HEADER OXIDOREDUCTASE 01-JUN-12 4FFU
TITLE CRYSTAL STRUCTURE OF PUTATIVE MAOC-LIKE (MONOAMINE OXIDASE-LIKE)
TITLE 2 PROTEIN, SIMILAR TO NODN FROM SINORHIZO BIUM MELILOTI 1021
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXIDASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: PUTATIVE MAOC-LIKE (MONOAMINE OXIDASE-LIKE) PROTEIN, SIMILAR
COMPND 5 TO NODN;
COMPND 6 EC: 1.4.3.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI;
SOURCE 3 ORGANISM_COMMON: ENSIFER MELILOTI;
SOURCE 4 ORGANISM_TAXID: 266834;
SOURCE 5 STRAIN: 1021;
SOURCE 6 GENE: RB0689, SM_B21110;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NEW YORK
KEYWDS 2 STRUCTURAL GENOMIX RESEARCH CONSORTIUM, NYSGRC, OXIDASE, PSI-
KEYWDS 3 BIOLOGY, NEW YORK STRUCTURAL GENOMICS RESEARCH CONSORTIUM,
KEYWDS 4 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.N.MALASHKEVICH,R.BHOSLE,R.TORO,B.HILLERICH,A.GIZZI,S.GARFORTH,
AUTHOR 2 A.KAR,M.K.CHAN,J.LAFLUER,H.PATEL,B.MATIKAINEN,S.CHAMALA,S.LIM,
AUTHOR 3 A.CELIKGIL,G.VILLEGAS,B.EVANS,W.ZENCHEK,J.LOVE,A.FISER,K.KHAFIZOV,
AUTHOR 4 R.SEIDEL,J.B.BONANNO,S.C.ALMO,NEW YORK STRUCTURAL GENOMICS RESEARCH
AUTHOR 5 CONSORTIUM (NYSGRC)
REVDAT 3 06-DEC-23 4FFU 1 REMARK
REVDAT 2 13-SEP-23 4FFU 1 REMARK SEQADV LINK
REVDAT 1 13-JUN-12 4FFU 0
JRNL AUTH V.N.MALASHKEVICH,R.BHOSLE,R.TORO,B.HILLERICH,A.GIZZI,
JRNL AUTH 2 S.GARFORTH,A.KAR,M.K.CHAN,J.LAFLUER,H.PATEL,B.MATIKAINEN,
JRNL AUTH 3 S.CHAMALA,S.LIM,A.CELIKGIL,G.VILLEGAS,B.EVANS,W.ZENCHEK,
JRNL AUTH 4 J.LOVE,A.FISER,K.KHAFIZOV,R.SEIDEL,J.B.BONANNO,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE MAOC-LIKE (MONOAMINE
JRNL TITL 2 OXIDASE-LIKE) PROTEIN, SIMILAR TO NODN FROM SINORHIZO BIUM
JRNL TITL 3 MELILOTI 1021
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 194753
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9811
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) : 13398
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 682
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14074
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 1829
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.02000
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): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.054
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14741 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20041 ; 1.325 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1872 ; 5.812 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 729 ;30.523 ;22.085
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2286 ;12.901 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 163 ;17.915 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2215 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11486 ; 0.006 ; 0.021
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 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 -6 A 148
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4892 39.9376 38.8704
REMARK 3 T TENSOR
REMARK 3 T11: 0.0178 T22: 0.0301
REMARK 3 T33: 0.0377 T12: 0.0054
REMARK 3 T13: -0.0200 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 0.0853 L22: 0.6357
REMARK 3 L33: 0.2388 L12: -0.2132
REMARK 3 L13: -0.0440 L23: 0.1762
REMARK 3 S TENSOR
REMARK 3 S11: 0.0166 S12: 0.0218 S13: -0.0247
REMARK 3 S21: -0.0310 S22: -0.0065 S23: 0.0153
REMARK 3 S31: -0.0064 S32: -0.0021 S33: -0.0102
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 : B -1 B 148
REMARK 3 ORIGIN FOR THE GROUP (A): 54.5973 81.5702 36.9871
REMARK 3 T TENSOR
REMARK 3 T11: 0.0488 T22: 0.0413
REMARK 3 T33: 0.0190 T12: 0.0167
REMARK 3 T13: 0.0249 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.1701 L22: 1.0970
REMARK 3 L33: 0.2880 L12: -0.2898
REMARK 3 L13: 0.2026 L23: -0.5130
REMARK 3 S TENSOR
REMARK 3 S11: 0.0016 S12: 0.0571 S13: 0.0164
REMARK 3 S21: -0.0276 S22: -0.0043 S23: 0.0187
REMARK 3 S31: 0.0114 S32: 0.0410 S33: 0.0027
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 : C 4 C 153
REMARK 3 ORIGIN FOR THE GROUP (A): 53.7199 46.2978 53.1802
REMARK 3 T TENSOR
REMARK 3 T11: 0.0133 T22: 0.0474
REMARK 3 T33: 0.0323 T12: 0.0055
REMARK 3 T13: -0.0038 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.7275 L22: 0.2075
REMARK 3 L33: 0.0809 L12: 0.0218
REMARK 3 L13: 0.0402 L23: -0.0288
REMARK 3 S TENSOR
REMARK 3 S11: 0.0129 S12: 0.0145 S13: -0.1237
REMARK 3 S21: -0.0504 S22: -0.0077 S23: 0.0073
REMARK 3 S31: 0.0030 S32: -0.0557 S33: -0.0052
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 : D 3 D 149
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0171 76.6873 52.0379
REMARK 3 T TENSOR
REMARK 3 T11: 0.0076 T22: 0.0198
REMARK 3 T33: 0.0220 T12: -0.0111
REMARK 3 T13: -0.0064 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.6396 L22: 0.5588
REMARK 3 L33: 0.2956 L12: 0.1632
REMARK 3 L13: -0.0875 L23: -0.0952
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: -0.0085 S13: 0.0733
REMARK 3 S21: -0.0145 S22: -0.0119 S23: -0.0375
REMARK 3 S31: -0.0349 S32: 0.0721 S33: 0.0218
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 : E 3 E 153
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6104 52.1975 38.0989
REMARK 3 T TENSOR
REMARK 3 T11: 0.0241 T22: 0.0512
REMARK 3 T33: 0.0242 T12: -0.0205
REMARK 3 T13: 0.0088 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.1295 L22: 0.4266
REMARK 3 L33: 0.5664 L12: -0.0839
REMARK 3 L13: 0.0448 L23: 0.0012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: 0.0361 S13: -0.0279
REMARK 3 S21: -0.0707 S22: 0.0208 S23: -0.0420
REMARK 3 S31: -0.0692 S32: 0.1197 S33: -0.0217
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 : F 3 F 147
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2420 49.0887 69.2728
REMARK 3 T TENSOR
REMARK 3 T11: 0.0277 T22: 0.0531
REMARK 3 T33: 0.0200 T12: 0.0243
REMARK 3 T13: 0.0096 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.7298 L22: 0.6696
REMARK 3 L33: 0.7631 L12: -0.1553
REMARK 3 L13: -0.0808 L23: -0.0802
REMARK 3 S TENSOR
REMARK 3 S11: -0.0468 S12: -0.1418 S13: -0.0485
REMARK 3 S21: 0.1233 S22: 0.0854 S23: 0.0764
REMARK 3 S31: -0.0235 S32: -0.0346 S33: -0.0386
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 3 G 147
REMARK 3 ORIGIN FOR THE GROUP (A): 74.4106 74.6571 68.6139
REMARK 3 T TENSOR
REMARK 3 T11: 0.0525 T22: 0.0341
REMARK 3 T33: 0.0482 T12: 0.0266
REMARK 3 T13: -0.0302 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 0.7855 L22: 0.9514
REMARK 3 L33: 0.7652 L12: -0.3521
REMARK 3 L13: 0.3094 L23: -0.1978
REMARK 3 S TENSOR
REMARK 3 S11: -0.1011 S12: -0.1220 S13: 0.1100
REMARK 3 S21: 0.1965 S22: 0.0958 S23: -0.1857
REMARK 3 S31: -0.1108 S32: -0.0159 S33: 0.0052
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 -7 H 148
REMARK 3 ORIGIN FOR THE GROUP (A): 58.0289 51.4466 67.9719
REMARK 3 T TENSOR
REMARK 3 T11: 0.0162 T22: 0.0386
REMARK 3 T33: 0.0229 T12: 0.0060
REMARK 3 T13: 0.0058 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 0.2242 L22: 0.6160
REMARK 3 L33: 0.2243 L12: -0.0673
REMARK 3 L13: -0.1916 L23: -0.1003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0133 S12: -0.0221 S13: -0.0486
REMARK 3 S21: 0.0943 S22: -0.0119 S23: 0.0120
REMARK 3 S31: -0.0198 S32: -0.0027 S33: 0.0252
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 : I -7 I 149
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9910 72.9598 66.9543
REMARK 3 T TENSOR
REMARK 3 T11: 0.0388 T22: 0.0250
REMARK 3 T33: 0.0127 T12: -0.0057
REMARK 3 T13: -0.0011 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.1504 L22: 0.6869
REMARK 3 L33: 0.2215 L12: 0.1166
REMARK 3 L13: 0.0794 L23: 0.0524
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: -0.0430 S13: 0.0329
REMARK 3 S21: 0.1396 S22: -0.0356 S23: 0.0377
REMARK 3 S31: -0.0284 S32: 0.0163 S33: 0.0273
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 : J 4 J 146
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3792 37.1056 66.9255
REMARK 3 T TENSOR
REMARK 3 T11: 0.0333 T22: 0.0266
REMARK 3 T33: 0.0681 T12: 0.0045
REMARK 3 T13: -0.0079 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 0.4879 L22: 1.3360
REMARK 3 L33: 0.1531 L12: -0.2490
REMARK 3 L13: -0.1029 L23: -0.1325
REMARK 3 S TENSOR
REMARK 3 S11: -0.0305 S12: -0.0260 S13: -0.1419
REMARK 3 S21: 0.0326 S22: 0.0207 S23: 0.1921
REMARK 3 S31: 0.0104 S32: -0.0014 S33: 0.0098
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 : K 4 K 146
REMARK 3 ORIGIN FOR THE GROUP (A): 64.8241 86.3433 65.7129
REMARK 3 T TENSOR
REMARK 3 T11: 0.0757 T22: 0.0029
REMARK 3 T33: 0.0877 T12: 0.0053
REMARK 3 T13: 0.0071 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.8987 L22: 0.9245
REMARK 3 L33: 0.2252 L12: -0.3082
REMARK 3 L13: -0.0194 L23: 0.0626
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.0106 S13: 0.2501
REMARK 3 S21: 0.0458 S22: 0.0057 S23: -0.1870
REMARK 3 S31: -0.0819 S32: -0.0172 S33: -0.0063
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 : L 3 L 153
REMARK 3 ORIGIN FOR THE GROUP (A): 43.5595 70.5152 37.7044
REMARK 3 T TENSOR
REMARK 3 T11: 0.0460 T22: 0.0641
REMARK 3 T33: 0.0073 T12: -0.0030
REMARK 3 T13: -0.0077 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.1577 L22: 0.4863
REMARK 3 L33: 0.6319 L12: 0.0292
REMARK 3 L13: -0.0394 L23: -0.0618
REMARK 3 S TENSOR
REMARK 3 S11: -0.0317 S12: 0.0456 S13: -0.0141
REMARK 3 S21: -0.0962 S22: 0.0778 S23: 0.0280
REMARK 3 S31: 0.0297 S32: -0.1321 S33: -0.0462
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: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN USED IF PRESENT IN THE INPUT
REMARK 4
REMARK 4 4FFU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000072848.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
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-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 194995
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
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 (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.49900
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 2.3.0
REMARK 200 STARTING MODEL: PDB ENTRY 1Q6W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M LICL, 0.1M HEPES, 25% PEG 6000,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 58.24500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.84250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.46900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.84250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.24500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.46900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: HEXAMERIC
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E, F, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, G, H, 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 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 MSE A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 SER A -15
REMARK 465 SER A -14
REMARK 465 GLY A -13
REMARK 465 VAL A -12
REMARK 465 ASP A -11
REMARK 465 LEU A -10
REMARK 465 GLY A -9
REMARK 465 THR A -8
REMARK 465 GLU A -7
REMARK 465 GLU A 149
REMARK 465 GLY A 150
REMARK 465 THR A 151
REMARK 465 ILE A 152
REMARK 465 GLN A 153
REMARK 465 MSE B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 SER B -15
REMARK 465 SER B -14
REMARK 465 GLY B -13
REMARK 465 VAL B -12
REMARK 465 ASP B -11
REMARK 465 LEU B -10
REMARK 465 GLY B -9
REMARK 465 THR B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLU B 149
REMARK 465 GLY B 150
REMARK 465 THR B 151
REMARK 465 ILE B 152
REMARK 465 GLN B 153
REMARK 465 MSE C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 SER C -15
REMARK 465 SER C -14
REMARK 465 GLY C -13
REMARK 465 VAL C -12
REMARK 465 ASP C -11
REMARK 465 LEU C -10
REMARK 465 GLY C -9
REMARK 465 THR C -8
REMARK 465 GLU C -7
REMARK 465 ASN C -6
REMARK 465 LEU C -5
REMARK 465 TYR C -4
REMARK 465 PHE C -3
REMARK 465 GLN C -2
REMARK 465 SER C -1
REMARK 465 MSE C 0
REMARK 465 MSE C 1
REMARK 465 SER C 2
REMARK 465 GLU C 3
REMARK 465 MSE D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 SER D -15
REMARK 465 SER D -14
REMARK 465 GLY D -13
REMARK 465 VAL D -12
REMARK 465 ASP D -11
REMARK 465 LEU D -10
REMARK 465 GLY D -9
REMARK 465 THR D -8
REMARK 465 GLU D -7
REMARK 465 ASN D -6
REMARK 465 LEU D -5
REMARK 465 TYR D -4
REMARK 465 PHE D -3
REMARK 465 GLN D -2
REMARK 465 SER D -1
REMARK 465 MSE D 0
REMARK 465 MSE D 1
REMARK 465 SER D 2
REMARK 465 GLY D 150
REMARK 465 THR D 151
REMARK 465 ILE D 152
REMARK 465 GLN D 153
REMARK 465 MSE E -22
REMARK 465 HIS E -21
REMARK 465 HIS E -20
REMARK 465 HIS E -19
REMARK 465 HIS E -18
REMARK 465 HIS E -17
REMARK 465 HIS E -16
REMARK 465 SER E -15
REMARK 465 SER E -14
REMARK 465 GLY E -13
REMARK 465 VAL E -12
REMARK 465 ASP E -11
REMARK 465 LEU E -10
REMARK 465 GLY E -9
REMARK 465 THR E -8
REMARK 465 GLU E -7
REMARK 465 ASN E -6
REMARK 465 LEU E -5
REMARK 465 TYR E -4
REMARK 465 PHE E -3
REMARK 465 GLN E -2
REMARK 465 SER E -1
REMARK 465 MSE E 0
REMARK 465 MSE E 1
REMARK 465 SER E 2
REMARK 465 MSE F -22
REMARK 465 HIS F -21
REMARK 465 HIS F -20
REMARK 465 HIS F -19
REMARK 465 HIS F -18
REMARK 465 HIS F -17
REMARK 465 HIS F -16
REMARK 465 SER F -15
REMARK 465 SER F -14
REMARK 465 GLY F -13
REMARK 465 VAL F -12
REMARK 465 ASP F -11
REMARK 465 LEU F -10
REMARK 465 GLY F -9
REMARK 465 THR F -8
REMARK 465 GLU F -7
REMARK 465 ASN F -6
REMARK 465 LEU F -5
REMARK 465 TYR F -4
REMARK 465 PHE F -3
REMARK 465 GLN F -2
REMARK 465 SER F -1
REMARK 465 MSE F 0
REMARK 465 MSE F 1
REMARK 465 SER F 2
REMARK 465 PRO F 148
REMARK 465 GLU F 149
REMARK 465 GLY F 150
REMARK 465 THR F 151
REMARK 465 ILE F 152
REMARK 465 GLN F 153
REMARK 465 MSE G -22
REMARK 465 HIS G -21
REMARK 465 HIS G -20
REMARK 465 HIS G -19
REMARK 465 HIS G -18
REMARK 465 HIS G -17
REMARK 465 HIS G -16
REMARK 465 SER G -15
REMARK 465 SER G -14
REMARK 465 GLY G -13
REMARK 465 VAL G -12
REMARK 465 ASP G -11
REMARK 465 LEU G -10
REMARK 465 GLY G -9
REMARK 465 THR G -8
REMARK 465 GLU G -7
REMARK 465 ASN G -6
REMARK 465 LEU G -5
REMARK 465 TYR G -4
REMARK 465 PHE G -3
REMARK 465 GLN G -2
REMARK 465 SER G -1
REMARK 465 MSE G 0
REMARK 465 MSE G 1
REMARK 465 SER G 2
REMARK 465 PRO G 148
REMARK 465 GLU G 149
REMARK 465 GLY G 150
REMARK 465 THR G 151
REMARK 465 ILE G 152
REMARK 465 GLN G 153
REMARK 465 MSE H -22
REMARK 465 HIS H -21
REMARK 465 HIS H -20
REMARK 465 HIS H -19
REMARK 465 HIS H -18
REMARK 465 HIS H -17
REMARK 465 HIS H -16
REMARK 465 SER H -15
REMARK 465 SER H -14
REMARK 465 GLY H -13
REMARK 465 VAL H -12
REMARK 465 ASP H -11
REMARK 465 LEU H -10
REMARK 465 GLY H -9
REMARK 465 THR H -8
REMARK 465 GLU H 149
REMARK 465 GLY H 150
REMARK 465 THR H 151
REMARK 465 ILE H 152
REMARK 465 GLN H 153
REMARK 465 MSE I -22
REMARK 465 HIS I -21
REMARK 465 HIS I -20
REMARK 465 HIS I -19
REMARK 465 HIS I -18
REMARK 465 HIS I -17
REMARK 465 HIS I -16
REMARK 465 SER I -15
REMARK 465 SER I -14
REMARK 465 GLY I -13
REMARK 465 VAL I -12
REMARK 465 ASP I -11
REMARK 465 LEU I -10
REMARK 465 GLY I -9
REMARK 465 THR I -8
REMARK 465 GLY I 150
REMARK 465 THR I 151
REMARK 465 ILE I 152
REMARK 465 GLN I 153
REMARK 465 MSE J -22
REMARK 465 HIS J -21
REMARK 465 HIS J -20
REMARK 465 HIS J -19
REMARK 465 HIS J -18
REMARK 465 HIS J -17
REMARK 465 HIS J -16
REMARK 465 SER J -15
REMARK 465 SER J -14
REMARK 465 GLY J -13
REMARK 465 VAL J -12
REMARK 465 ASP J -11
REMARK 465 LEU J -10
REMARK 465 GLY J -9
REMARK 465 THR J -8
REMARK 465 GLU J -7
REMARK 465 ASN J -6
REMARK 465 LEU J -5
REMARK 465 TYR J -4
REMARK 465 PHE J -3
REMARK 465 GLN J -2
REMARK 465 SER J -1
REMARK 465 MSE J 0
REMARK 465 MSE J 1
REMARK 465 SER J 2
REMARK 465 GLU J 3
REMARK 465 LYS J 147
REMARK 465 PRO J 148
REMARK 465 GLU J 149
REMARK 465 GLY J 150
REMARK 465 THR J 151
REMARK 465 ILE J 152
REMARK 465 GLN J 153
REMARK 465 MSE K -22
REMARK 465 HIS K -21
REMARK 465 HIS K -20
REMARK 465 HIS K -19
REMARK 465 HIS K -18
REMARK 465 HIS K -17
REMARK 465 HIS K -16
REMARK 465 SER K -15
REMARK 465 SER K -14
REMARK 465 GLY K -13
REMARK 465 VAL K -12
REMARK 465 ASP K -11
REMARK 465 LEU K -10
REMARK 465 GLY K -9
REMARK 465 THR K -8
REMARK 465 GLU K -7
REMARK 465 ASN K -6
REMARK 465 LEU K -5
REMARK 465 TYR K -4
REMARK 465 PHE K -3
REMARK 465 GLN K -2
REMARK 465 SER K -1
REMARK 465 MSE K 0
REMARK 465 MSE K 1
REMARK 465 SER K 2
REMARK 465 GLU K 3
REMARK 465 ASP K 111
REMARK 465 ASP K 112
REMARK 465 PRO K 113
REMARK 465 LYS K 114
REMARK 465 ARG K 115
REMARK 465 PRO K 116
REMARK 465 GLY K 117
REMARK 465 ALA K 118
REMARK 465 LYS K 147
REMARK 465 PRO K 148
REMARK 465 GLU K 149
REMARK 465 GLY K 150
REMARK 465 THR K 151
REMARK 465 ILE K 152
REMARK 465 GLN K 153
REMARK 465 MSE L -22
REMARK 465 HIS L -21
REMARK 465 HIS L -20
REMARK 465 HIS L -19
REMARK 465 HIS L -18
REMARK 465 HIS L -17
REMARK 465 HIS L -16
REMARK 465 SER L -15
REMARK 465 SER L -14
REMARK 465 GLY L -13
REMARK 465 VAL L -12
REMARK 465 ASP L -11
REMARK 465 LEU L -10
REMARK 465 GLY L -9
REMARK 465 THR L -8
REMARK 465 GLU L -7
REMARK 465 ASN L -6
REMARK 465 LEU L -5
REMARK 465 TYR L -4
REMARK 465 PHE L -3
REMARK 465 GLN L -2
REMARK 465 SER L -1
REMARK 465 MSE L 0
REMARK 465 MSE L 1
REMARK 465 SER L 2
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 GLN D 56 CA GLN D 56 C 0.158
REMARK 500 ARG F 101 CA ARG F 101 C 0.177
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 53 C - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500 MSE D 63 CA - CB - CG ANGL. DEV. = -10.5 DEGREES
REMARK 500 MSE D 63 CG - SE - CE ANGL. DEV. = -18.8 DEGREES
REMARK 500 HIS G 42 CA - C - N ANGL. DEV. = -14.7 DEGREES
REMARK 500 HIS G 42 CA - C - N ANGL. DEV. = -14.7 DEGREES
REMARK 500 ARG H 17 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG H 17 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 MSE L 63 CG - SE - CE ANGL. DEV. = -17.8 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 ALA B 107 -116.22 -103.29
REMARK 500 SER C 74 -72.89 13.60
REMARK 500 LEU E 75 94.85 -69.39
REMARK 500 SER J 74 -9.18 -58.28
REMARK 500 LEU K 75 40.34 -94.00
REMARK 500 PRO K 78 3.34 -64.68
REMARK 500 LEU L 75 96.14 -63.16
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 GLY A 54 -12.73
REMARK 500 GLY B 54 -15.36
REMARK 500 GLY C 54 -16.58
REMARK 500 GLY D 54 -16.57
REMARK 500 GLY F 54 -13.25
REMARK 500 GLY G 54 -14.36
REMARK 500 GLY I 54 -12.93
REMARK 500 GLY J 54 -15.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGRC-012249 RELATED DB: TARGETTRACK
DBREF 4FFU A 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU B 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU C 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU D 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU E 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU F 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU G 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU H 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU I 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU J 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU K 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
DBREF 4FFU L 1 153 UNP Q92VL2 Q92VL2_RHIME 1 153
SEQADV 4FFU MSE A -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS A -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS A -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS A -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS A -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS A -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS A -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER A -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER A -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY A -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL A -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP A -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU A -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY A -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR A -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU A -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN A -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU A -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR A -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE A -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN A -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER A -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE A 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE B -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS B -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS B -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS B -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS B -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS B -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS B -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER B -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER B -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY B -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL B -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP B -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU B -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY B -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR B -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU B -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN B -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU B -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR B -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE B -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN B -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER B -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE B 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE C -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS C -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS C -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS C -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS C -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS C -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS C -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER C -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER C -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY C -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL C -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP C -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU C -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY C -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR C -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU C -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN C -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU C -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR C -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE C -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN C -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER C -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE C 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE D -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS D -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS D -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS D -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS D -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS D -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS D -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER D -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER D -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY D -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL D -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP D -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU D -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY D -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR D -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU D -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN D -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU D -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR D -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE D -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN D -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER D -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE D 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE E -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS E -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS E -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS E -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS E -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS E -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS E -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER E -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER E -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY E -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL E -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP E -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU E -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY E -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR E -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU E -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN E -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU E -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR E -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE E -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN E -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER E -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE E 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE F -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS F -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS F -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS F -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS F -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS F -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS F -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER F -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER F -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY F -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL F -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP F -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU F -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY F -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR F -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU F -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN F -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU F -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR F -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE F -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN F -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER F -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE F 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE G -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS G -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS G -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS G -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS G -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS G -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS G -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER G -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER G -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY G -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL G -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP G -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU G -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY G -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR G -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU G -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN G -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU G -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR G -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE G -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN G -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER G -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE G 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE H -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS H -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS H -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS H -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS H -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS H -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS H -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER H -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER H -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY H -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL H -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP H -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU H -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY H -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR H -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU H -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN H -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU H -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR H -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE H -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN H -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER H -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE H 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE I -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS I -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS I -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS I -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS I -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS I -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS I -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER I -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER I -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY I -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL I -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP I -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU I -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY I -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR I -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU I -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN I -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU I -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR I -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE I -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN I -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER I -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE I 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE J -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS J -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS J -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS J -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS J -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS J -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS J -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER J -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER J -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY J -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL J -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP J -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU J -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY J -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR J -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU J -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN J -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU J -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR J -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE J -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN J -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER J -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE J 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE K -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS K -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS K -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS K -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS K -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS K -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS K -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER K -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER K -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY K -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL K -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP K -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU K -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY K -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR K -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU K -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN K -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU K -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR K -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE K -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN K -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER K -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE K 0 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE L -22 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS L -21 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS L -20 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS L -19 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS L -18 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS L -17 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU HIS L -16 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER L -15 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER L -14 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY L -13 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU VAL L -12 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASP L -11 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU L -10 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLY L -9 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU THR L -8 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLU L -7 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU ASN L -6 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU LEU L -5 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU TYR L -4 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU PHE L -3 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU GLN L -2 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU SER L -1 UNP Q92VL2 EXPRESSION TAG
SEQADV 4FFU MSE L 0 UNP Q92VL2 EXPRESSION TAG
SEQRES 1 A 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 A 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 A 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 A 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 A 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 A 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 A 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 A 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 A 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 A 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 A 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 A 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 A 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 B 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 B 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 B 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 B 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 B 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 B 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 B 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 B 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 B 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 B 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 B 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 B 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 B 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 C 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 C 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 C 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 C 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 C 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 C 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 C 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 C 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 C 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 C 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 C 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 C 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 C 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 D 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 D 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 D 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 D 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 D 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 D 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 D 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 D 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 D 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 D 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 D 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 D 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 D 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 E 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 E 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 E 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 E 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 E 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 E 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 E 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 E 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 E 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 E 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 E 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 E 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 E 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 E 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 F 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 F 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 F 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 F 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 F 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 F 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 F 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 F 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 F 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 F 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 F 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 F 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 F 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 F 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 G 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 G 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 G 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 G 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 G 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 G 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 G 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 G 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 G 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 G 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 G 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 G 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 G 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 G 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 H 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 H 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 H 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 H 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 H 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 H 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 H 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 H 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 H 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 H 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 H 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 H 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 H 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 H 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 I 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 I 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 I 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 I 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 I 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 I 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 I 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 I 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 I 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 I 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 I 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 I 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 I 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 I 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 J 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 J 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 J 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 J 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 J 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 J 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 J 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 J 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 J 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 J 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 J 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 J 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 J 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 J 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 K 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 K 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 K 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 K 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 K 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 K 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 K 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 K 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 K 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 K 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 K 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 K 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 K 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 K 176 LYS PRO GLU GLY THR ILE GLN
SEQRES 1 L 176 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 L 176 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE SER GLU
SEQRES 3 L 176 GLN THR ILE TYR TYR GLU ASP TYR GLU GLN GLY HIS VAL
SEQRES 4 L 176 ARG LEU THR SER GLY ARG THR ILE THR GLU THR ASP PHE
SEQRES 5 L 176 VAL VAL HIS ALA GLY HIS THR GLY ASP PHE PHE PRO HIS
SEQRES 6 L 176 HIS MSE ASP ALA GLU PHE ALA LYS THR LEU PRO GLY GLY
SEQRES 7 L 176 GLN ARG ILE ALA HIS GLY THR MSE ILE PHE SER ILE GLY
SEQRES 8 L 176 VAL GLY LEU THR ALA SER LEU ILE ASN PRO VAL ALA PHE
SEQRES 9 L 176 SER TYR GLY TYR ASP ARG LEU ARG PHE VAL ARG PRO VAL
SEQRES 10 L 176 HIS ILE GLY ASP THR ILE ARG THR ARG VAL THR ILE ALA
SEQRES 11 L 176 ALA LYS GLU ASP ASP PRO LYS ARG PRO GLY ALA GLY ARG
SEQRES 12 L 176 VAL VAL GLU ARG CYS GLU VAL ILE ASN GLN ARG GLY GLU
SEQRES 13 L 176 VAL VAL LEU ALA ALA ASP HIS ILE LEU ILE VAL GLU ARG
SEQRES 14 L 176 LYS PRO GLU GLY THR ILE GLN
MODRES 4FFU MSE A 0 MET SELENOMETHIONINE
MODRES 4FFU MSE A 1 MET SELENOMETHIONINE
MODRES 4FFU MSE A 44 MET SELENOMETHIONINE
MODRES 4FFU MSE A 63 MET SELENOMETHIONINE
MODRES 4FFU MSE B 0 MET SELENOMETHIONINE
MODRES 4FFU MSE B 1 MET SELENOMETHIONINE
MODRES 4FFU MSE B 44 MET SELENOMETHIONINE
MODRES 4FFU MSE B 63 MET SELENOMETHIONINE
MODRES 4FFU MSE C 44 MET SELENOMETHIONINE
MODRES 4FFU MSE C 63 MET SELENOMETHIONINE
MODRES 4FFU MSE D 44 MET SELENOMETHIONINE
MODRES 4FFU MSE D 63 MET SELENOMETHIONINE
MODRES 4FFU MSE E 44 MET SELENOMETHIONINE
MODRES 4FFU MSE E 63 MET SELENOMETHIONINE
MODRES 4FFU MSE F 44 MET SELENOMETHIONINE
MODRES 4FFU MSE F 63 MET SELENOMETHIONINE
MODRES 4FFU MSE G 44 MET SELENOMETHIONINE
MODRES 4FFU MSE G 63 MET SELENOMETHIONINE
MODRES 4FFU MSE H 0 MET SELENOMETHIONINE
MODRES 4FFU MSE H 1 MET SELENOMETHIONINE
MODRES 4FFU MSE H 44 MET SELENOMETHIONINE
MODRES 4FFU MSE H 63 MET SELENOMETHIONINE
MODRES 4FFU MSE I 0 MET SELENOMETHIONINE
MODRES 4FFU MSE I 1 MET SELENOMETHIONINE
MODRES 4FFU MSE I 44 MET SELENOMETHIONINE
MODRES 4FFU MSE I 63 MET SELENOMETHIONINE
MODRES 4FFU MSE J 44 MET SELENOMETHIONINE
MODRES 4FFU MSE J 63 MET SELENOMETHIONINE
MODRES 4FFU MSE K 44 MET SELENOMETHIONINE
MODRES 4FFU MSE K 63 MET SELENOMETHIONINE
MODRES 4FFU MSE L 44 MET SELENOMETHIONINE
MODRES 4FFU MSE L 63 MET SELENOMETHIONINE
HET MSE A 0 8
HET MSE A 1 8
HET MSE A 44 8
HET MSE A 63 8
HET MSE B 0 8
HET MSE B 1 8
HET MSE B 44 8
HET MSE B 63 8
HET MSE C 44 8
HET MSE C 63 8
HET MSE D 44 8
HET MSE D 63 13
HET MSE E 44 8
HET MSE E 63 8
HET MSE F 44 8
HET MSE F 63 13
HET MSE G 44 8
HET MSE G 63 13
HET MSE H 0 8
HET MSE H 1 13
HET MSE H 44 8
HET MSE H 63 8
HET MSE I 0 13
HET MSE I 1 8
HET MSE I 44 8
HET MSE I 63 8
HET MSE J 44 8
HET MSE J 63 8
HET MSE K 44 8
HET MSE K 63 13
HET MSE L 44 13
HET MSE L 63 8
HET CL H 201 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 32(C5 H11 N O2 SE)
FORMUL 13 CL CL 1-
FORMUL 14 HOH *1829(H2 O)
HELIX 1 1 TYR A 7 TYR A 11 5 5
HELIX 2 2 THR A 25 GLY A 37 1 13
HELIX 3 3 PHE A 40 ASP A 45 1 6
HELIX 4 4 ASP A 45 LYS A 50 1 6
HELIX 5 5 HIS A 60 THR A 72 1 13
HELIX 6 6 TYR B 7 TYR B 11 5 5
HELIX 7 7 THR B 25 GLY B 37 1 13
HELIX 8 8 PHE B 40 ASP B 45 1 6
HELIX 9 9 ASP B 45 LYS B 50 1 6
HELIX 10 10 HIS B 60 THR B 72 1 13
HELIX 11 11 TYR C 7 TYR C 11 5 5
HELIX 12 12 THR C 25 GLY C 37 1 13
HELIX 13 13 PHE C 40 ASP C 45 1 6
HELIX 14 14 ASP C 45 LYS C 50 1 6
HELIX 15 15 HIS C 60 LEU C 71 1 12
HELIX 16 16 TYR D 7 TYR D 11 5 5
HELIX 17 17 THR D 25 GLY D 37 1 13
HELIX 18 18 PHE D 40 ASP D 45 1 6
HELIX 19 19 GLU D 47 LEU D 52 5 6
HELIX 20 20 HIS D 60 LEU D 71 1 12
HELIX 21 21 TYR E 7 TYR E 11 5 5
HELIX 22 22 THR E 25 GLY E 37 1 13
HELIX 23 23 PHE E 40 ASP E 45 1 6
HELIX 24 24 ASP E 45 LYS E 50 1 6
HELIX 25 25 HIS E 60 LEU E 71 1 12
HELIX 26 26 TYR F 7 TYR F 11 5 5
HELIX 27 27 THR F 25 GLY F 37 1 13
HELIX 28 28 PHE F 40 ASP F 45 1 6
HELIX 29 29 ASP F 45 LYS F 50 1 6
HELIX 30 30 HIS F 60 LEU F 71 1 12
HELIX 31 31 TYR G 7 TYR G 11 5 5
HELIX 32 32 THR G 25 GLY G 37 1 13
HELIX 33 33 PHE G 40 ASP G 45 1 6
HELIX 34 34 ASP G 45 LYS G 50 1 6
HELIX 35 35 HIS G 60 LEU G 71 1 12
HELIX 36 36 ASN H -6 GLN H -2 5 5
HELIX 37 37 TYR H 7 TYR H 11 5 5
HELIX 38 38 THR H 25 GLY H 37 1 13
HELIX 39 39 PHE H 40 ASP H 45 1 6
HELIX 40 40 ASP H 45 LYS H 50 1 6
HELIX 41 41 HIS H 60 LEU H 71 1 12
HELIX 42 42 ASN I -6 GLN I -2 5 5
HELIX 43 43 TYR I 7 TYR I 11 5 5
HELIX 44 44 THR I 25 GLY I 37 1 13
HELIX 45 45 PHE I 40 ASP I 45 1 6
HELIX 46 46 ASP I 45 LYS I 50 1 6
HELIX 47 47 HIS I 60 LEU I 71 1 12
HELIX 48 48 TYR J 7 TYR J 11 5 5
HELIX 49 49 THR J 25 GLY J 37 1 13
HELIX 50 50 PHE J 40 ASP J 45 1 6
HELIX 51 51 ASP J 45 LYS J 50 1 6
HELIX 52 52 HIS J 60 LEU J 71 1 12
HELIX 53 53 THR J 72 ILE J 76 5 5
HELIX 54 54 TYR K 7 TYR K 11 5 5
HELIX 55 55 THR K 25 GLY K 37 1 13
HELIX 56 56 PHE K 40 ASP K 45 1 6
HELIX 57 57 ASP K 45 LYS K 50 1 6
HELIX 58 58 HIS K 60 LEU K 71 1 12
HELIX 59 59 THR K 72 ILE K 76 5 5
HELIX 60 60 TYR L 7 TYR L 11 5 5
HELIX 61 61 THR L 25 GLY L 37 1 13
HELIX 62 62 PHE L 40 ASP L 45 1 6
HELIX 63 63 ASP L 45 LYS L 50 1 6
HELIX 64 64 HIS L 60 LEU L 71 1 12
SHEET 1 A11 PHE A -3 SER A -1 0
SHEET 2 A11 VAL J 16 LEU J 18 1 O VAL J 16 N GLN A -2
SHEET 3 A11 THR J 99 ASP J 111 -1 O VAL J 104 N ARG J 17
SHEET 4 A11 ALA J 118 ILE J 128 -1 O GLU J 126 N ARG J 103
SHEET 5 A11 VAL J 134 GLU J 145 -1 O ALA J 138 N CYS J 125
SHEET 6 A11 ALA J 80 PHE J 90 -1 N ARG J 89 O ALA J 137
SHEET 7 A11 ALA F 80 PHE F 90 -1 N LEU F 88 O TYR J 85
SHEET 8 A11 VAL F 134 GLU F 145 -1 O ILE F 143 N PHE F 81
SHEET 9 A11 ALA F 118 ILE F 128 -1 N CYS F 125 O ALA F 138
SHEET 10 A11 THR F 99 ASP F 111 -1 N GLU F 110 O ARG F 120
SHEET 11 A11 ARG F 22 THR F 23 -1 N ARG F 22 O ILE F 100
SHEET 1 B10 VAL F 16 LEU F 18 0
SHEET 2 B10 THR F 99 ASP F 111 -1 O VAL F 104 N ARG F 17
SHEET 3 B10 ALA F 118 ILE F 128 -1 O ARG F 120 N GLU F 110
SHEET 4 B10 VAL F 134 GLU F 145 -1 O ALA F 138 N CYS F 125
SHEET 5 B10 ALA F 80 PHE F 90 -1 N PHE F 81 O ILE F 143
SHEET 6 B10 ALA J 80 PHE J 90 -1 O TYR J 85 N LEU F 88
SHEET 7 B10 VAL J 134 GLU J 145 -1 O ALA J 137 N ARG J 89
SHEET 8 B10 ALA J 118 ILE J 128 -1 N CYS J 125 O ALA J 138
SHEET 9 B10 THR J 99 ASP J 111 -1 N ARG J 103 O GLU J 126
SHEET 10 B10 ARG J 22 THR J 23 -1 N ARG J 22 O ILE J 100
SHEET 1 C10 VAL A 16 LEU A 18 0
SHEET 2 C10 THR A 99 ASP A 111 -1 O VAL A 104 N ARG A 17
SHEET 3 C10 ALA A 118 ILE A 128 -1 O ARG A 120 N GLU A 110
SHEET 4 C10 VAL A 134 GLU A 145 -1 O ALA A 138 N CYS A 125
SHEET 5 C10 ALA A 80 PHE A 90 -1 N PHE A 81 O ILE A 143
SHEET 6 C10 ALA E 80 PHE E 90 -1 O PHE E 90 N TYR A 83
SHEET 7 C10 VAL E 134 GLU E 145 -1 O ALA E 137 N ARG E 89
SHEET 8 C10 ALA E 118 ILE E 128 -1 N CYS E 125 O ALA E 138
SHEET 9 C10 THR E 99 ASP E 111 -1 N GLU E 110 O ARG E 120
SHEET 10 C10 VAL E 16 LEU E 18 -1 N ARG E 17 O VAL E 104
SHEET 1 D10 ARG A 22 THR A 23 0
SHEET 2 D10 THR A 99 ASP A 111 -1 O ILE A 100 N ARG A 22
SHEET 3 D10 ALA A 118 ILE A 128 -1 O ARG A 120 N GLU A 110
SHEET 4 D10 VAL A 134 GLU A 145 -1 O ALA A 138 N CYS A 125
SHEET 5 D10 ALA A 80 PHE A 90 -1 N PHE A 81 O ILE A 143
SHEET 6 D10 ALA E 80 PHE E 90 -1 O PHE E 90 N TYR A 83
SHEET 7 D10 VAL E 134 GLU E 145 -1 O ALA E 137 N ARG E 89
SHEET 8 D10 ALA E 118 ILE E 128 -1 N CYS E 125 O ALA E 138
SHEET 9 D10 THR E 99 ASP E 111 -1 N GLU E 110 O ARG E 120
SHEET 10 D10 ARG E 22 THR E 23 -1 N ARG E 22 O ILE E 100
SHEET 1 E10 VAL B 16 LEU B 18 0
SHEET 2 E10 THR B 99 ASP B 111 -1 O VAL B 104 N ARG B 17
SHEET 3 E10 ALA B 118 ILE B 128 -1 O ILE B 128 N ARG B 101
SHEET 4 E10 VAL B 134 GLU B 145 -1 O HIS B 140 N GLU B 123
SHEET 5 E10 ALA B 80 PHE B 90 -1 N ARG B 89 O ALA B 137
SHEET 6 E10 ALA L 80 PHE L 90 -1 O TYR L 85 N LEU B 88
SHEET 7 E10 VAL L 134 GLU L 145 -1 O ALA L 137 N ARG L 89
SHEET 8 E10 ALA L 118 ILE L 128 -1 N GLY L 119 O VAL L 144
SHEET 9 E10 THR L 99 ASP L 111 -1 N ARG L 101 O ILE L 128
SHEET 10 E10 VAL L 16 LEU L 18 -1 N ARG L 17 O VAL L 104
SHEET 1 F10 ARG B 22 THR B 23 0
SHEET 2 F10 THR B 99 ASP B 111 -1 O ILE B 100 N ARG B 22
SHEET 3 F10 ALA B 118 ILE B 128 -1 O ILE B 128 N ARG B 101
SHEET 4 F10 VAL B 134 GLU B 145 -1 O HIS B 140 N GLU B 123
SHEET 5 F10 ALA B 80 PHE B 90 -1 N ARG B 89 O ALA B 137
SHEET 6 F10 ALA L 80 PHE L 90 -1 O TYR L 85 N LEU B 88
SHEET 7 F10 VAL L 134 GLU L 145 -1 O ALA L 137 N ARG L 89
SHEET 8 F10 ALA L 118 ILE L 128 -1 N GLY L 119 O VAL L 144
SHEET 9 F10 THR L 99 ASP L 111 -1 N ARG L 101 O ILE L 128
SHEET 10 F10 ARG L 22 THR L 23 -1 N ARG L 22 O ILE L 100
SHEET 1 G10 VAL C 16 LEU C 18 0
SHEET 2 G10 THR C 99 ASP C 111 -1 O VAL C 104 N ARG C 17
SHEET 3 G10 ALA C 118 ILE C 128 -1 O GLU C 126 N ARG C 103
SHEET 4 G10 VAL C 134 GLU C 145 -1 O ALA C 138 N CYS C 125
SHEET 5 G10 ALA C 80 PHE C 90 -1 N ARG C 89 O ALA C 137
SHEET 6 G10 ALA H 80 PHE H 90 -1 O TYR H 85 N LEU C 88
SHEET 7 G10 VAL H 134 GLU H 145 -1 O ALA H 137 N ARG H 89
SHEET 8 G10 ALA H 118 ILE H 128 -1 N CYS H 125 O ALA H 138
SHEET 9 G10 THR H 99 ASP H 111 -1 N GLU H 110 O ARG H 120
SHEET 10 G10 VAL H 16 LEU H 18 -1 N ARG H 17 O VAL H 104
SHEET 1 H10 ARG C 22 THR C 23 0
SHEET 2 H10 THR C 99 ASP C 111 -1 O ILE C 100 N ARG C 22
SHEET 3 H10 ALA C 118 ILE C 128 -1 O GLU C 126 N ARG C 103
SHEET 4 H10 VAL C 134 GLU C 145 -1 O ALA C 138 N CYS C 125
SHEET 5 H10 ALA C 80 PHE C 90 -1 N ARG C 89 O ALA C 137
SHEET 6 H10 ALA H 80 PHE H 90 -1 O TYR H 85 N LEU C 88
SHEET 7 H10 VAL H 134 GLU H 145 -1 O ALA H 137 N ARG H 89
SHEET 8 H10 ALA H 118 ILE H 128 -1 N CYS H 125 O ALA H 138
SHEET 9 H10 THR H 99 ASP H 111 -1 N GLU H 110 O ARG H 120
SHEET 10 H10 ARG H 22 THR H 23 -1 N ARG H 22 O ILE H 100
SHEET 1 I10 VAL D 16 LEU D 18 0
SHEET 2 I10 THR D 99 ASP D 111 -1 O VAL D 104 N ARG D 17
SHEET 3 I10 ALA D 118 ILE D 128 -1 O ARG D 120 N GLU D 110
SHEET 4 I10 VAL D 134 GLU D 145 -1 O VAL D 135 N VAL D 127
SHEET 5 I10 ALA D 80 PHE D 90 -1 N PHE D 81 O ILE D 143
SHEET 6 I10 ALA I 80 PHE I 90 -1 O TYR I 83 N PHE D 90
SHEET 7 I10 VAL I 134 GLU I 145 -1 O ASP I 139 N ASP I 86
SHEET 8 I10 ALA I 118 ILE I 128 -1 N CYS I 125 O ALA I 138
SHEET 9 I10 THR I 99 ASP I 111 -1 N GLU I 110 O ARG I 120
SHEET 10 I10 VAL I 16 LEU I 18 -1 N ARG I 17 O VAL I 104
SHEET 1 J10 ARG D 22 THR D 23 0
SHEET 2 J10 THR D 99 ASP D 111 -1 O ILE D 100 N ARG D 22
SHEET 3 J10 ALA D 118 ILE D 128 -1 O ARG D 120 N GLU D 110
SHEET 4 J10 VAL D 134 GLU D 145 -1 O VAL D 135 N VAL D 127
SHEET 5 J10 ALA D 80 PHE D 90 -1 N PHE D 81 O ILE D 143
SHEET 6 J10 ALA I 80 PHE I 90 -1 O TYR I 83 N PHE D 90
SHEET 7 J10 VAL I 134 GLU I 145 -1 O ASP I 139 N ASP I 86
SHEET 8 J10 ALA I 118 ILE I 128 -1 N CYS I 125 O ALA I 138
SHEET 9 J10 THR I 99 ASP I 111 -1 N GLU I 110 O ARG I 120
SHEET 10 J10 ARG I 22 THR I 23 -1 N ARG I 22 O ILE I 100
SHEET 1 K10 VAL G 16 LEU G 18 0
SHEET 2 K10 THR G 99 ASP G 111 -1 O VAL G 104 N ARG G 17
SHEET 3 K10 ALA G 118 ILE G 128 -1 O ARG G 120 N GLU G 110
SHEET 4 K10 VAL G 134 GLU G 145 -1 O VAL G 144 N GLY G 119
SHEET 5 K10 ALA G 80 PHE G 90 -1 N PHE G 81 O ILE G 143
SHEET 6 K10 ALA K 80 PHE K 90 -1 O TYR K 83 N PHE G 90
SHEET 7 K10 VAL K 134 VAL K 144 -1 O ILE K 141 N GLY K 84
SHEET 8 K10 ARG K 120 ILE K 128 -1 N GLU K 123 O HIS K 140
SHEET 9 K10 THR K 99 LYS K 109 -1 N ARG K 103 O GLU K 126
SHEET 10 K10 VAL K 16 LEU K 18 -1 N ARG K 17 O VAL K 104
SHEET 1 L10 ARG G 22 THR G 23 0
SHEET 2 L10 THR G 99 ASP G 111 -1 O ILE G 100 N ARG G 22
SHEET 3 L10 ALA G 118 ILE G 128 -1 O ARG G 120 N GLU G 110
SHEET 4 L10 VAL G 134 GLU G 145 -1 O VAL G 144 N GLY G 119
SHEET 5 L10 ALA G 80 PHE G 90 -1 N PHE G 81 O ILE G 143
SHEET 6 L10 ALA K 80 PHE K 90 -1 O TYR K 83 N PHE G 90
SHEET 7 L10 VAL K 134 VAL K 144 -1 O ILE K 141 N GLY K 84
SHEET 8 L10 ARG K 120 ILE K 128 -1 N GLU K 123 O HIS K 140
SHEET 9 L10 THR K 99 LYS K 109 -1 N ARG K 103 O GLU K 126
SHEET 10 L10 ARG K 22 THR K 23 -1 N ARG K 22 O ILE K 100
LINK C SER A -1 N MSE A 0 1555 1555 1.32
LINK C MSE A 0 N MSE A 1 1555 1555 1.30
LINK C MSE A 1 N SER A 2 1555 1555 1.33
LINK C HIS A 43 N MSE A 44 1555 1555 1.35
LINK C MSE A 44 N ASP A 45 1555 1555 1.34
LINK C THR A 62 N MSE A 63 1555 1555 1.33
LINK C MSE A 63 N ILE A 64 1555 1555 1.32
LINK C SER B -1 N MSE B 0 1555 1555 1.33
LINK C MSE B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N SER B 2 1555 1555 1.33
LINK C HIS B 43 N MSE B 44 1555 1555 1.34
LINK C MSE B 44 N ASP B 45 1555 1555 1.33
LINK C THR B 62 N MSE B 63 1555 1555 1.34
LINK C MSE B 63 N ILE B 64 1555 1555 1.33
LINK C HIS C 43 N MSE C 44 1555 1555 1.33
LINK C MSE C 44 N ASP C 45 1555 1555 1.34
LINK C THR C 62 N MSE C 63 1555 1555 1.34
LINK C MSE C 63 N ILE C 64 1555 1555 1.33
LINK C HIS D 43 N MSE D 44 1555 1555 1.33
LINK C MSE D 44 N ASP D 45 1555 1555 1.35
LINK C THR D 62 N MSE D 63 1555 1555 1.34
LINK C MSE D 63 N ILE D 64 1555 1555 1.33
LINK C HIS E 43 N MSE E 44 1555 1555 1.34
LINK C MSE E 44 N ASP E 45 1555 1555 1.35
LINK C THR E 62 N MSE E 63 1555 1555 1.34
LINK C MSE E 63 N ILE E 64 1555 1555 1.33
LINK C HIS F 43 N MSE F 44 1555 1555 1.34
LINK C MSE F 44 N ASP F 45 1555 1555 1.34
LINK C THR F 62 N MSE F 63 1555 1555 1.33
LINK C MSE F 63 N ILE F 64 1555 1555 1.32
LINK C HIS G 43 N MSE G 44 1555 1555 1.33
LINK C MSE G 44 N ASP G 45 1555 1555 1.34
LINK C THR G 62 N MSE G 63 1555 1555 1.34
LINK C MSE G 63 N ILE G 64 1555 1555 1.33
LINK C SER H -1 N MSE H 0 1555 1555 1.34
LINK C MSE H 0 N MSE H 1 1555 1555 1.34
LINK C MSE H 1 N SER H 2 1555 1555 1.33
LINK C HIS H 43 N MSE H 44 1555 1555 1.34
LINK C MSE H 44 N ASP H 45 1555 1555 1.34
LINK C THR H 62 N MSE H 63 1555 1555 1.32
LINK C MSE H 63 N ILE H 64 1555 1555 1.33
LINK C SER I -1 N MSE I 0 1555 1555 1.34
LINK C MSE I 0 N MSE I 1 1555 1555 1.33
LINK C MSE I 1 N SER I 2 1555 1555 1.33
LINK C HIS I 43 N MSE I 44 1555 1555 1.33
LINK C MSE I 44 N ASP I 45 1555 1555 1.34
LINK C THR I 62 N MSE I 63 1555 1555 1.33
LINK C MSE I 63 N ILE I 64 1555 1555 1.33
LINK C HIS J 43 N MSE J 44 1555 1555 1.34
LINK C MSE J 44 N ASP J 45 1555 1555 1.34
LINK C THR J 62 N MSE J 63 1555 1555 1.33
LINK C MSE J 63 N ILE J 64 1555 1555 1.32
LINK C HIS K 43 N MSE K 44 1555 1555 1.33
LINK C MSE K 44 N ASP K 45 1555 1555 1.34
LINK C THR K 62 N MSE K 63 1555 1555 1.33
LINK C MSE K 63 N ILE K 64 1555 1555 1.33
LINK C HIS L 43 N MSE L 44 1555 1555 1.35
LINK C MSE L 44 N ASP L 45 1555 1555 1.33
LINK C THR L 62 N MSE L 63 1555 1555 1.32
LINK C MSE L 63 N ILE L 64 1555 1555 1.32
SITE 1 AC1 5 GLN H 13 ALA H 108 LYS H 109 HOH H 307
SITE 2 AC1 5 ARG J 101
CRYST1 116.490 122.938 147.685 90.00 90.00 90.00 P 21 21 21 48
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 0.008584 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008134 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006771 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
