REMARK 3 S31: -0.0591 S32: -0.1134 S33: 0.0258
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5VK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226506.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123372
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.29900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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: 3EQS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1340 MM AMMONIUM SULFATE, 6.7%
REMARK 280 GLYCEROL, 50 MM MAGNESIUM SULFATE, 100 MM IMIDAZOLE PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 98.32500
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 98.32500
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 45.41900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 78.73500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.41900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 78.73500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 98.32500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.41900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 78.73500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 98.32500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.41900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 78.73500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T
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: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V
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: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, 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 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 GLU E 25
REMARK 465 VAL E 109
REMARK 465 GLU O 25
REMARK 465 VAL O 109
REMARK 465 GLU Q 25
REMARK 465 VAL Q 109
REMARK 465 VAL U 109
REMARK 465 VAL W 109
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O CYS L 12 N NH2 L 13 1.79
REMARK 500 O CYS N 12 N NH2 N 13 1.80
REMARK 500 O LYS U 94 ND1 HIS U 96 1.89
REMARK 500 O MET U 102 ND2 ASN U 106 1.95
REMARK 500 NH2 ARG U 105 O HOH U 201 1.97
REMARK 500 OH TYR S 60 OD1 ASP S 80 2.03
REMARK 500 SG CYS U 77 O HOH U 211 2.06
REMARK 500 OE1 GLN O 59 OG1 THR O 63 2.13
REMARK 500 OG1 THR L 1 O HOH L 101 2.14
REMARK 500 OH TYR Q 48 O HOH Q 201 2.15
REMARK 500 O ILE M 74 O HOH M 201 2.16
REMARK 500 O HOH X 206 O HOH X 208 2.16
REMARK 500 NH1 ARG Q 105 O HOH Q 202 2.18
REMARK 500 OG SER T 2 NE2 GLN U 59 2.19
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 OG SER K 78 ND1 HIS U 96 8545 2.12
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 LEU A 85 CA - CB - CG ANGL. DEV. = 17.5 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ACE B 0 O - C - N ANGL. DEV. = -18.8 DEGREES
REMARK 500 9E7 B 8 O - C - N ANGL. DEV. = -24.3 DEGREES
REMARK 500 CYS B 12 O - C - N ANGL. DEV. = -11.4 DEGREES
REMARK 500 ASP C 68 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 VAL C 109 CA - C - O ANGL. DEV. = -14.7 DEGREES
REMARK 500 ACE D 0 O - C - N ANGL. DEV. = -24.7 DEGREES
REMARK 500 THR D 1 C - N - CA ANGL. DEV. = 43.8 DEGREES
REMARK 500 TRP D 7 O - C - N ANGL. DEV. = -12.6 DEGREES
REMARK 500 9E7 D 8 O - C - N ANGL. DEV. = -23.2 DEGREES
REMARK 500 LEU D 9 C - N - CA ANGL. DEV. = 16.4 DEGREES
REMARK 500 CYS D 12 CA - C - N ANGL. DEV. = 20.8 DEGREES
REMARK 500 CYS D 12 O - C - N ANGL. DEV. = -29.8 DEGREES
REMARK 500 PRO E 89 C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500 ACE F 0 O - C - N ANGL. DEV. = -30.5 DEGREES
REMARK 500 THR F 1 C - N - CA ANGL. DEV. = 31.1 DEGREES
REMARK 500 TRP F 7 CA - C - N ANGL. DEV. = 13.2 DEGREES
REMARK 500 TRP F 7 O - C - N ANGL. DEV. = -13.0 DEGREES
REMARK 500 9E7 F 8 C - N - CA ANGL. DEV. = 21.4 DEGREES
REMARK 500 9E7 F 8 O - C - N ANGL. DEV. = -12.5 DEGREES
REMARK 500 CYS F 12 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 CYS G 77 CA - CB - SG ANGL. DEV. = 9.4 DEGREES
REMARK 500 ACE H 0 O - C - N ANGL. DEV. = -25.5 DEGREES
REMARK 500 CYS H 12 O - C - N ANGL. DEV. = -14.6 DEGREES
REMARK 500 ACE J 0 O - C - N ANGL. DEV. = -19.0 DEGREES
REMARK 500 9E7 J 8 O - C - N ANGL. DEV. = -15.2 DEGREES
REMARK 500 CYS J 12 CA - C - N ANGL. DEV. = 26.8 DEGREES
REMARK 500 CYS J 12 O - C - N ANGL. DEV. = -26.9 DEGREES
REMARK 500 GLN K 71 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 ASP K 84 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 PRO K 89 C - N - CA ANGL. DEV. = 14.7 DEGREES
REMARK 500 ACE L 0 O - C - N ANGL. DEV. = -12.3 DEGREES
REMARK 500 TRP L 7 O - C - N ANGL. DEV. = -22.8 DEGREES
REMARK 500 CYS L 12 CA - C - N ANGL. DEV. = 13.3 DEGREES
REMARK 500 CYS L 12 O - C - N ANGL. DEV. = -31.1 DEGREES
REMARK 500 PRO M 32 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG M 105 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ACE N 0 O - C - N ANGL. DEV. = -26.2 DEGREES
REMARK 500 THR N 1 C - N - CA ANGL. DEV. = 27.6 DEGREES
REMARK 500 CYS N 12 CA - C - N ANGL. DEV. = 27.7 DEGREES
REMARK 500 CYS N 12 O - C - N ANGL. DEV. = -32.6 DEGREES
REMARK 500 ASP O 46 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 CYS O 77 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 ACE P 0 O - C - N ANGL. DEV. = -13.0 DEGREES
REMARK 500 THR P 1 C - N - CA ANGL. DEV. = 33.2 DEGREES
REMARK 500 TRP P 7 CA - C - N ANGL. DEV. = 21.2 DEGREES
REMARK 500 TRP P 7 O - C - N ANGL. DEV. = -21.1 DEGREES
REMARK 500 9E7 P 8 C - N - CA ANGL. DEV. = 31.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 77 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 26 105.16 18.44
REMARK 500 ARG A 65 60.25 30.95
REMARK 500 ALA B 4 -59.26 -29.87
REMARK 500 SER B 11 -148.20 -65.53
REMARK 500 SER D 11 -78.85 -124.72
REMARK 500 ARG E 65 77.33 48.86
REMARK 500 GLN E 71 79.17 -106.29
REMARK 500 CYS E 77 29.79 -155.33
REMARK 500 LEU E 107 -113.17 -134.83
REMARK 500 LEU G 81 -33.64 -39.09
REMARK 500 THR I 26 144.20 179.62
REMARK 500 GLN I 44 -3.30 -141.69
REMARK 500 SER J 11 -73.00 -112.97
REMARK 500 PRO K 32 -77.32 -31.50
REMARK 500 ALA K 43 97.42 -55.52
REMARK 500 GLN K 44 29.22 -76.55
REMARK 500 ARG K 65 49.57 73.83
REMARK 500 GLN K 72 43.92 -154.21
REMARK 500 PRO K 89 -15.21 -30.82
REMARK 500 VAL K 93 -8.84 -57.49
REMARK 500 LEU L 10 -24.07 -34.16
REMARK 500 SER L 11 -100.70 -172.76
REMARK 500 PRO M 32 -95.28 -29.70
REMARK 500 ALA M 43 129.79 -14.08
REMARK 500 SER M 78 154.46 -48.26
REMARK 500 GLU M 95 75.50 -102.34
REMARK 500 LEU O 27 135.47 82.63
REMARK 500 ALA O 43 140.15 137.27
REMARK 500 GLN O 44 21.07 -145.59
REMARK 500 ARG O 65 42.63 75.88
REMARK 500 CYS O 77 33.47 -157.62
REMARK 500 ASP O 84 -61.92 -18.93
REMARK 500 GLU O 95 59.60 -106.12
REMARK 500 ARG O 97 -95.31 -27.66
REMARK 500 ILE O 99 -70.12 -63.78
REMARK 500 LEU P 9 36.70 -45.91
REMARK 500 LEU P 10 49.93 -174.35
REMARK 500 SER P 11 -142.52 175.95
REMARK 500 CYS Q 77 19.09 -142.75
REMARK 500 GLN S 44 12.67 -142.25
REMARK 500 PHE S 55 -42.51 -158.22
REMARK 500 ARG S 65 15.39 85.02
REMARK 500 SER S 78 112.44 -28.41
REMARK 500 ASN S 79 -9.70 79.10
REMARK 500 LEU S 81 -48.68 -19.44
REMARK 500 GLU S 95 60.37 -103.35
REMARK 500 VAL S 108 -136.72 -87.78
REMARK 500 ARG U 65 66.10 7.91
REMARK 500 ASP U 68 -147.29 -105.51
REMARK 500 GLU U 69 -54.10 -147.71
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER D 11 CYS D 12 -128.38
REMARK 500 PRO K 89 SER K 90 145.18
REMARK 500 9E7 P 8 LEU P 9 125.79
REMARK 500 LEU Q 107 VAL Q 108 126.00
REMARK 500 GLN U 44 LYS U 45 -148.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 9E7 B 8 -34.86
REMARK 500 TRP D 7 -11.83
REMARK 500 9E7 D 8 -35.37
REMARK 500 9E7 F 8 -25.76
REMARK 500 9E7 H 8 -22.00
REMARK 500 9E7 J 8 -29.31
REMARK 500 TRP L 7 -31.76
REMARK 500 9E7 L 8 -24.83
REMARK 500 9E7 N 8 -19.34
REMARK 500 9E7 P 8 -27.29
REMARK 500 TRP R 7 12.21
REMARK 500 9E7 R 8 -24.02
REMARK 500 9E7 T 8 -39.69
REMARK 500 9E7 V 8 -20.59
REMARK 500 9E7 X 8 -15.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH K 224 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH K 225 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH M 242 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH U 238 DISTANCE = 5.90 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL X 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EQS RELATED DB: PDB
REMARK 900 3EQS CONTAINS SAME MDM2 PROTEIN WITH UNSTAPLED PMI PEPTIDE.
REMARK 900 RELATED ID: 5VK1 RELATED DB: PDB
DBREF 5VK0 A 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 B 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 C 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 D 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 E 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 F 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 G 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 H 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 I 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 J 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 K 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 L 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 M 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 N 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 O 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 P 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 Q 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 R 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 S 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 T 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 U 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 V 0 13 PDB 5VK0 5VK0 0 13
DBREF 5VK0 W 25 109 UNP Q00987 MDM2_HUMAN 25 109
DBREF 5VK0 X 0 13 PDB 5VK0 5VK0 0 13
SEQRES 1 A 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 A 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 A 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 A 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 A 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 A 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 A 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 B 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 B 14 NH2
SEQRES 1 C 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 C 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 C 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 C 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 C 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 C 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 C 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 D 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 D 14 NH2
SEQRES 1 E 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 E 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 E 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 E 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 E 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 E 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 E 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 F 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 F 14 NH2
SEQRES 1 G 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 G 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 G 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 G 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 G 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 G 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 G 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 H 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 H 14 NH2
SEQRES 1 I 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 I 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 I 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 I 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 I 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 I 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 I 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 J 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 J 14 NH2
SEQRES 1 K 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 K 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 K 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 K 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 K 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 K 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 K 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 L 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 L 14 NH2
SEQRES 1 M 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 M 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 M 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 M 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 M 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 M 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 M 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 N 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 N 14 NH2
SEQRES 1 O 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 O 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 O 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 O 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 O 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 O 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 O 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 P 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 P 14 NH2
SEQRES 1 Q 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 Q 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 Q 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 Q 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 Q 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 Q 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 Q 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 R 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 R 14 NH2
SEQRES 1 S 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 S 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 S 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 S 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 S 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 S 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 S 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 T 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 T 14 NH2
SEQRES 1 U 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 U 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 U 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 U 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 U 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 U 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 U 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 V 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 V 14 NH2
SEQRES 1 W 85 GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU
SEQRES 2 W 85 LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET
SEQRES 3 W 85 LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR
SEQRES 4 W 85 LYS ARG LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR
SEQRES 5 W 85 CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO
SEQRES 6 W 85 SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET
SEQRES 7 W 85 ILE TYR ARG ASN LEU VAL VAL
SEQRES 1 X 14 ACE THR SER PHE ALA GLU TYR TRP 9E7 LEU LEU SER CYS
SEQRES 2 X 14 NH2
HET ACE B 0 3
HET 9E7 B 8 11
HET NH2 B 13 1
HET ACE D 0 3
HET 9E7 D 8 11
HET NH2 D 13 1
HET ACE F 0 3
HET 9E7 F 8 11
HET NH2 F 13 1
HET ACE H 0 3
HET 9E7 H 8 11
HET NH2 H 13 1
HET ACE J 0 3
HET 9E7 J 8 11
HET NH2 J 13 1
HET ACE L 0 3
HET 9E7 L 8 11
HET NH2 L 13 1
HET ACE N 0 3
HET 9E7 N 8 11
HET NH2 N 13 1
HET ACE P 0 3
HET 9E7 P 8 11
HET NH2 P 13 1
HET ACE R 0 3
HET 9E7 R 8 11
HET NH2 R 13 1
HET ACE T 0 3
HET 9E7 T 8 11
HET NH2 T 13 1
HET ACE V 0 3
HET 9E7 V 8 11
HET NH2 V 13 1
HET ACE X 0 3
HET 9E7 X 8 11
HET NH2 X 13 1
HET CL C 201 1
HET CL X 101 1
HETNAM ACE ACETYL GROUP
HETNAM 9E7 N~6~-(SULFANYLMETHYL)-L-LYSINE
HETNAM NH2 AMINO GROUP
HETNAM CL CHLORIDE ION
FORMUL 2 ACE 12(C2 H4 O)
FORMUL 2 9E7 12(C7 H16 N2 O2 S)
FORMUL 2 NH2 12(H2 N)
FORMUL 25 CL 2(CL 1-)
FORMUL 27 HOH *418(H2 O)
HELIX 1 AA1 LYS A 31 VAL A 41 1 11
HELIX 2 AA2 THR A 49 ARG A 65 1 17
HELIX 3 AA3 ASP A 80 GLY A 87 1 8
HELIX 4 AA4 GLU A 95 ASN A 106 1 12
HELIX 5 AA5 SER B 2 SER B 11 1 10
HELIX 6 AA6 LYS C 31 SER C 40 1 10
HELIX 7 AA7 THR C 49 ARG C 65 1 17
HELIX 8 AA8 ASP C 80 GLY C 87 1 8
HELIX 9 AA9 GLU C 95 ASN C 106 1 12
HELIX 10 AB1 SER D 2 LEU D 10 1 9
HELIX 11 AB2 LYS E 31 VAL E 41 1 11
HELIX 12 AB3 THR E 49 LYS E 64 1 16
HELIX 13 AB4 ASP E 80 GLY E 87 1 8
HELIX 14 AB5 GLU E 95 ASN E 106 1 12
HELIX 15 AB6 SER F 2 CYS F 12 1 11
HELIX 16 AB7 LYS G 31 VAL G 41 1 11
HELIX 17 AB8 THR G 49 LYS G 64 1 16
HELIX 18 AB9 ASP G 80 GLY G 87 1 8
HELIX 19 AC1 GLU G 95 ARG G 105 1 11
HELIX 20 AC2 SER H 2 CYS H 12 1 11
HELIX 21 AC3 LYS I 31 VAL I 41 1 11
HELIX 22 AC4 THR I 49 LYS I 64 1 16
HELIX 23 AC5 ASP I 80 GLY I 87 1 8
HELIX 24 AC6 GLU I 95 ASN I 106 1 12
HELIX 25 AC7 SER J 2 CYS J 12 1 11
HELIX 26 AC8 LYS K 31 VAL K 41 1 11
HELIX 27 AC9 THR K 49 ARG K 65 1 17
HELIX 28 AD1 ASP K 80 GLY K 87 1 8
HELIX 29 AD2 GLU K 95 ASN K 106 1 12
HELIX 30 AD3 SER L 2 LEU L 10 1 9
HELIX 31 AD4 LYS M 31 SER M 40 1 10
HELIX 32 AD5 THR M 49 LYS M 64 1 16
HELIX 33 AD6 ASP M 80 GLY M 87 1 8
HELIX 34 AD7 GLU M 95 ASN M 106 1 12
HELIX 35 AD8 SER N 2 SER N 11 1 10
HELIX 36 AD9 LYS O 31 SER O 40 1 10
HELIX 37 AE1 THR O 49 ARG O 65 1 17
HELIX 38 AE2 ASP O 80 GLY O 87 1 8
HELIX 39 AE3 GLU O 95 ASN O 106 1 12
HELIX 40 AE4 SER P 2 LEU P 9 1 8
HELIX 41 AE5 LYS Q 31 SER Q 40 1 10
HELIX 42 AE6 THR Q 49 LYS Q 64 1 16
HELIX 43 AE7 ASP Q 80 GLY Q 87 1 8
HELIX 44 AE8 GLU Q 95 ARG Q 105 1 11
HELIX 45 AE9 SER R 2 CYS R 12 1 11
HELIX 46 AF1 LYS S 31 VAL S 41 1 11
HELIX 47 AF2 MET S 50 LYS S 64 1 15
HELIX 48 AF3 ASP S 80 GLY S 87 1 8
HELIX 49 AF4 GLU S 95 ASN S 106 1 12
HELIX 50 AF5 SER T 2 LEU T 10 1 9
HELIX 51 AF6 LYS U 31 VAL U 41 1 11
HELIX 52 AF7 THR U 49 LYS U 64 1 16
HELIX 53 AF8 ASP U 80 GLY U 87 1 8
HELIX 54 AF9 ARG U 97 ARG U 105 1 9
HELIX 55 AG1 SER V 2 SER V 11 1 10
HELIX 56 AG2 LYS W 31 VAL W 41 1 11
HELIX 57 AG3 MET W 50 LYS W 64 1 15
HELIX 58 AG4 LEU W 81 GLY W 87 1 7
HELIX 59 AG5 GLU W 95 ARG W 105 1 11
HELIX 60 AG6 SER X 2 CYS X 12 1 11
SHEET 1 AA1 2 ARG A 29 PRO A 30 0
SHEET 2 AA1 2 LEU A 107 VAL A 108 -1 O VAL A 108 N ARG A 29
SHEET 1 AA2 2 ILE A 74 TYR A 76 0
SHEET 2 AA2 2 SER A 90 SER A 92 -1 O PHE A 91 N VAL A 75
SHEET 1 AA3 2 ARG C 29 PRO C 30 0
SHEET 2 AA3 2 LEU C 107 VAL C 108 -1 O VAL C 108 N ARG C 29
SHEET 1 AA4 2 ILE C 74 TYR C 76 0
SHEET 2 AA4 2 SER C 90 SER C 92 -1 O PHE C 91 N VAL C 75
SHEET 1 AA5 2 ILE E 74 TYR E 76 0
SHEET 2 AA5 2 SER E 90 SER E 92 -1 O PHE E 91 N VAL E 75
SHEET 1 AA6 2 ARG G 29 PRO G 30 0
SHEET 2 AA6 2 LEU G 107 VAL G 108 -1 O VAL G 108 N ARG G 29
SHEET 1 AA7 2 ILE G 74 TYR G 76 0
SHEET 2 AA7 2 SER G 90 SER G 92 -1 O PHE G 91 N VAL G 75
SHEET 1 AA8 2 ARG I 29 PRO I 30 0
SHEET 2 AA8 2 LEU I 107 VAL I 108 -1 O VAL I 108 N ARG I 29
SHEET 1 AA9 2 ILE I 74 TYR I 76 0
SHEET 2 AA9 2 SER I 90 SER I 92 -1 O PHE I 91 N VAL I 75
SHEET 1 AB1 2 ILE K 74 TYR K 76 0
SHEET 2 AB1 2 SER K 90 SER K 92 -1 O PHE K 91 N VAL K 75
SHEET 1 AB2 2 ARG M 29 PRO M 30 0
SHEET 2 AB2 2 LEU M 107 VAL M 108 -1 O VAL M 108 N ARG M 29
SHEET 1 AB3 2 ILE M 74 TYR M 76 0
SHEET 2 AB3 2 SER M 90 SER M 92 -1 O PHE M 91 N VAL M 75
SHEET 1 AB4 2 ILE O 74 TYR O 76 0
SHEET 2 AB4 2 SER O 90 SER O 92 -1 O PHE O 91 N VAL O 75
SHEET 1 AB5 2 ARG Q 29 PRO Q 30 0
SHEET 2 AB5 2 LEU Q 107 VAL Q 108 -1 O VAL Q 108 N ARG Q 29
SHEET 1 AB6 2 ILE Q 74 TYR Q 76 0
SHEET 2 AB6 2 SER Q 90 SER Q 92 -1 O PHE Q 91 N VAL Q 75
SHEET 1 AB7 2 LEU S 27 VAL S 28 0
SHEET 2 AB7 2 TYR S 48 THR S 49 -1 O TYR S 48 N VAL S 28
SHEET 1 AB8 2 ILE S 74 TYR S 76 0
SHEET 2 AB8 2 SER S 90 SER S 92 -1 O PHE S 91 N VAL S 75
SHEET 1 AB9 2 ILE U 74 TYR U 76 0
SHEET 2 AB9 2 SER U 90 SER U 92 -1 O PHE U 91 N VAL U 75
SHEET 1 AC1 2 LEU W 27 VAL W 28 0
SHEET 2 AC1 2 TYR W 48 THR W 49 -1 O TYR W 48 N VAL W 28
SHEET 1 AC2 2 ILE W 74 TYR W 76 0
SHEET 2 AC2 2 SER W 90 SER W 92 -1 O PHE W 91 N VAL W 75
LINK C ACE B 0 N THR B 1 1555 1555 1.32
LINK C TRP B 7 N 9E7 B 8 1555 1555 1.31
LINK C 9E7 B 8 N LEU B 9 1555 1555 1.32
LINK C1 9E7 B 8 SG CYS B 12 1555 1555 1.62
LINK C CYS B 12 N NH2 B 13 1555 1555 1.27
LINK C ACE D 0 N THR D 1 1555 1555 1.33
LINK C TRP D 7 N 9E7 D 8 1555 1555 1.27
LINK C 9E7 D 8 N LEU D 9 1555 1555 1.32
LINK C1 9E7 D 8 SG CYS D 12 1555 1555 1.61
LINK C CYS D 12 N NH2 D 13 1555 1555 1.29
LINK C ACE F 0 N THR F 1 1555 1555 1.33
LINK C TRP F 7 N 9E7 F 8 1555 1555 1.29
LINK C 9E7 F 8 N LEU F 9 1555 1555 1.35
LINK C1 9E7 F 8 SG CYS F 12 1555 1555 1.64
LINK C CYS F 12 N NH2 F 13 1555 1555 1.29
LINK C ACE H 0 N THR H 1 1555 1555 1.32
LINK C TRP H 7 N 9E7 H 8 1555 1555 1.27
LINK C 9E7 H 8 N LEU H 9 1555 1555 1.32
LINK C1 9E7 H 8 SG CYS H 12 1555 1555 1.64
LINK C CYS H 12 N NH2 H 13 1555 1555 1.29
LINK C ACE J 0 N THR J 1 1555 1555 1.31
LINK C TRP J 7 N 9E7 J 8 1555 1555 1.27
LINK C 9E7 J 8 N LEU J 9 1555 1555 1.31
LINK C1 9E7 J 8 SG CYS J 12 1555 1555 1.62
LINK C CYS J 12 N NH2 J 13 1555 1555 1.28
LINK C ACE L 0 N THR L 1 1555 1555 1.32
LINK C TRP L 7 N 9E7 L 8 1555 1555 1.33
LINK C 9E7 L 8 N LEU L 9 1555 1555 1.34
LINK C1 9E7 L 8 SG CYS L 12 1555 1555 1.61
LINK C CYS L 12 N NH2 L 13 1555 1555 1.28
LINK C ACE N 0 N THR N 1 1555 1555 1.32
LINK C TRP N 7 N 9E7 N 8 1555 1555 1.29
LINK C 9E7 N 8 N LEU N 9 1555 1555 1.35
LINK C1 9E7 N 8 SG CYS N 12 1555 1555 1.66
LINK C CYS N 12 N NH2 N 13 1555 1555 1.28
LINK C ACE P 0 N THR P 1 1555 1555 1.34
LINK C TRP P 7 N 9E7 P 8 1555 1555 1.26
LINK C 9E7 P 8 N LEU P 9 1555 1555 1.34
LINK C1 9E7 P 8 SG CYS P 12 1555 1555 1.65
LINK C CYS P 12 N NH2 P 13 1555 1555 1.26
LINK C ACE R 0 N THR R 1 1555 1555 1.33
LINK C TRP R 7 N 9E7 R 8 1555 1555 1.24
LINK C 9E7 R 8 N LEU R 9 1555 1555 1.33
LINK C1 9E7 R 8 SG CYS R 12 1555 1555 1.69
LINK C CYS R 12 N NH2 R 13 1555 1555 1.28
LINK C ACE T 0 N THR T 1 1555 1555 1.30
LINK C TRP T 7 N 9E7 T 8 1555 1555 1.31
LINK C 9E7 T 8 N LEU T 9 1555 1555 1.32
LINK C1 9E7 T 8 SG CYS T 12 1555 1555 1.63
LINK C CYS T 12 N NH2 T 13 1555 1555 1.27
LINK C ACE V 0 N THR V 1 1555 1555 1.33
LINK C TRP V 7 N 9E7 V 8 1555 1555 1.27
LINK C 9E7 V 8 N LEU V 9 1555 1555 1.35
LINK C1 9E7 V 8 SG CYS V 12 1555 1555 1.67
LINK C CYS V 12 N NH2 V 13 1555 1555 1.29
LINK C ACE X 0 N THR X 1 1555 1555 1.33
LINK C TRP X 7 N 9E7 X 8 1555 1555 1.28
LINK C 9E7 X 8 N LEU X 9 1555 1555 1.35
LINK C1 9E7 X 8 SG CYS X 12 1555 1555 1.67
LINK C CYS X 12 N NH2 X 13 1555 1555 1.29
SITE 1 AC1 1 LEU C 33
SITE 1 AC2 1 SER X 11
CRYST1 90.838 157.470 196.650 90.00 90.00 90.00 C 2 2 21 96
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 0.011009 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006350 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005085 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
