HEADER RIBOSOME 05-OCT-04 1XNQ
TITLE STRUCTURE OF AN INOSINE-ADENINE WOBBLE BASE PAIR COMPLEX IN THE
TITLE 2 CONTEXT OF THE DECODING CENTER
CAVEAT 1XNQ CHIRALITY ERROR AT U1528A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 16S RIBOSOMAL RNA;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ANTICODON TRNA;
COMPND 6 CHAIN: X;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 3;
COMPND 9 MOLECULE: MRNA;
COMPND 10 CHAIN: W;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 4;
COMPND 13 MOLECULE: RIBOSOMAL PROTEIN S2;
COMPND 14 CHAIN: B;
COMPND 15 MOL_ID: 5;
COMPND 16 MOLECULE: RIBOSOMAL PROTEIN S3;
COMPND 17 CHAIN: C;
COMPND 18 MOL_ID: 6;
COMPND 19 MOLECULE: RIBOSOMAL PROTEIN S4;
COMPND 20 CHAIN: D;
COMPND 21 MOL_ID: 7;
COMPND 22 MOLECULE: RIBOSOMAL PROTEIN S5;
COMPND 23 CHAIN: E;
COMPND 24 MOL_ID: 8;
COMPND 25 MOLECULE: RIBOSOMAL PROTEIN S6;
COMPND 26 CHAIN: F;
COMPND 27 SYNONYM: TS9;
COMPND 28 MOL_ID: 9;
COMPND 29 MOLECULE: RIBOSOMAL PROTEIN S7;
COMPND 30 CHAIN: G;
COMPND 31 MOL_ID: 10;
COMPND 32 MOLECULE: RIBOSOMAL PROTEIN S8;
COMPND 33 CHAIN: H;
COMPND 34 MOL_ID: 11;
COMPND 35 MOLECULE: RIBOSOMAL PROTEIN S9;
COMPND 36 CHAIN: I;
COMPND 37 MOL_ID: 12;
COMPND 38 MOLECULE: RIBOSOMAL PROTEIN S10;
COMPND 39 CHAIN: J;
COMPND 40 MOL_ID: 13;
COMPND 41 MOLECULE: RIBOSOMAL PROTEIN S11;
COMPND 42 CHAIN: K;
COMPND 43 MOL_ID: 14;
COMPND 44 MOLECULE: RIBOSOMAL PROTEIN S12;
COMPND 45 CHAIN: L;
COMPND 46 MOL_ID: 15;
COMPND 47 MOLECULE: RIBOSOMAL PROTEIN S13;
COMPND 48 CHAIN: M;
COMPND 49 MOL_ID: 16;
COMPND 50 MOLECULE: RIBOSOMAL PROTEIN S14;
COMPND 51 CHAIN: N;
COMPND 52 MOL_ID: 17;
COMPND 53 MOLECULE: RIBOSOMAL PROTEIN S15;
COMPND 54 CHAIN: O;
COMPND 55 MOL_ID: 18;
COMPND 56 MOLECULE: RIBOSOMAL PROTEIN S16;
COMPND 57 CHAIN: P;
COMPND 58 MOL_ID: 19;
COMPND 59 MOLECULE: RIBOSOMAL PROTEIN S17;
COMPND 60 CHAIN: Q;
COMPND 61 MOL_ID: 20;
COMPND 62 MOLECULE: RIBOSOMAL PROTEIN S18;
COMPND 63 CHAIN: R;
COMPND 64 MOL_ID: 21;
COMPND 65 MOLECULE: RIBOSOMAL PROTEIN S19;
COMPND 66 CHAIN: S;
COMPND 67 MOL_ID: 22;
COMPND 68 MOLECULE: RIBOSOMAL PROTEIN S20;
COMPND 69 CHAIN: T;
COMPND 70 MOL_ID: 23;
COMPND 71 MOLECULE: RIBOSOMAL PROTEIN THX;
COMPND 72 CHAIN: V
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 MOL_ID: 2;
SOURCE 5 SYNTHETIC: YES;
SOURCE 6 MOL_ID: 3;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 MOL_ID: 4;
SOURCE 9 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 10 ORGANISM_TAXID: 274;
SOURCE 11 MOL_ID: 5;
SOURCE 12 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 13 ORGANISM_TAXID: 274;
SOURCE 14 MOL_ID: 6;
SOURCE 15 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 16 ORGANISM_TAXID: 274;
SOURCE 17 MOL_ID: 7;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 19 ORGANISM_TAXID: 274;
SOURCE 20 MOL_ID: 8;
SOURCE 21 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 22 ORGANISM_TAXID: 274;
SOURCE 23 MOL_ID: 9;
SOURCE 24 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 25 ORGANISM_TAXID: 274;
SOURCE 26 MOL_ID: 10;
SOURCE 27 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 28 ORGANISM_TAXID: 274;
SOURCE 29 MOL_ID: 11;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 31 ORGANISM_TAXID: 274;
SOURCE 32 MOL_ID: 12;
SOURCE 33 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 34 ORGANISM_TAXID: 274;
SOURCE 35 MOL_ID: 13;
SOURCE 36 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 37 ORGANISM_TAXID: 274;
SOURCE 38 MOL_ID: 14;
SOURCE 39 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 40 ORGANISM_TAXID: 274;
SOURCE 41 MOL_ID: 15;
SOURCE 42 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 43 ORGANISM_TAXID: 274;
SOURCE 44 MOL_ID: 16;
SOURCE 45 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 46 ORGANISM_TAXID: 274;
SOURCE 47 MOL_ID: 17;
SOURCE 48 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 49 ORGANISM_TAXID: 274;
SOURCE 50 MOL_ID: 18;
SOURCE 51 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 52 ORGANISM_TAXID: 274;
SOURCE 53 MOL_ID: 19;
SOURCE 54 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 55 ORGANISM_TAXID: 274;
SOURCE 56 MOL_ID: 20;
SOURCE 57 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 58 ORGANISM_TAXID: 274;
SOURCE 59 MOL_ID: 21;
SOURCE 60 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 61 ORGANISM_TAXID: 274;
SOURCE 62 MOL_ID: 22;
SOURCE 63 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 64 ORGANISM_TAXID: 274;
SOURCE 65 MOL_ID: 23;
SOURCE 66 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 67 ORGANISM_TAXID: 274
KEYWDS RIBOSOME, DECODING, TRANSLATION, INOSINE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.V.MURPHY,V.RAMAKRISHNAN
REVDAT 3 03-APR-24 1XNQ 1 REMARK HETSYN LINK
REVDAT 2 24-FEB-09 1XNQ 1 VERSN
REVDAT 1 14-DEC-04 1XNQ 0
JRNL AUTH F.V.MURPHY,V.RAMAKRISHNAN
JRNL TITL STRUCTURE OF A PURINE-PURINE WOBBLE BASE PAIR IN THE
JRNL TITL 2 DECODING CENTER OF THE RIBOSOME.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 1251 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15558050
JRNL DOI 10.1038/NSMB866
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 99.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 271076
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : CARRIED THROUGH FROM STARTING
REMARK 3 MODEL
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 12807
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19229
REMARK 3 NUCLEIC ACID ATOMS : 32696
REMARK 3 HETEROGEN ATOMS : 151
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : 0.58
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.61
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XNQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030556.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : SI111
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 272898
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 27.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.880
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: EMPTY 30S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, MAGNESIUM CHLORIDE, POTASSIUM
REMARK 280 CHLORIDE, AMMONIUM CHLORIDE, MES-KOH, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277.K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 87.59650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 200.56750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 200.56750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.79825
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 200.56750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 200.56750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 131.39475
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 200.56750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 200.56750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 43.79825
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 200.56750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 200.56750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 131.39475
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 87.59650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 23-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X, W, B, C, D, E, F, G, H,
REMARK 350 AND CHAINS: I, J, K, L, M, N, O, P, Q,
REMARK 350 AND CHAINS: R, S, T, 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 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 U A 0
REMARK 465 U A 1
REMARK 465 U A 2
REMARK 465 G A 3
REMARK 465 U A 4
REMARK 465 G A 1001A
REMARK 465 G A 1030A
REMARK 465 C A 1030B
REMARK 465 G A 1030C
REMARK 465 A A 1030D
REMARK 465 C A 1361A
REMARK 465 C A 1535
REMARK 465 C A 1536
REMARK 465 U A 1537
REMARK 465 C A 1538
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 VAL B 3
REMARK 465 GLU B 4
REMARK 465 ILE B 5
REMARK 465 THR B 6
REMARK 465 GLU B 241
REMARK 465 ALA B 242
REMARK 465 GLU B 243
REMARK 465 ALA B 244
REMARK 465 THR B 245
REMARK 465 GLU B 246
REMARK 465 THR B 247
REMARK 465 PRO B 248
REMARK 465 GLU B 249
REMARK 465 GLY B 250
REMARK 465 GLU B 251
REMARK 465 SER B 252
REMARK 465 GLU B 253
REMARK 465 VAL B 254
REMARK 465 GLU B 255
REMARK 465 ALA B 256
REMARK 465 MET C 1
REMARK 465 ILE C 208
REMARK 465 GLY C 209
REMARK 465 GLY C 210
REMARK 465 GLN C 211
REMARK 465 LYS C 212
REMARK 465 PRO C 213
REMARK 465 LYS C 214
REMARK 465 ALA C 215
REMARK 465 ARG C 216
REMARK 465 PRO C 217
REMARK 465 GLU C 218
REMARK 465 LEU C 219
REMARK 465 PRO C 220
REMARK 465 LYS C 221
REMARK 465 ALA C 222
REMARK 465 GLU C 223
REMARK 465 GLU C 224
REMARK 465 ARG C 225
REMARK 465 PRO C 226
REMARK 465 ARG C 227
REMARK 465 ARG C 228
REMARK 465 ARG C 229
REMARK 465 ARG C 230
REMARK 465 PRO C 231
REMARK 465 ALA C 232
REMARK 465 VAL C 233
REMARK 465 ARG C 234
REMARK 465 VAL C 235
REMARK 465 LYS C 236
REMARK 465 LYS C 237
REMARK 465 GLU C 238
REMARK 465 GLU C 239
REMARK 465 MET D 1
REMARK 465 MET E 1
REMARK 465 PRO E 2
REMARK 465 GLU E 3
REMARK 465 THR E 4
REMARK 465 GLU E 155
REMARK 465 ALA E 156
REMARK 465 HIS E 157
REMARK 465 ALA E 158
REMARK 465 GLN E 159
REMARK 465 ALA E 160
REMARK 465 GLN E 161
REMARK 465 GLY E 162
REMARK 465 MET G 1
REMARK 465 MET I 1
REMARK 465 MET J 1
REMARK 465 PRO J 2
REMARK 465 VAL J 101
REMARK 465 GLY J 102
REMARK 465 GLY J 103
REMARK 465 GLY J 104
REMARK 465 ARG J 105
REMARK 465 MET K 1
REMARK 465 ALA K 2
REMARK 465 LYS K 3
REMARK 465 LYS K 4
REMARK 465 PRO K 5
REMARK 465 SER K 6
REMARK 465 LYS K 7
REMARK 465 LYS K 8
REMARK 465 LYS K 9
REMARK 465 VAL K 10
REMARK 465 MET L 1
REMARK 465 VAL L 2
REMARK 465 ALA L 3
REMARK 465 LEU L 4
REMARK 465 ALA L 129
REMARK 465 LYS L 130
REMARK 465 THR L 131
REMARK 465 ALA L 132
REMARK 465 ALA L 133
REMARK 465 LYS L 134
REMARK 465 LYS L 135
REMARK 465 MET M 1
REMARK 465 MET N 1
REMARK 465 MET O 1
REMARK 465 ALA P 84
REMARK 465 ARG P 85
REMARK 465 GLU P 86
REMARK 465 GLY P 87
REMARK 465 ALA P 88
REMARK 465 MET Q 1
REMARK 465 MET R 1
REMARK 465 SER R 2
REMARK 465 THR R 3
REMARK 465 LYS R 4
REMARK 465 ASN R 5
REMARK 465 ALA R 6
REMARK 465 LYS R 7
REMARK 465 PRO R 8
REMARK 465 LYS R 9
REMARK 465 LYS R 10
REMARK 465 GLU R 11
REMARK 465 ALA R 12
REMARK 465 GLN R 13
REMARK 465 ARG R 14
REMARK 465 ARG R 15
REMARK 465 MET S 1
REMARK 465 GLY S 82
REMARK 465 HIS S 83
REMARK 465 GLY S 84
REMARK 465 LYS S 85
REMARK 465 GLU S 86
REMARK 465 ALA S 87
REMARK 465 LYS S 88
REMARK 465 ALA S 89
REMARK 465 THR S 90
REMARK 465 LYS S 91
REMARK 465 LYS S 92
REMARK 465 LYS S 93
REMARK 465 MET T 1
REMARK 465 ALA T 2
REMARK 465 GLN T 3
REMARK 465 LYS T 4
REMARK 465 LYS T 5
REMARK 465 PRO T 6
REMARK 465 LYS T 7
REMARK 465 MET V 1
REMARK 465 LYS V 26
REMARK 465 LYS V 27
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 U A 5 P OP1 OP2
REMARK 470 THR J 100 OG1 CG2
REMARK 470 ILE T 41 CD1
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 VAL J 49 O ARG J 60 2.11
REMARK 500 O LEU L 27 N GLY L 29 2.16
REMARK 500 O2' G A 28 OP1 U A 296 2.16
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 NE ARG J 79 NE ARG J 79 8665 2.15
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 A A 60 C2' - C3' - O3' ANGL. DEV. = 12.2 DEGREES
REMARK 500 G A 115 C2' - C3' - O3' ANGL. DEV. = 17.1 DEGREES
REMARK 500 G A 181 C2' - C3' - O3' ANGL. DEV. = 14.3 DEGREES
REMARK 500 C A 188 C2' - C3' - O3' ANGL. DEV. = 12.3 DEGREES
REMARK 500 G A 189 N9 - C1' - C2' ANGL. DEV. = -8.5 DEGREES
REMARK 500 A A 243 C2' - C3' - O3' ANGL. DEV. = 16.1 DEGREES
REMARK 500 G A 266 C2' - C3' - O3' ANGL. DEV. = 10.4 DEGREES
REMARK 500 C A 366 C2' - C3' - O3' ANGL. DEV. = 14.6 DEGREES
REMARK 500 A A 533 C2' - C3' - O3' ANGL. DEV. = 12.4 DEGREES
REMARK 500 A A 559 C2' - C3' - O3' ANGL. DEV. = 15.5 DEGREES
REMARK 500 G A 575 C2' - C3' - O3' ANGL. DEV. = 15.1 DEGREES
REMARK 500 U A 686 N1 - C1' - C2' ANGL. DEV. = 7.9 DEGREES
REMARK 500 G A 760 N9 - C1' - C2' ANGL. DEV. = -7.5 DEGREES
REMARK 500 A A 792 C2' - C3' - O3' ANGL. DEV. = 12.4 DEGREES
REMARK 500 C A 812 C2' - C3' - O3' ANGL. DEV. = 10.7 DEGREES
REMARK 500 U A 960 C2' - C3' - O3' ANGL. DEV. = 10.2 DEGREES
REMARK 500 A A 965 C2' - C3' - O3' ANGL. DEV. = 13.0 DEGREES
REMARK 500 A A1299 N9 - C1' - C2' ANGL. DEV. = 9.1 DEGREES
REMARK 500 U A1498 C2' - C3' - O3' ANGL. DEV. = 18.2 DEGREES
REMARK 500 A A1503 C2' - C3' - O3' ANGL. DEV. = 14.2 DEGREES
REMARK 500 G A1505 C2' - C3' - O3' ANGL. DEV. = 11.9 DEGREES
REMARK 500 U A1528 C2' - C3' - O3' ANGL. DEV. = 14.2 DEGREES
REMARK 500 LEU C 196 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ALA G 147 N - CA - C ANGL. DEV. = -17.1 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 LYS B 8 -95.74 -176.44
REMARK 500 GLU B 9 93.96 42.23
REMARK 500 LEU B 11 65.63 -69.95
REMARK 500 ALA B 13 -7.97 -58.11
REMARK 500 HIS B 16 -160.09 52.49
REMARK 500 PHE B 17 143.06 57.38
REMARK 500 GLU B 20 129.21 58.04
REMARK 500 ARG B 21 -97.73 -26.29
REMARK 500 LYS B 22 14.90 -167.68
REMARK 500 TRP B 24 -156.18 6.34
REMARK 500 LYS B 27 42.51 -63.30
REMARK 500 PHE B 28 2.18 -155.36
REMARK 500 GLU B 52 -70.20 -46.44
REMARK 500 ILE B 58 -71.38 -60.18
REMARK 500 ASP B 60 -84.34 -51.13
REMARK 500 MET B 63 2.44 -69.96
REMARK 500 LYS B 74 108.51 -39.94
REMARK 500 GLN B 76 4.43 -57.71
REMARK 500 ALA B 77 33.26 -176.31
REMARK 500 MET B 83 -76.15 -77.28
REMARK 500 ALA B 88 153.62 137.71
REMARK 500 GLN B 95 -110.75 -59.62
REMARK 500 TRP B 97 92.70 -68.04
REMARK 500 ILE B 108 -17.74 -49.23
REMARK 500 HIS B 113 9.19 -66.75
REMARK 500 LEU B 115 -82.06 -51.53
REMARK 500 GLU B 119 -50.59 -24.42
REMARK 500 ARG B 130 149.14 66.64
REMARK 500 PRO B 131 166.86 -46.32
REMARK 500 LYS B 133 28.32 -74.51
REMARK 500 GLU B 134 -39.01 -167.03
REMARK 500 VAL B 136 -36.70 -131.36
REMARK 500 LEU B 154 -77.33 -56.23
REMARK 500 LEU B 155 106.24 -22.43
REMARK 500 ALA B 161 -169.28 -171.77
REMARK 500 ALA B 177 -71.80 -50.74
REMARK 500 PHE B 181 13.41 57.72
REMARK 500 PRO B 183 152.45 -48.10
REMARK 500 THR B 190 -4.47 -55.77
REMARK 500 PRO B 202 66.02 -58.63
REMARK 500 ALA B 207 102.11 83.32
REMARK 500 SER B 210 -88.58 -95.05
REMARK 500 ILE B 211 -77.19 -13.93
REMARK 500 ASP B 220 45.77 -76.81
REMARK 500 LEU B 221 -18.00 -158.22
REMARK 500 GLN B 224 16.20 -61.39
REMARK 500 VAL B 229 102.74 4.65
REMARK 500 PRO B 232 159.01 -49.67
REMARK 500 ASN C 3 -139.97 -112.58
REMARK 500 LYS C 4 110.87 82.87
REMARK 500
REMARK 500 THIS ENTRY HAS 334 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 U A 37 0.06 SIDE CHAIN
REMARK 500 G A 77 0.05 SIDE CHAIN
REMARK 500 G A 108 0.05 SIDE CHAIN
REMARK 500 G A 189 0.07 SIDE CHAIN
REMARK 500 A A 197 0.07 SIDE CHAIN
REMARK 500 A A 250 0.07 SIDE CHAIN
REMARK 500 G A 251 0.07 SIDE CHAIN
REMARK 500 G A 299 0.07 SIDE CHAIN
REMARK 500 U A 323 0.08 SIDE CHAIN
REMARK 500 G A 380 0.05 SIDE CHAIN
REMARK 500 U A 387 0.07 SIDE CHAIN
REMARK 500 U A 404 0.07 SIDE CHAIN
REMARK 500 A A 460 0.08 SIDE CHAIN
REMARK 500 G A 490 0.06 SIDE CHAIN
REMARK 500 C A 528 0.06 SIDE CHAIN
REMARK 500 C A 554 0.07 SIDE CHAIN
REMARK 500 U A 561 0.10 SIDE CHAIN
REMARK 500 U A 571 0.07 SIDE CHAIN
REMARK 500 A A 572 0.06 SIDE CHAIN
REMARK 500 A A 573 0.06 SIDE CHAIN
REMARK 500 G A 575 0.05 SIDE CHAIN
REMARK 500 U A 580 0.06 SIDE CHAIN
REMARK 500 G A 587 0.06 SIDE CHAIN
REMARK 500 G A 639 0.06 SIDE CHAIN
REMARK 500 G A 727 0.07 SIDE CHAIN
REMARK 500 G A 741 0.05 SIDE CHAIN
REMARK 500 U A 743 0.07 SIDE CHAIN
REMARK 500 C A 879 0.07 SIDE CHAIN
REMARK 500 C A 880 0.06 SIDE CHAIN
REMARK 500 G A 898 0.05 SIDE CHAIN
REMARK 500 G A1077 0.07 SIDE CHAIN
REMARK 500 A A1130 0.07 SIDE CHAIN
REMARK 500 C A1145 0.06 SIDE CHAIN
REMARK 500 A A1299 0.06 SIDE CHAIN
REMARK 500 G A1331 0.06 SIDE CHAIN
REMARK 500 G A1361 0.07 SIDE CHAIN
REMARK 500 G A1370 0.06 SIDE CHAIN
REMARK 500 U A1414 0.09 SIDE CHAIN
REMARK 500 G A1454 0.06 SIDE CHAIN
REMARK 500 U A1498 0.08 SIDE CHAIN
REMARK 500 A A1502 0.06 SIDE CHAIN
REMARK 500 A A1519 0.05 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1632 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 46 O6
REMARK 620 2 G A 394 O6 68.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1626 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 48 OP2
REMARK 620 2 G A 115 OP1 81.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 469 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 59 OP1
REMARK 620 2 U A 387 OP1 81.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 61 O6
REMARK 620 2 U A 62 O4 72.1
REMARK 620 3 G A 105 O6 66.6 70.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 69 O6
REMARK 620 2 G A 70 O6 83.3
REMARK 620 3 U A 98 O4 99.1 75.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 467 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 107 OP1
REMARK 620 2 G A 107 OP2 53.4
REMARK 620 3 A A 325 N7 82.0 134.8
REMARK 620 4 G A 326 O6 91.7 91.3 82.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1600 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 109 OP1
REMARK 620 2 G A 331 OP2 160.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1587 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 116 OP2
REMARK 620 2 A A 116 OP1 51.3
REMARK 620 3 G A 117 OP2 96.1 100.9
REMARK 620 4 G A 289 OP2 77.8 93.1 156.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1598 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 121 N3
REMARK 620 2 C A 121 O2 43.9
REMARK 620 3 G A 124 O6 96.9 85.0
REMARK 620 4 U A 125 O4 158.2 116.2 68.7
REMARK 620 5 G A 126 O6 129.4 137.2 131.2 69.9
REMARK 620 6 G A 236 O6 113.1 147.3 74.2 79.7 73.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1599 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 174 OP1
REMARK 620 2 C A 175 OP2 74.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 210 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 604 O6
REMARK 620 2 U A 605 O4 70.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1572 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 299 O6
REMARK 620 2 G A 558 OP1 124.5
REMARK 620 3 U A 560 OP1 136.6 81.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1627 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 352 O2
REMARK 620 2 G A 357 O6 66.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1631 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 450 OP1
REMARK 620 2 A A 451 O2' 87.9
REMARK 620 3 A A 451 O3' 94.4 57.7
REMARK 620 4 A A 452 OP2 101.6 120.7 63.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 471 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 575 O3'
REMARK 620 2 G A 576 OP1 48.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 473 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A1300 O3'
REMARK 620 2 U A1301 OP1 46.6
REMARK 620 3 U A1301 OP2 54.0 52.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 493 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A1343 OP2
REMARK 620 2 G A1343 O5' 65.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1557 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 509 OP2
REMARK 620 2 A A 510 OP2 91.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1617 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U A 516 O4
REMARK 620 2 A A 533 OP1 139.7
REMARK 620 3 A A 533 OP2 89.9 53.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1597 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 518 N3
REMARK 620 2 G A 529 N7 82.7
REMARK 620 3 G A 529 O6 83.1 64.1
REMARK 620 4 PRO L 48 O 94.1 167.0 103.1
REMARK 620 5 ASN L 49 ND2 148.9 110.6 78.4 66.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1606 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 518 N3
REMARK 620 2 C A 518 O2 43.6
REMARK 620 3 G A 530 O6 86.9 93.1
REMARK 620 4 A W 3 O2' 110.3 152.7 75.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 530 O3'
REMARK 620 2 G A 530 O2' 54.1
REMARK 620 3 C X 35 O2' 154.7 128.9
REMARK 620 4 C X 35 O4' 128.2 85.9 75.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1595 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U A 534 O3'
REMARK 620 2 A A 535 OP1 50.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1592 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 563 O3'
REMARK 620 2 A A 563 O2' 52.0
REMARK 620 3 C A 564 OP2 50.7 97.6
REMARK 620 4 U A 565 OP2 75.4 82.4 102.0
REMARK 620 5 G A 567 OP2 129.6 82.7 179.7 78.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1574 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 572 OP2
REMARK 620 2 A A 573 OP2 82.8
REMARK 620 3 A A 574 OP2 167.9 90.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1561 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 595 O3'
REMARK 620 2 G A 595 O2' 50.3
REMARK 620 3 C A 596 OP2 52.5 97.7
REMARK 620 4 G A 597 OP2 102.5 145.3 72.1
REMARK 620 5 U A 598 O4 133.7 96.0 162.4 90.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1550 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 749 OP2
REMARK 620 2 G A 750 OP2 129.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1590 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 782 OP2
REMARK 620 2 A A 782 OP1 51.3
REMARK 620 3 A A 794 OP2 119.7 169.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1577 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 865 O3'
REMARK 620 2 C A 866 OP1 48.8
REMARK 620 3 G A1079 O6 110.6 159.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1620 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 924 N4
REMARK 620 2 G A 925 O6 65.6
REMARK 620 3 G A 927 O6 125.4 64.0
REMARK 620 4 U A1390 O4 104.3 111.5 76.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1546 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 944 OP1
REMARK 620 2 G A 945 OP2 78.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1568 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 964 OP1
REMARK 620 2 U A1199 OP1 87.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1618 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 972 OP1
REMARK 620 2 LYS J 57 NZ 74.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 449 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 973 OP1
REMARK 620 2 ARG J 60 NH2 129.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1570 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A1053 O2'
REMARK 620 2 C A1054 OP2 95.3
REMARK 620 3 G A1197 OP1 98.9 76.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1571 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A1054 OP1
REMARK 620 2 U A1196 O3' 87.2
REMARK 620 3 G A1197 OP1 74.0 58.1
REMARK 620 4 G A1198 OP2 88.3 118.7 61.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1578 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1067 O3'
REMARK 620 2 G A1068 OP1 55.9
REMARK 620 3 G A1094 OP1 90.4 109.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1610 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A1088 O6
REMARK 620 2 G A1088 N7 75.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1579 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U A1095 OP2
REMARK 620 2 G A1108 O6 87.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1619 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1204 OP1
REMARK 620 2 A A1204 OP2 56.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1611 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1238 OP2
REMARK 620 2 C A1335 O2 60.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1591 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A1303 OP1
REMARK 620 2 G A1304 OP2 85.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1635 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A1401 O3'
REMARK 620 2 G A1401 OP1 103.3
REMARK 620 3 C A1402 OP1 47.8 147.9
REMARK 620 4 C A1402 OP2 53.1 96.0 57.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1582 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1499 O3'
REMARK 620 2 A A1500 OP1 55.3
REMARK 620 3 G A1508 OP1 117.4 62.1
REMARK 620 4 G A1521 OP1 98.5 139.4 130.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1583 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1499 OP2
REMARK 620 2 A A1500 OP2 104.7
REMARK 620 3 G A1504 O2' 158.4 70.0
REMARK 620 4 G A1505 OP2 153.2 91.0 47.9
REMARK 620 5 G A1505 OP1 120.4 55.6 74.8 52.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1584 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1500 OP1
REMARK 620 2 G A1504 O3' 101.0
REMARK 620 3 G A1505 OP1 77.1 53.1
REMARK 620 4 G A1508 OP1 80.2 163.8 141.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 35 N4
REMARK 620 2 G X 36 O6 68.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 306 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 9 SG
REMARK 620 2 CYS D 12 SG 123.5
REMARK 620 3 CYS D 26 SG 98.0 128.0
REMARK 620 4 CYS D 31 SG 97.4 112.8 88.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN N 307 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 24 SG
REMARK 620 2 CYS N 27 SG 102.5
REMARK 620 3 CYS N 40 SG 89.1 107.1
REMARK 620 4 CYS N 43 SG 95.9 160.5 79.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PAR A 1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1556
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1557
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1558
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1560
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1561
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 71
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1564
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1565
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 86
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1568
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1570
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1571
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1572
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1573
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1574
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1575
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1576
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1577
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1578
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1579
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1582
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1583
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1584
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1585
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1586
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1587
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1588
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1590
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1591
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1592
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 214
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1594
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1595
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1596
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1597
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1598
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1599
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1600
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1606
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1607
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1608
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1609
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1610
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1611
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1612
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1613
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1614
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1615
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1616
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1617
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1618
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1619
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1620
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 441
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1621
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 449
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1624
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1625
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1626
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1627
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1628
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1629
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1630
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 466
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1631
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1632
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1633
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 493
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1635
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XMO RELATED DB: PDB
REMARK 900 RELATED ID: 1XMQ RELATED DB: PDB
REMARK 900 RELATED ID: 1IBL RELATED DB: PDB
REMARK 900 RELATED ID: 1IBM RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE RESIDUES G1002 AND G1003; G1031 AND 1032; C1362 AND
REMARK 999 A1363; C1539 AND U1540 IN CHAIN A ARE LINKED TOGETHER WHICH ARE
REMARK 999 SHOWN AS CLOSE CONTACTS AT REMARK 500. THE MISSING RESIDUES
REMARK 999 WITHIN THE LINKS ARE LISTED IN REMARK 465.
DBREF 1XNQ A 0 1521 GB 155076 M26924 646 2167
DBREF 1XNQ B 1 256 UNP P80371 RS2_THETH 0 255
DBREF 1XNQ C 1 239 UNP P80372 RS3_THETH 0 238
DBREF 1XNQ D 1 209 UNP P80373 RS4_THETH 0 208
DBREF 1XNQ E 1 162 UNP P27152 RS5_THETH 0 161
DBREF 1XNQ F 1 101 UNP P23370 RS6_THETH 1 101
DBREF 1XNQ G 1 156 UNP P17291 RS7_THETH 0 155
DBREF 1XNQ H 1 138 UNP P62668 RS8_THET2 1 138
DBREF 1XNQ I 1 128 UNP P80374 RS9_THETH 1 128
DBREF 1XNQ J 1 105 UNP P80375 RS10_THETH 0 104
DBREF 1XNQ K 1 129 UNP P80376 RS11_THETH 0 128
DBREF 1XNQ L 1 135 GB 581812 CAA36418 1 135
DBREF 1XNQ M 1 126 UNP P80377 RS13_THETH 0 125
DBREF 1XNQ N 1 61 UNP P24320 RS14_THETH 0 60
DBREF 1XNQ O 1 89 UNP P80378 RS15_THETH 0 88
DBREF 1XNQ P 1 88 UNP P80379 RS16_THETH 1 88
DBREF 1XNQ Q 1 105 UNP P62658 RS17_THET2 0 104
DBREF 1XNQ R 1 88 UNP P80382 RS18_THETH 0 87
DBREF 1XNQ S 1 93 UNP P80381 RS19_THETH 0 92
DBREF 1XNQ T 1 106 UNP P80380 RS20_THETH 0 105
DBREF 1XNQ V 1 27 UNP P62612 RSHX_THETH 0 26
DBREF 1XNQ X 30 40 PDB 1XNQ 1XNQ 30 40
DBREF 1XNQ W 1 4 PDB 1XNQ 1XNQ 1 4
SEQRES 1 A 1522 U U U G U U G G A G A G U
SEQRES 2 A 1522 U U G A U C C U G G C U C
SEQRES 3 A 1522 A G G G U G A A C G C U G
SEQRES 4 A 1522 G C G G C G U G C C U A A
SEQRES 5 A 1522 G A C A U G C A A G U C G
SEQRES 6 A 1522 U G C G G G C C G C G G G
SEQRES 7 A 1522 G U U U U A C U C C G U G
SEQRES 8 A 1522 G U C A G C G G C G G A C
SEQRES 9 A 1522 G G G U G A G U A A C G C
SEQRES 10 A 1522 G U G G G U G A C C U A C
SEQRES 11 A 1522 C C G G A A G A G G G G G
SEQRES 12 A 1522 A C A A C C C G G G G A A
SEQRES 13 A 1522 A C U C G G G C U A A U C
SEQRES 14 A 1522 C C C C A U G U G G A C C
SEQRES 15 A 1522 C G C C C C U U G G G G U
SEQRES 16 A 1522 G U G U C C A A A G G G C
SEQRES 17 A 1522 U U U G C C C G C U U C C
SEQRES 18 A 1522 G G A U G G G C C C G C G
SEQRES 19 A 1522 U C C C A U C A G C U A G
SEQRES 20 A 1522 U U G G U G G G G U A A U
SEQRES 21 A 1522 G G C C C A C C A A G G C
SEQRES 22 A 1522 G A C G A C G G G U A G C
SEQRES 23 A 1522 C G G U C U G A G A G G A
SEQRES 24 A 1522 U G G C C G G C C A C A G
SEQRES 25 A 1522 G G G C A C U G A G A C A
SEQRES 26 A 1522 C G G G C C C C A C U C C
SEQRES 27 A 1522 U A C G G G A G G C A G C
SEQRES 28 A 1522 A G U U A G G A A U C U U
SEQRES 29 A 1522 C C G C A A U G G G C G C
SEQRES 30 A 1522 A A G C C U G A C G G A G
SEQRES 31 A 1522 C G A C G C C G C U U G G
SEQRES 32 A 1522 A G G A A G A A G C C C U
SEQRES 33 A 1522 U C G G G G U G U A A A C
SEQRES 34 A 1522 U C C U G A A C C C G G G
SEQRES 35 A 1522 A C G A A A C C C C C G A
SEQRES 36 A 1522 C G A G G G G A C U G A C
SEQRES 37 A 1522 G G U A C C G G G G U A A
SEQRES 38 A 1522 U A G C G C C G G C C A A
SEQRES 39 A 1522 C U C C G U G C C A G C A
SEQRES 40 A 1522 G C C G C G G U A A U A C
SEQRES 41 A 1522 G G A G G G C G C G A G C
SEQRES 42 A 1522 G U U A C C C G G A U U C
SEQRES 43 A 1522 A C U G G G C G U A A A G
SEQRES 44 A 1522 G G C G U G U A G G C G G
SEQRES 45 A 1522 C C U G G G G C G U C C C
SEQRES 46 A 1522 A U G U G A A A G A C C A
SEQRES 47 A 1522 C G G C U C A A C C G U G
SEQRES 48 A 1522 G G G G A G C G U G G G A
SEQRES 49 A 1522 U A C G C U C A G G C U A
SEQRES 50 A 1522 G A C G G U G G G A G A G
SEQRES 51 A 1522 G G U G G U G G A A U U C
SEQRES 52 A 1522 C C G G A G U A G C G G U
SEQRES 53 A 1522 G A A A U G C G C A G A U
SEQRES 54 A 1522 A C C G G G A G G A A C G
SEQRES 55 A 1522 C C G A U G G C G A A G G
SEQRES 56 A 1522 C A G C C A C C U G G U C
SEQRES 57 A 1522 C A C C C G U G A C G C U
SEQRES 58 A 1522 G A G G C G C G A A A G C
SEQRES 59 A 1522 G U G G G G A G C A A A C
SEQRES 60 A 1522 C G G A U U A G A U A C C
SEQRES 61 A 1522 C G G G U A G U C C A C G
SEQRES 62 A 1522 C C C U A A A C G A U G C
SEQRES 63 A 1522 G C G C U A G G U C U C U
SEQRES 64 A 1522 G G G U C U C C U G G G G
SEQRES 65 A 1522 G C C G A A G C U A A C G
SEQRES 66 A 1522 C G U U A A G C G C G C C
SEQRES 67 A 1522 G C C U G G G G A G U A C
SEQRES 68 A 1522 G G C C G C A A G G C U G
SEQRES 69 A 1522 A A A C U C A A A G G A A
SEQRES 70 A 1522 U U G A C G G G G G C C C
SEQRES 71 A 1522 G C A C A A G C G G U G G
SEQRES 72 A 1522 A G C A U G U G G U U U A
SEQRES 73 A 1522 A U U C G A A G C A A C G
SEQRES 74 A 1522 C G A A G A A C C U U A C
SEQRES 75 A 1522 C A G G C C U U G A C A U
SEQRES 76 A 1522 G C U A G G G A A C C C G
SEQRES 77 A 1522 G G U G A A A G C C U G G
SEQRES 78 A 1522 G G U G C C C C G C G A G
SEQRES 79 A 1522 G G G A G C C C U A G C A
SEQRES 80 A 1522 C A G G U G C U G C A U G
SEQRES 81 A 1522 G C C G U C G U C A G C U
SEQRES 82 A 1522 C G U G C C G U G A G G U
SEQRES 83 A 1522 G U U G G G U U A A G U C
SEQRES 84 A 1522 C C G C A A C G A G C G C
SEQRES 85 A 1522 A A C C C C C G C C G U U
SEQRES 86 A 1522 A G U U G C C A G C G G U
SEQRES 87 A 1522 U C G G C C G G G C A C U
SEQRES 88 A 1522 C U A A C G G G A C U G C
SEQRES 89 A 1522 C C G C G A A A G C G G G
SEQRES 90 A 1522 A G G A A G G A G G G G A
SEQRES 91 A 1522 C G A C G U C U G G U C A
SEQRES 92 A 1522 G C A U G G C C C U U A C
SEQRES 93 A 1522 G G C C U G G G C G A C A
SEQRES 94 A 1522 C A C G U G C U A C A A U
SEQRES 95 A 1522 G C C C A C U A C A A A G
SEQRES 96 A 1522 C G A U G C C A C C C G G
SEQRES 97 A 1522 C A A C G G G G A G C U A
SEQRES 98 A 1522 A U C G C A A A A A G G U
SEQRES 99 A 1522 G G G C C C A G U U C G G
SEQRES 100 A 1522 A U U G G G G U C U G C A
SEQRES 101 A 1522 A C C C G A C C C C A U G
SEQRES 102 A 1522 A A G C C G G A A U C G C
SEQRES 103 A 1522 U A G U A A U C G C G G A
SEQRES 104 A 1522 U C A G C C A U G C C G C
SEQRES 105 A 1522 G G U G A A U A C G U U C
SEQRES 106 A 1522 C C G G G C C U U G U A C
SEQRES 107 A 1522 A C A C C G C C C G U C A
SEQRES 108 A 1522 C G C C A U G G G A G C G
SEQRES 109 A 1522 G G C U C U A C C C G A A
SEQRES 110 A 1522 G U C G C C G G G A G C C
SEQRES 111 A 1522 U A C G G G C A G G C G C
SEQRES 112 A 1522 C G A G G G U A G G G C C
SEQRES 113 A 1522 C G U G A C U G G G G C G
SEQRES 114 A 1522 A A G U C G U A A C A A G
SEQRES 115 A 1522 G U A G C U G U A C C G G
SEQRES 116 A 1522 A A G G U G C G G C U G G
SEQRES 117 A 1522 A U C A C C U C C U U U C
SEQRES 118 A 1522 U
SEQRES 1 X 11 G G C U I C G A A C C
SEQRES 1 W 4 C G A A
SEQRES 1 B 256 MET PRO VAL GLU ILE THR VAL LYS GLU LEU LEU GLU ALA
SEQRES 2 B 256 GLY VAL HIS PHE GLY HIS GLU ARG LYS ARG TRP ASN PRO
SEQRES 3 B 256 LYS PHE ALA ARG TYR ILE TYR ALA GLU ARG ASN GLY ILE
SEQRES 4 B 256 HIS ILE ILE ASP LEU GLN LYS THR MET GLU GLU LEU GLU
SEQRES 5 B 256 ARG THR PHE ARG PHE ILE GLU ASP LEU ALA MET ARG GLY
SEQRES 6 B 256 GLY THR ILE LEU PHE VAL GLY THR LYS LYS GLN ALA GLN
SEQRES 7 B 256 ASP ILE VAL ARG MET GLU ALA GLU ARG ALA GLY MET PRO
SEQRES 8 B 256 TYR VAL ASN GLN ARG TRP LEU GLY GLY MET LEU THR ASN
SEQRES 9 B 256 PHE LYS THR ILE SER GLN ARG VAL HIS ARG LEU GLU GLU
SEQRES 10 B 256 LEU GLU ALA LEU PHE ALA SER PRO GLU ILE GLU GLU ARG
SEQRES 11 B 256 PRO LYS LYS GLU GLN VAL ARG LEU LYS HIS GLU LEU GLU
SEQRES 12 B 256 ARG LEU GLN LYS TYR LEU SER GLY PHE ARG LEU LEU LYS
SEQRES 13 B 256 ARG LEU PRO ASP ALA ILE PHE VAL VAL ASP PRO THR LYS
SEQRES 14 B 256 GLU ALA ILE ALA VAL ARG GLU ALA ARG LYS LEU PHE ILE
SEQRES 15 B 256 PRO VAL ILE ALA LEU ALA ASP THR ASP SER ASP PRO ASP
SEQRES 16 B 256 LEU VAL ASP TYR ILE ILE PRO GLY ASN ASP ASP ALA ILE
SEQRES 17 B 256 ARG SER ILE GLN LEU ILE LEU SER ARG ALA VAL ASP LEU
SEQRES 18 B 256 ILE ILE GLN ALA ARG GLY GLY VAL VAL GLU PRO SER PRO
SEQRES 19 B 256 SER TYR ALA LEU VAL GLN GLU ALA GLU ALA THR GLU THR
SEQRES 20 B 256 PRO GLU GLY GLU SER GLU VAL GLU ALA
SEQRES 1 C 239 MET GLY ASN LYS ILE HIS PRO ILE GLY PHE ARG LEU GLY
SEQRES 2 C 239 ILE THR ARG ASP TRP GLU SER ARG TRP TYR ALA GLY LYS
SEQRES 3 C 239 LYS GLN TYR ARG HIS LEU LEU LEU GLU ASP GLN ARG ILE
SEQRES 4 C 239 ARG GLY LEU LEU GLU LYS GLU LEU TYR SER ALA GLY LEU
SEQRES 5 C 239 ALA ARG VAL ASP ILE GLU ARG ALA ALA ASP ASN VAL ALA
SEQRES 6 C 239 VAL THR VAL HIS VAL ALA LYS PRO GLY VAL VAL ILE GLY
SEQRES 7 C 239 ARG GLY GLY GLU ARG ILE ARG VAL LEU ARG GLU GLU LEU
SEQRES 8 C 239 ALA LYS LEU THR GLY LYS ASN VAL ALA LEU ASN VAL GLN
SEQRES 9 C 239 GLU VAL GLN ASN PRO ASN LEU SER ALA PRO LEU VAL ALA
SEQRES 10 C 239 GLN ARG VAL ALA GLU GLN ILE GLU ARG ARG PHE ALA VAL
SEQRES 11 C 239 ARG ARG ALA ILE LYS GLN ALA VAL GLN ARG VAL MET GLU
SEQRES 12 C 239 SER GLY ALA LYS GLY ALA LYS VAL ILE VAL SER GLY ARG
SEQRES 13 C 239 ILE GLY GLY ALA GLU GLN ALA ARG THR GLU TRP ALA ALA
SEQRES 14 C 239 GLN GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASN ILE
SEQRES 15 C 239 ASP TYR GLY PHE ALA LEU ALA ARG THR THR TYR GLY VAL
SEQRES 16 C 239 LEU GLY VAL LYS ALA TYR ILE PHE LEU GLY GLU VAL ILE
SEQRES 17 C 239 GLY GLY GLN LYS PRO LYS ALA ARG PRO GLU LEU PRO LYS
SEQRES 18 C 239 ALA GLU GLU ARG PRO ARG ARG ARG ARG PRO ALA VAL ARG
SEQRES 19 C 239 VAL LYS LYS GLU GLU
SEQRES 1 D 209 MET GLY ARG TYR ILE GLY PRO VAL CYS ARG LEU CYS ARG
SEQRES 2 D 209 ARG GLU GLY VAL LYS LEU TYR LEU LYS GLY GLU ARG CYS
SEQRES 3 D 209 TYR SER PRO LYS CYS ALA MET GLU ARG ARG PRO TYR PRO
SEQRES 4 D 209 PRO GLY GLN HIS GLY GLN LYS ARG ALA ARG ARG PRO SER
SEQRES 5 D 209 ASP TYR ALA VAL ARG LEU ARG GLU LYS GLN LYS LEU ARG
SEQRES 6 D 209 ARG ILE TYR GLY ILE SER GLU ARG GLN PHE ARG ASN LEU
SEQRES 7 D 209 PHE GLU GLU ALA SER LYS LYS LYS GLY VAL THR GLY SER
SEQRES 8 D 209 VAL PHE LEU GLY LEU LEU GLU SER ARG LEU ASP ASN VAL
SEQRES 9 D 209 VAL TYR ARG LEU GLY PHE ALA VAL SER ARG ARG GLN ALA
SEQRES 10 D 209 ARG GLN LEU VAL ARG HIS GLY HIS ILE THR VAL ASN GLY
SEQRES 11 D 209 ARG ARG VAL ASP LEU PRO SER TYR ARG VAL ARG PRO GLY
SEQRES 12 D 209 ASP GLU ILE ALA VAL ALA GLU LYS SER ARG ASN LEU GLU
SEQRES 13 D 209 LEU ILE ARG GLN ASN LEU GLU ALA MET LYS GLY ARG LYS
SEQRES 14 D 209 VAL GLY PRO TRP LEU SER LEU ASP VAL GLU GLY MET LYS
SEQRES 15 D 209 GLY LYS PHE LEU ARG LEU PRO ASP ARG GLU ASP LEU ALA
SEQRES 16 D 209 LEU PRO VAL ASN GLU GLN LEU VAL ILE GLU PHE TYR SER
SEQRES 17 D 209 ARG
SEQRES 1 E 162 MET PRO GLU THR ASP PHE GLU GLU LYS MET ILE LEU ILE
SEQRES 2 E 162 ARG ARG THR ALA ARG MET GLN ALA GLY GLY ARG ARG PHE
SEQRES 3 E 162 ARG PHE GLY ALA LEU VAL VAL VAL GLY ASP ARG GLN GLY
SEQRES 4 E 162 ARG VAL GLY LEU GLY PHE GLY LYS ALA PRO GLU VAL PRO
SEQRES 5 E 162 LEU ALA VAL GLN LYS ALA GLY TYR TYR ALA ARG ARG ASN
SEQRES 6 E 162 MET VAL GLU VAL PRO LEU GLN ASN GLY THR ILE PRO HIS
SEQRES 7 E 162 GLU ILE GLU VAL GLU PHE GLY ALA SER LYS ILE VAL LEU
SEQRES 8 E 162 LYS PRO ALA ALA PRO GLY THR GLY VAL ILE ALA GLY ALA
SEQRES 9 E 162 VAL PRO ARG ALA ILE LEU GLU LEU ALA GLY VAL THR ASP
SEQRES 10 E 162 ILE LEU THR LYS GLU LEU GLY SER ARG ASN PRO ILE ASN
SEQRES 11 E 162 ILE ALA TYR ALA THR MET GLU ALA LEU ARG GLN LEU ARG
SEQRES 12 E 162 THR LYS ALA ASP VAL GLU ARG LEU ARG LYS GLY GLU ALA
SEQRES 13 E 162 HIS ALA GLN ALA GLN GLY
SEQRES 1 F 101 MET ARG ARG TYR GLU VAL ASN ILE VAL LEU ASN PRO ASN
SEQRES 2 F 101 LEU ASP GLN SER GLN LEU ALA LEU GLU LYS GLU ILE ILE
SEQRES 3 F 101 GLN ARG ALA LEU GLU ASN TYR GLY ALA ARG VAL GLU LYS
SEQRES 4 F 101 VAL GLU GLU LEU GLY LEU ARG ARG LEU ALA TYR PRO ILE
SEQRES 5 F 101 ALA LYS ASP PRO GLN GLY TYR PHE LEU TRP TYR GLN VAL
SEQRES 6 F 101 GLU MET PRO GLU ASP ARG VAL ASN ASP LEU ALA ARG GLU
SEQRES 7 F 101 LEU ARG ILE ARG ASP ASN VAL ARG ARG VAL MET VAL VAL
SEQRES 8 F 101 LYS SER GLN GLU PRO PHE LEU ALA ASN ALA
SEQRES 1 G 156 MET ALA ARG ARG ARG ARG ALA GLU VAL ARG GLN LEU GLN
SEQRES 2 G 156 PRO ASP LEU VAL TYR GLY ASP VAL LEU VAL THR ALA PHE
SEQRES 3 G 156 ILE ASN LYS ILE MET ARG ASP GLY LYS LYS ASN LEU ALA
SEQRES 4 G 156 ALA ARG ILE PHE TYR ASP ALA CYS LYS ILE ILE GLN GLU
SEQRES 5 G 156 LYS THR GLY GLN GLU PRO LEU LYS VAL PHE LYS GLN ALA
SEQRES 6 G 156 VAL GLU ASN VAL LYS PRO ARG MET GLU VAL ARG SER ARG
SEQRES 7 G 156 ARG VAL GLY GLY ALA ASN TYR GLN VAL PRO MET GLU VAL
SEQRES 8 G 156 SER PRO ARG ARG GLN GLN SER LEU ALA LEU ARG TRP LEU
SEQRES 9 G 156 VAL GLN ALA ALA ASN GLN ARG PRO GLU ARG ARG ALA ALA
SEQRES 10 G 156 VAL ARG ILE ALA HIS GLU LEU MET ASP ALA ALA GLU GLY
SEQRES 11 G 156 LYS GLY GLY ALA VAL LYS LYS LYS GLU ASP VAL GLU ARG
SEQRES 12 G 156 MET ALA GLU ALA ASN ARG ALA TYR ALA HIS TYR ARG TRP
SEQRES 1 H 138 MET LEU THR ASP PRO ILE ALA ASP MET LEU THR ARG ILE
SEQRES 2 H 138 ARG ASN ALA THR ARG VAL TYR LYS GLU SER THR ASP VAL
SEQRES 3 H 138 PRO ALA SER ARG PHE LYS GLU GLU ILE LEU ARG ILE LEU
SEQRES 4 H 138 ALA ARG GLU GLY PHE ILE LYS GLY TYR GLU ARG VAL ASP
SEQRES 5 H 138 VAL ASP GLY LYS PRO TYR LEU ARG VAL TYR LEU LYS TYR
SEQRES 6 H 138 GLY PRO ARG ARG GLN GLY PRO ASP PRO ARG PRO GLU GLN
SEQRES 7 H 138 VAL ILE HIS HIS ILE ARG ARG ILE SER LYS PRO GLY ARG
SEQRES 8 H 138 ARG VAL TYR VAL GLY VAL LYS GLU ILE PRO ARG VAL ARG
SEQRES 9 H 138 ARG GLY LEU GLY ILE ALA ILE LEU SER THR SER LYS GLY
SEQRES 10 H 138 VAL LEU THR ASP ARG GLU ALA ARG LYS LEU GLY VAL GLY
SEQRES 11 H 138 GLY GLU LEU ILE CYS GLU VAL TRP
SEQRES 1 I 128 MET GLU GLN TYR TYR GLY THR GLY ARG ARG LYS GLU ALA
SEQRES 2 I 128 VAL ALA ARG VAL PHE LEU ARG PRO GLY ASN GLY LYS VAL
SEQRES 3 I 128 THR VAL ASN GLY GLN ASP PHE ASN GLU TYR PHE GLN GLY
SEQRES 4 I 128 LEU VAL ARG ALA VAL ALA ALA LEU GLU PRO LEU ARG ALA
SEQRES 5 I 128 VAL ASP ALA LEU GLY ARG PHE ASP ALA TYR ILE THR VAL
SEQRES 6 I 128 ARG GLY GLY GLY LYS SER GLY GLN ILE ASP ALA ILE LYS
SEQRES 7 I 128 LEU GLY ILE ALA ARG ALA LEU VAL GLN TYR ASN PRO ASP
SEQRES 8 I 128 TYR ARG ALA LYS LEU LYS PRO LEU GLY PHE LEU THR ARG
SEQRES 9 I 128 ASP ALA ARG VAL VAL GLU ARG LYS LYS TYR GLY LYS HIS
SEQRES 10 I 128 LYS ALA ARG ARG ALA PRO GLN TYR SER LYS ARG
SEQRES 1 J 105 MET PRO LYS ILE ARG ILE LYS LEU ARG GLY PHE ASP HIS
SEQRES 2 J 105 LYS THR LEU ASP ALA SER ALA GLN LYS ILE VAL GLU ALA
SEQRES 3 J 105 ALA ARG ARG SER GLY ALA GLN VAL SER GLY PRO ILE PRO
SEQRES 4 J 105 LEU PRO THR ARG VAL ARG ARG PHE THR VAL ILE ARG GLY
SEQRES 5 J 105 PRO PHE LYS HIS LYS ASP SER ARG GLU HIS PHE GLU LEU
SEQRES 6 J 105 ARG THR HIS ASN ARG LEU VAL ASP ILE ILE ASN PRO ASN
SEQRES 7 J 105 ARG LYS THR ILE GLU GLN LEU MET THR LEU ASP LEU PRO
SEQRES 8 J 105 THR GLY VAL GLU ILE GLU ILE LYS THR VAL GLY GLY GLY
SEQRES 9 J 105 ARG
SEQRES 1 K 129 MET ALA LYS LYS PRO SER LYS LYS LYS VAL LYS ARG GLN
SEQRES 2 K 129 VAL ALA SER GLY ARG ALA TYR ILE HIS ALA SER TYR ASN
SEQRES 3 K 129 ASN THR ILE VAL THR ILE THR ASP PRO ASP GLY ASN PRO
SEQRES 4 K 129 ILE THR TRP SER SER GLY GLY VAL ILE GLY TYR LYS GLY
SEQRES 5 K 129 SER ARG LYS GLY THR PRO TYR ALA ALA GLN LEU ALA ALA
SEQRES 6 K 129 LEU ASP ALA ALA LYS LYS ALA MET ALA TYR GLY MET GLN
SEQRES 7 K 129 SER VAL ASP VAL ILE VAL ARG GLY THR GLY ALA GLY ARG
SEQRES 8 K 129 GLU GLN ALA ILE ARG ALA LEU GLN ALA SER GLY LEU GLN
SEQRES 9 K 129 VAL LYS SER ILE VAL ASP ASP THR PRO VAL PRO HIS ASN
SEQRES 10 K 129 GLY CYS ARG PRO LYS LYS LYS PHE ARG LYS ALA SER
SEQRES 1 L 135 MET VAL ALA LEU PRO THR ILE ASN GLN LEU VAL ARG LYS
SEQRES 2 L 135 GLY ARG GLU LYS VAL ARG LYS LYS SER LYS VAL PRO ALA
SEQRES 3 L 135 LEU LYS GLY ALA PRO PHE ARG ARG GLY VAL CYS THR VAL
SEQRES 4 L 135 VAL ARG THR VAL THR PRO LYS LYS PRO ASN SER ALA LEU
SEQRES 5 L 135 ARG LYS VAL ALA LYS VAL ARG LEU THR SER GLY TYR GLU
SEQRES 6 L 135 VAL THR ALA TYR ILE PRO GLY GLU GLY HIS ASN LEU GLN
SEQRES 7 L 135 GLU HIS SER VAL VAL LEU ILE ARG GLY GLY ARG VAL LYS
SEQRES 8 L 135 ASP LEU PRO GLY VAL ARG TYR HIS ILE VAL ARG GLY VAL
SEQRES 9 L 135 TYR ASP ALA ALA GLY VAL LYS ASP ARG LYS LYS SER ARG
SEQRES 10 L 135 SER LYS TYR GLY THR LYS LYS PRO LYS GLU ALA ALA LYS
SEQRES 11 L 135 THR ALA ALA LYS LYS
SEQRES 1 M 126 MET ALA ARG ILE ALA GLY VAL GLU ILE PRO ARG ASN LYS
SEQRES 2 M 126 ARG VAL ASP VAL ALA LEU THR TYR ILE TYR GLY ILE GLY
SEQRES 3 M 126 LYS ALA ARG ALA LYS GLU ALA LEU GLU LYS THR GLY ILE
SEQRES 4 M 126 ASN PRO ALA THR ARG VAL LYS ASP LEU THR GLU ALA GLU
SEQRES 5 M 126 VAL VAL ARG LEU ARG GLU TYR VAL GLU ASN THR TRP LYS
SEQRES 6 M 126 LEU GLU GLY GLU LEU ARG ALA GLU VAL ALA ALA ASN ILE
SEQRES 7 M 126 LYS ARG LEU MET ASP ILE GLY CYS TYR ARG GLY LEU ARG
SEQRES 8 M 126 HIS ARG ARG GLY LEU PRO VAL ARG GLY GLN ARG THR ARG
SEQRES 9 M 126 THR ASN ALA ARG THR ARG LYS GLY PRO ARG LYS THR VAL
SEQRES 10 M 126 ALA GLY LYS LYS LYS ALA PRO ARG LYS
SEQRES 1 N 61 MET ALA ARG LYS ALA LEU ILE GLU LYS ALA LYS ARG THR
SEQRES 2 N 61 PRO LYS PHE LYS VAL ARG ALA TYR THR ARG CYS VAL ARG
SEQRES 3 N 61 CYS GLY ARG ALA ARG SER VAL TYR ARG PHE PHE GLY LEU
SEQRES 4 N 61 CYS ARG ILE CYS LEU ARG GLU LEU ALA HIS LYS GLY GLN
SEQRES 5 N 61 LEU PRO GLY VAL ARG LYS ALA SER TRP
SEQRES 1 O 89 MET PRO ILE THR LYS GLU GLU LYS GLN LYS VAL ILE GLN
SEQRES 2 O 89 GLU PHE ALA ARG PHE PRO GLY ASP THR GLY SER THR GLU
SEQRES 3 O 89 VAL GLN VAL ALA LEU LEU THR LEU ARG ILE ASN ARG LEU
SEQRES 4 O 89 SER GLU HIS LEU LYS VAL HIS LYS LYS ASP HIS HIS SER
SEQRES 5 O 89 HIS ARG GLY LEU LEU MET MET VAL GLY GLN ARG ARG ARG
SEQRES 6 O 89 LEU LEU ARG TYR LEU GLN ARG GLU ASP PRO GLU ARG TYR
SEQRES 7 O 89 ARG ALA LEU ILE GLU LYS LEU GLY ILE ARG GLY
SEQRES 1 P 88 MET VAL LYS ILE ARG LEU ALA ARG PHE GLY SER LYS HIS
SEQRES 2 P 88 ASN PRO HIS TYR ARG ILE VAL VAL THR ASP ALA ARG ARG
SEQRES 3 P 88 LYS ARG ASP GLY LYS TYR ILE GLU LYS ILE GLY TYR TYR
SEQRES 4 P 88 ASP PRO ARG LYS THR THR PRO ASP TRP LEU LYS VAL ASP
SEQRES 5 P 88 VAL GLU ARG ALA ARG TYR TRP LEU SER VAL GLY ALA GLN
SEQRES 6 P 88 PRO THR ASP THR ALA ARG ARG LEU LEU ARG GLN ALA GLY
SEQRES 7 P 88 VAL PHE ARG GLN GLU ALA ARG GLU GLY ALA
SEQRES 1 Q 105 MET PRO LYS LYS VAL LEU THR GLY VAL VAL VAL SER ASP
SEQRES 2 Q 105 LYS MET GLN LYS THR VAL THR VAL LEU VAL GLU ARG GLN
SEQRES 3 Q 105 PHE PRO HIS PRO LEU TYR GLY LYS VAL ILE LYS ARG SER
SEQRES 4 Q 105 LYS LYS TYR LEU ALA HIS ASP PRO GLU GLU LYS TYR LYS
SEQRES 5 Q 105 LEU GLY ASP VAL VAL GLU ILE ILE GLU SER ARG PRO ILE
SEQRES 6 Q 105 SER LYS ARG LYS ARG PHE ARG VAL LEU ARG LEU VAL GLU
SEQRES 7 Q 105 SER GLY ARG MET ASP LEU VAL GLU LYS TYR LEU ILE ARG
SEQRES 8 Q 105 ARG GLN ASN TYR GLN SER LEU SER LYS ARG GLY GLY LYS
SEQRES 9 Q 105 ALA
SEQRES 1 R 88 MET SER THR LYS ASN ALA LYS PRO LYS LYS GLU ALA GLN
SEQRES 2 R 88 ARG ARG PRO SER ARG LYS ALA LYS VAL LYS ALA THR LEU
SEQRES 3 R 88 GLY GLU PHE ASP LEU ARG ASP TYR ARG ASN VAL GLU VAL
SEQRES 4 R 88 LEU LYS ARG PHE LEU SER GLU THR GLY LYS ILE LEU PRO
SEQRES 5 R 88 ARG ARG ARG THR GLY LEU SER GLY LYS GLU GLN ARG ILE
SEQRES 6 R 88 LEU ALA LYS THR ILE LYS ARG ALA ARG ILE LEU GLY LEU
SEQRES 7 R 88 LEU PRO PHE THR GLU LYS LEU VAL ARG LYS
SEQRES 1 S 93 MET PRO ARG SER LEU LYS LYS GLY VAL PHE VAL ASP ASP
SEQRES 2 S 93 HIS LEU LEU GLU LYS VAL LEU GLU LEU ASN ALA LYS GLY
SEQRES 3 S 93 GLU LYS ARG LEU ILE LYS THR TRP SER ARG ARG SER THR
SEQRES 4 S 93 ILE VAL PRO GLU MET VAL GLY HIS THR ILE ALA VAL TYR
SEQRES 5 S 93 ASN GLY LYS GLN HIS VAL PRO VAL TYR ILE THR GLU ASN
SEQRES 6 S 93 MET VAL GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG
SEQRES 7 S 93 THR TYR ARG GLY HIS GLY LYS GLU ALA LYS ALA THR LYS
SEQRES 8 S 93 LYS LYS
SEQRES 1 T 106 MET ALA GLN LYS LYS PRO LYS ARG ASN LEU SER ALA LEU
SEQRES 2 T 106 LYS ARG HIS ARG GLN SER LEU LYS ARG ARG LEU ARG ASN
SEQRES 3 T 106 LYS ALA LYS LYS SER ALA ILE LYS THR LEU SER LYS LYS
SEQRES 4 T 106 ALA ILE GLN LEU ALA GLN GLU GLY LYS ALA GLU GLU ALA
SEQRES 5 T 106 LEU LYS ILE MET ARG LYS ALA GLU SER LEU ILE ASP LYS
SEQRES 6 T 106 ALA ALA LYS GLY SER THR LEU HIS LYS ASN ALA ALA ALA
SEQRES 7 T 106 ARG ARG LYS SER ARG LEU MET ARG LYS VAL ARG GLN LEU
SEQRES 8 T 106 LEU GLU ALA ALA GLY ALA PRO LEU ILE GLY GLY GLY LEU
SEQRES 9 T 106 SER ALA
SEQRES 1 V 27 MET GLY LYS GLY ASP ARG ARG THR ARG ARG GLY LYS ILE
SEQRES 2 V 27 TRP ARG GLY THR TYR GLY LYS TYR ARG PRO ARG LYS LYS
SEQRES 3 V 27 LYS
HET PAR A1545 42
HET MG A1546 1
HET MG A1547 1
HET MG A1548 1
HET MG A1549 1
HET MG A1550 1
HET MG A1551 1
HET MG A1552 1
HET MG A1553 1
HET MG A1554 1
HET MG A1555 1
HET MG A1556 1
HET MG A1557 1
HET MG A1558 1
HET MG A1559 1
HET MG A1560 1
HET MG A1561 1
HET MG A1562 1
HET MG A1563 1
HET MG A 71 1
HET MG A1564 1
HET MG A1565 1
HET MG A1566 1
HET MG A1567 1
HET MG A 86 1
HET MG A 87 1
HET MG A1568 1
HET MG A1569 1
HET MG A1570 1
HET MG A1571 1
HET MG A1572 1
HET MG A1573 1
HET MG A1574 1
HET MG A1575 1
HET MG A1576 1
HET MG A1577 1
HET MG A1578 1
HET MG A1579 1
HET MG A1580 1
HET MG A1581 1
HET MG A1582 1
HET MG A1583 1
HET MG A1584 1
HET MG A1585 1
HET MG A1586 1
HET MG A1587 1
HET MG A1588 1
HET MG A1589 1
HET MG A1590 1
HET MG A1591 1
HET MG A1592 1
HET MG A 210 1
HET MG A 211 1
HET MG A 214 1
HET MG A1593 1
HET MG A1594 1
HET MG A1595 1
HET MG A1596 1
HET MG A1597 1
HET MG A1598 1
HET MG A1599 1
HET MG A1600 1
HET MG A1601 1
HET MG A1602 1
HET MG A1603 1
HET MG A1604 1
HET MG A1605 1
HET MG A1606 1
HET MG A1607 1
HET MG A1608 1
HET MG A1609 1
HET MG A1610 1
HET MG A1611 1
HET MG A1612 1
HET MG A1613 1
HET MG A1614 1
HET MG A1615 1
HET MG A1616 1
HET MG A1617 1
HET MG A1618 1
HET MG A1619 1
HET MG A1620 1
HET MG A 441 1
HET MG A1621 1
HET MG A1622 1
HET MG A1623 1
HET MG A1624 1
HET MG A1625 1
HET MG A1626 1
HET MG A1627 1
HET MG A1628 1
HET MG A1629 1
HET MG A1630 1
HET MG A 466 1
HET MG A 467 1
HET MG A 469 1
HET MG A 470 1
HET MG A 471 1
HET MG A 473 1
HET MG A1631 1
HET MG A1632 1
HET MG A1633 1
HET MG A1634 1
HET MG A 493 1
HET MG A1635 1
HET MG X 500 1
HET MG X 502 1
HET ZN D 306 1
HET MG J 449 1
HET ZN N 307 1
HETNAM PAR PAROMOMYCIN
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETSYN PAR PAROMOMYCIN I; AMMINOSIDIN; CATENULIN; CRESTOMYCIN;
HETSYN 2 PAR MONOMYCIN A; NEOMYCIN E
FORMUL 24 PAR C23 H45 N5 O14
FORMUL 25 MG 107(MG 2+)
FORMUL 31 ZN 2(ZN 2+)
HELIX 1 1 LEU B 11 VAL B 15 5 5
HELIX 2 2 PHE B 28 ARG B 30 5 3
HELIX 3 3 ASP B 43 ARG B 64 1 22
HELIX 4 4 LYS B 74 GLN B 78 5 5
HELIX 5 5 ASP B 79 ARG B 87 1 9
HELIX 6 6 ASN B 104 PHE B 122 1 19
HELIX 7 7 PRO B 125 GLU B 129 5 5
HELIX 8 8 PRO B 131 VAL B 136 1 6
HELIX 9 9 LEU B 138 LEU B 149 1 12
HELIX 10 10 GLU B 170 LEU B 180 1 11
HELIX 11 11 ASP B 193 VAL B 197 5 5
HELIX 12 12 ALA B 207 ALA B 218 1 12
HELIX 13 13 SER B 233 GLN B 240 5 8
HELIX 14 14 ILE C 8 LEU C 12 5 5
HELIX 15 15 GLN C 28 LEU C 47 1 20
HELIX 16 16 LYS C 72 GLY C 78 1 7
HELIX 17 17 VAL C 86 THR C 95 1 10
HELIX 18 18 ASN C 108 LEU C 111 5 4
HELIX 19 19 SER C 112 ARG C 126 1 15
HELIX 20 20 ALA C 129 SER C 144 1 16
HELIX 21 21 ARG C 156 ALA C 160 5 5
HELIX 22 22 ARG D 10 GLY D 16 1 7
HELIX 23 23 SER D 52 TYR D 68 1 17
HELIX 24 24 SER D 71 LYS D 85 1 15
HELIX 25 25 VAL D 88 SER D 99 1 12
HELIX 26 26 ARG D 100 LEU D 108 1 9
HELIX 27 27 SER D 113 HIS D 123 1 11
HELIX 28 28 GLU D 150 ARG D 153 5 4
HELIX 29 29 LEU D 155 ALA D 164 1 10
HELIX 30 30 ASP D 190 LEU D 194 5 5
HELIX 31 31 ASN D 199 ARG D 209 1 11
HELIX 32 32 GLU E 50 ARG E 64 1 15
HELIX 33 33 GLY E 103 LEU E 112 1 10
HELIX 34 34 ASN E 127 LEU E 142 1 16
HELIX 35 35 THR E 144 LYS E 153 1 10
HELIX 36 36 ASP F 15 TYR F 33 1 19
HELIX 37 37 PRO F 68 ILE F 81 1 14
HELIX 38 38 ASP G 20 MET G 31 1 12
HELIX 39 39 LYS G 35 GLU G 52 1 18
HELIX 40 40 GLU G 57 LYS G 70 1 14
HELIX 41 41 SER G 92 ASN G 109 1 18
HELIX 42 42 ARG G 115 GLY G 130 1 16
HELIX 43 43 LYS G 131 ALA G 145 1 15
HELIX 44 44 ASN G 148 ALA G 152 5 5
HELIX 45 45 ASP H 4 VAL H 19 1 16
HELIX 46 46 SER H 29 GLU H 42 1 14
HELIX 47 47 GLY H 96 ILE H 100 5 5
HELIX 48 48 THR H 120 LEU H 127 1 8
HELIX 49 49 ASP I 32 PHE I 37 1 6
HELIX 50 50 LEU I 40 ALA I 46 5 7
HELIX 51 51 LEU I 47 ALA I 52 1 6
HELIX 52 52 GLY I 69 ASN I 89 1 21
HELIX 53 53 TYR I 92 LYS I 97 1 6
HELIX 54 54 LYS J 80 LEU J 85 1 6
HELIX 55 55 GLY K 45 GLY K 49 1 5
HELIX 56 56 SER K 53 GLY K 56 5 4
HELIX 57 57 THR K 57 TYR K 75 1 19
HELIX 58 58 GLY K 90 ALA K 100 1 11
HELIX 59 59 LYS K 122 ARG K 126 5 5
HELIX 60 60 THR L 6 LYS L 13 1 8
HELIX 61 61 SER L 118 THR L 122 5 5
HELIX 62 62 ARG M 14 THR M 20 1 7
HELIX 63 63 LYS M 27 THR M 37 1 11
HELIX 64 64 ARG M 44 LEU M 48 5 5
HELIX 65 65 ALA M 51 ASN M 62 1 12
HELIX 66 66 LEU M 66 ILE M 84 1 19
HELIX 67 67 CYS M 86 GLY M 95 1 10
HELIX 68 68 ALA M 107 GLY M 112 1 6
HELIX 69 69 ARG N 3 LYS N 11 5 9
HELIX 70 70 CYS N 40 GLY N 51 1 12
HELIX 71 71 THR O 4 ALA O 16 1 13
HELIX 72 72 SER O 24 HIS O 46 1 23
HELIX 73 73 ASP O 49 ASP O 74 1 26
HELIX 74 74 ASP O 74 LEU O 85 1 12
HELIX 75 75 ASP P 52 SER P 61 1 10
HELIX 76 76 THR P 67 ALA P 77 1 11
HELIX 77 77 ARG Q 81 ASN Q 94 1 14
HELIX 78 78 TYR Q 95 SER Q 97 5 3
HELIX 79 79 ASN R 36 LYS R 41 1 6
HELIX 80 80 ARG R 42 LEU R 44 5 3
HELIX 81 81 PRO R 52 GLY R 57 1 6
HELIX 82 82 SER R 59 GLY R 77 1 19
HELIX 83 83 ASP S 12 ASN S 23 1 12
HELIX 84 84 VAL S 41 VAL S 45 5 5
HELIX 85 85 THR S 63 VAL S 67 5 5
HELIX 86 86 LYS S 70 ALA S 75 5 6
HELIX 87 87 LEU T 13 GLU T 46 1 34
HELIX 88 88 LYS T 48 ALA T 67 1 20
HELIX 89 89 HIS T 73 ALA T 94 1 22
HELIX 90 90 THR V 8 ARG V 15 1 8
SHEET 1 A 2 ILE B 32 ARG B 36 0
SHEET 2 A 2 ILE B 39 ILE B 42 -1 O ILE B 41 N ALA B 34
SHEET 1 B 5 TYR B 92 VAL B 93 0
SHEET 2 B 5 ILE B 68 VAL B 71 1 N PHE B 70 O VAL B 93
SHEET 3 B 5 ALA B 161 VAL B 164 1 O PHE B 163 N LEU B 69
SHEET 4 B 5 ILE B 185 LEU B 187 1 O ILE B 185 N ILE B 162
SHEET 5 B 5 TYR B 199 ILE B 201 1 O ILE B 201 N ALA B 186
SHEET 1 C 2 HIS C 69 VAL C 70 0
SHEET 2 C 2 GLN C 104 GLU C 105 1 O GLN C 104 N VAL C 70
SHEET 1 D 4 ALA C 169 GLY C 171 0
SHEET 2 D 4 GLY C 148 VAL C 153 -1 N ALA C 149 O GLN C 170
SHEET 3 D 4 VAL C 198 PHE C 203 -1 O PHE C 203 N GLY C 148
SHEET 4 D 4 ASP C 183 ALA C 187 -1 N ALA C 187 O VAL C 198
SHEET 1 E 3 ARG D 131 ARG D 132 0
SHEET 2 E 3 ILE D 126 VAL D 128 -1 N VAL D 128 O ARG D 131
SHEET 3 E 3 ILE D 146 VAL D 148 -1 O ALA D 147 N THR D 127
SHEET 1 F 4 GLU E 7 ARG E 14 0
SHEET 2 F 4 GLY E 29 GLY E 35 -1 O VAL E 33 N LYS E 9
SHEET 3 F 4 ARG E 40 LYS E 47 -1 O GLY E 44 N VAL E 32
SHEET 4 F 4 MET E 66 GLU E 68 -1 O VAL E 67 N VAL E 41
SHEET 1 G 2 ALA E 17 GLN E 20 0
SHEET 2 G 2 GLY E 23 PHE E 26 -1 O ARG E 25 N ARG E 18
SHEET 1 H 4 ILE E 80 PHE E 84 0
SHEET 2 H 4 SER E 87 PRO E 93 -1 O SER E 87 N PHE E 84
SHEET 3 H 4 ILE E 118 GLY E 124 -1 O LEU E 119 N LYS E 92
SHEET 4 H 4 VAL E 100 ILE E 101 1 N ILE E 101 O ILE E 118
SHEET 1 I 5 ARG F 36 VAL F 37 0
SHEET 2 I 5 VAL F 65 MET F 67 -1 O GLU F 66 N ARG F 36
SHEET 3 I 5 ARG F 2 LEU F 10 -1 N TYR F 4 O VAL F 65
SHEET 4 I 5 ASP F 55 TRP F 62 -1 O LEU F 61 N ILE F 8
SHEET 5 I 5 GLU F 41 ILE F 52 -1 N ARG F 46 O GLY F 58
SHEET 1 J 4 ARG F 36 VAL F 37 0
SHEET 2 J 4 VAL F 65 MET F 67 -1 O GLU F 66 N ARG F 36
SHEET 3 J 4 ARG F 2 LEU F 10 -1 N TYR F 4 O VAL F 65
SHEET 4 J 4 VAL F 85 LYS F 92 -1 O ARG F 86 N VAL F 9
SHEET 1 K 2 LEU F 98 ALA F 99 0
SHEET 2 K 2 PHE R 29 ASP R 30 -1 O PHE R 29 N ALA F 99
SHEET 1 L 2 MET G 73 ARG G 76 0
SHEET 2 L 2 VAL G 87 GLU G 90 -1 O VAL G 87 N ARG G 76
SHEET 1 M 2 GLY H 47 GLU H 49 0
SHEET 2 M 2 ARG H 60 TYR H 62 -1 O TYR H 62 N GLY H 47
SHEET 1 N 2 ASP H 52 VAL H 53 0
SHEET 2 N 2 LYS H 56 PRO H 57 -1 O LYS H 56 N VAL H 53
SHEET 1 O 2 ILE H 83 ARG H 85 0
SHEET 2 O 2 CYS H 135 VAL H 137 -1 O GLU H 136 N ARG H 84
SHEET 1 P 2 TYR H 94 VAL H 95 0
SHEET 2 P 2 GLY H 131 GLU H 132 -1 O GLY H 131 N VAL H 95
SHEET 1 Q 2 LEU H 112 THR H 114 0
SHEET 2 Q 2 GLY H 117 LEU H 119 -1 O LEU H 119 N LEU H 112
SHEET 1 R 4 TYR I 5 GLY I 6 0
SHEET 2 R 4 VAL I 14 LEU I 19 -1 O VAL I 17 N GLY I 6
SHEET 3 R 4 ALA I 61 ARG I 66 -1 O THR I 64 N ARG I 16
SHEET 4 R 4 VAL I 26 VAL I 28 1 N THR I 27 O ALA I 61
SHEET 1 S 2 ILE J 6 LYS J 7 0
SHEET 2 S 2 GLU J 97 ILE J 98 -1 O GLU J 97 N LYS J 7
SHEET 1 T 3 ARG J 46 THR J 48 0
SHEET 2 T 3 HIS J 62 GLU J 64 -1 O PHE J 63 N PHE J 47
SHEET 3 T 3 ARG N 57 LYS N 58 -1 O ARG N 57 N GLU J 64
SHEET 1 U 5 PRO K 39 SER K 44 0
SHEET 2 U 5 THR K 28 THR K 33 -1 N ILE K 32 O ILE K 40
SHEET 3 U 5 GLY K 17 ALA K 23 -1 N TYR K 20 O THR K 31
SHEET 4 U 5 SER K 79 ARG K 85 1 O ILE K 83 N ALA K 19
SHEET 5 U 5 GLN K 104 VAL K 105 1 O GLN K 104 N VAL K 80
SHEET 1 V 2 VAL K 109 ASP K 110 0
SHEET 2 V 2 LEU R 85 VAL R 86 -1 O LEU R 85 N ASP K 110
SHEET 1 W 7 THR L 42 VAL L 43 0
SHEET 2 W 7 ARG L 53 LEU L 60 -1 O ARG L 53 N VAL L 43
SHEET 3 W 7 TYR L 64 TYR L 69 -1 O ALA L 68 N ALA L 56
SHEET 4 W 7 TYR L 98 ILE L 100 1 O TYR L 98 N TYR L 69
SHEET 5 W 7 VAL L 82 GLY L 87 -1 N ARG L 86 O HIS L 99
SHEET 6 W 7 PHE L 32 CYS L 37 -1 N GLY L 35 O VAL L 83
SHEET 7 W 7 ARG L 53 LEU L 60 -1 O ARG L 59 N VAL L 36
SHEET 1 X 5 LEU P 49 VAL P 51 0
SHEET 2 X 5 GLU P 34 TYR P 39 -1 N TYR P 38 O LYS P 50
SHEET 3 X 5 TYR P 17 ASP P 23 -1 N VAL P 21 O GLU P 34
SHEET 4 X 5 VAL P 2 ARG P 8 -1 N ARG P 5 O VAL P 20
SHEET 5 X 5 GLN P 65 PRO P 66 1 O GLN P 65 N VAL P 2
SHEET 1 Y 6 VAL Q 5 MET Q 15 0
SHEET 2 Y 6 THR Q 18 PRO Q 28 -1 O LEU Q 22 N VAL Q 9
SHEET 3 Y 6 VAL Q 35 HIS Q 45 -1 O ILE Q 36 N PHE Q 27
SHEET 4 Y 6 PHE Q 71 GLU Q 78 1 O PHE Q 71 N HIS Q 45
SHEET 5 Y 6 VAL Q 56 GLU Q 61 -1 N VAL Q 56 O VAL Q 77
SHEET 6 Y 6 VAL Q 5 MET Q 15 -1 N LEU Q 6 O ILE Q 59
SHEET 1 Z 2 ALA S 50 TYR S 52 0
SHEET 2 Z 2 HIS S 57 PRO S 59 -1 O VAL S 58 N VAL S 51
SSBOND 1 CYS N 40 CYS N 43 1555 1555 2.93
LINK OP2 U A 17 MG MG A1548 1555 1555 3.11
LINK OP1 G A 21 MG MG A1560 1555 1555 2.01
LINK O6 G A 46 MG MG A1632 1555 1555 2.66
LINK OP2 C A 48 MG MG A1626 1555 1555 1.93
LINK OP2 A A 53 MG MG A1625 1555 1555 2.04
LINK OP1 A A 59 MG MG A 469 1555 1555 1.99
LINK O6 G A 61 MG MG A1602 1555 1555 3.07
LINK O4 U A 62 MG MG A1602 1555 1555 2.86
LINK O6 G A 69 MG MG A1601 1555 1555 2.75
LINK O6 G A 70 MG MG A1601 1555 1555 2.43
LINK MG MG A 71 OP2 A A 860 1555 1555 2.17
LINK MG MG A 86 OP2 G A 588 1555 1555 2.01
LINK O4 U A 98 MG MG A1601 1555 1555 2.70
LINK O6 G A 105 MG MG A1602 1555 1555 2.78
LINK OP1 G A 107 MG MG A 467 1555 1555 3.14
LINK OP2 G A 107 MG MG A 467 1555 1555 2.31
LINK OP1 A A 109 MG MG A1600 1555 1555 2.72
LINK OP1 G A 115 MG MG A1626 1555 1555 2.85
LINK OP2 A A 116 MG MG A1587 1555 1555 2.99
LINK OP1 A A 116 MG MG A1587 1555 1555 2.95
LINK OP2 G A 117 MG MG A1587 1555 1555 2.03
LINK N3 C A 121 MG MG A1598 1555 1555 2.95
LINK O2 C A 121 MG MG A1598 1555 1555 3.09
LINK O6 G A 124 MG MG A1598 1555 1555 2.69
LINK O4 U A 125 MG MG A1598 1555 1555 2.61
LINK O6 G A 126 MG MG A1598 1555 1555 3.02
LINK OP1 C A 174 MG MG A1599 1555 1555 2.76
LINK OP2 C A 175 MG MG A1599 1555 1555 2.25
LINK OP2 A A 195 MG MG A1586 1555 1555 2.01
LINK MG MG A 210 O6 G A 604 1555 1555 2.76
LINK MG MG A 210 O4 U A 605 1555 1555 2.73
LINK MG MG A 214 OP1 G A 548 1555 1555 2.34
LINK O6 G A 236 MG MG A1598 1555 1555 2.60
LINK OP2 G A 289 MG MG A1587 1555 1555 2.14
LINK O6 G A 299 MG MG A1572 1555 1555 2.10
LINK OP1 A A 315 MG MG A1615 1555 1555 2.52
LINK N7 G A 324 MG MG A1573 1555 1555 2.35
LINK N7 A A 325 MG MG A 467 1555 1555 3.05
LINK O6 G A 326 MG MG A 467 1555 1555 2.81
LINK OP1 C A 328 MG MG A1614 1555 1555 2.12
LINK OP2 G A 331 MG MG A1600 1555 1555 2.27
LINK OP2 C A 352 MG MG A1588 1555 1555 2.19
LINK O2 C A 352 MG MG A1627 1555 1555 3.13
LINK O6 G A 357 MG MG A1627 1555 1555 2.98
LINK N7 G A 362 MG MG A1624 1555 1555 2.65
LINK OP1 U A 387 MG MG A 469 1555 1555 3.13
LINK O6 G A 394 MG MG A1632 1555 1555 2.93
LINK MG MG A 441 O6 G A 853 1555 1555 2.71
LINK OP1 G A 450 MG MG A1631 1555 1555 2.14
LINK O2' A A 451 MG MG A1631 1555 1555 2.93
LINK O3' A A 451 MG MG A1631 1555 1555 2.62
LINK OP2 A A 452 MG MG A1631 1555 1555 2.08
LINK OP1 A A 463 MG MG A1616 1555 1555 2.88
LINK MG MG A 471 O3' G A 575 1555 1555 3.04
LINK MG MG A 471 OP1 G A 576 1555 1555 2.81
LINK MG MG A 473 O3' G A1300 1555 1555 3.08
LINK MG MG A 473 OP1 U A1301 1555 1555 3.13
LINK MG MG A 473 OP2 U A1301 1555 1555 2.56
LINK MG MG A 493 OP2 G A1343 1555 1555 1.92
LINK MG MG A 493 O5' G A1343 1555 1555 2.57
LINK OP1 C A 504 MG MG A1596 1555 1555 2.46
LINK OP2 A A 509 MG MG A1557 1555 1555 2.54
LINK OP2 A A 510 MG MG A1557 1555 1555 2.17
LINK O4 U A 516 MG MG A1617 1555 1555 2.16
LINK N3 C A 518 MG MG A1597 1555 1555 2.91
LINK N3 C A 518 MG MG A1606 1555 1555 3.13
LINK O2 C A 518 MG MG A1606 1555 1555 2.97
LINK N7 G A 529 MG MG A1597 1555 1555 3.06
LINK O6 G A 529 MG MG A1597 1555 1555 2.66
LINK O6 G A 530 MG MG A1606 1555 1555 2.70
LINK O3' G A 530 MG MG X 500 1555 1555 3.10
LINK O2' G A 530 MG MG X 500 1555 1555 2.89
LINK OP1 A A 533 MG MG A1617 1555 1555 3.11
LINK OP2 A A 533 MG MG A1617 1555 1555 2.45
LINK O3' U A 534 MG MG A1595 1555 1555 2.91
LINK OP1 A A 535 MG MG A1595 1555 1555 2.88
LINK OP1 G A 558 MG MG A1572 1555 1555 2.12
LINK OP2 U A 560 MG MG A1558 1555 1555 2.33
LINK OP1 U A 560 MG MG A1572 1555 1555 3.14
LINK O2 U A 561 MG MG A1633 1555 1555 2.51
LINK O3' A A 563 MG MG A1592 1555 1555 3.06
LINK O2' A A 563 MG MG A1592 1555 1555 2.80
LINK OP2 C A 564 MG MG A1592 1555 1555 2.80
LINK OP2 U A 565 MG MG A1592 1555 1555 3.05
LINK OP2 G A 567 MG MG A1592 1555 1555 2.85
LINK OP2 A A 572 MG MG A1574 1555 1555 2.70
LINK OP1 A A 572 MG MG A1630 1555 1555 2.12
LINK OP2 A A 573 MG MG A1574 1555 1555 2.11
LINK OP2 A A 574 MG MG A1574 1555 1555 2.02
LINK OP1 C A 578 MG MG A1555 1555 1555 2.46
LINK O3' G A 595 MG MG A1561 1555 1555 3.05
LINK O2' G A 595 MG MG A1561 1555 1555 3.12
LINK OP2 C A 596 MG MG A1561 1555 1555 2.47
LINK OP2 G A 597 MG MG A1561 1555 1555 2.62
LINK O4 U A 598 MG MG A1561 1555 1555 2.61
LINK OP2 A A 608 MG MG A1612 1555 1555 2.19
LINK OP2 C A 749 MG MG A1550 1555 1555 2.41
LINK OP2 G A 750 MG MG A1550 1555 1555 2.14
LINK OP2 A A 766 MG MG A1551 1555 1555 2.08
LINK OP2 A A 768 MG MG A1552 1555 1555 2.11
LINK OP2 A A 782 MG MG A1590 1555 1555 3.08
LINK OP1 A A 782 MG MG A1590 1555 1555 2.81
LINK OP2 A A 794 MG MG A1590 1555 1555 2.62
LINK O3' A A 865 MG MG A1577 1555 1555 2.86
LINK OP1 C A 866 MG MG A1577 1555 1555 3.13
LINK OP2 G A 869 MG MG A1562 1555 1555 3.10
LINK OP2 A A 900 MG MG A1575 1555 1555 3.15
LINK OP1 G A 903 MG MG A1629 1555 1555 2.35
LINK N4 C A 924 MG MG A1620 1555 1555 3.07
LINK O6 G A 925 MG MG A1620 1555 1555 2.78
LINK O6 G A 927 MG MG A1620 1555 1555 2.98
LINK OP1 C A 934 MG MG A1565 1555 1555 2.22
LINK OP2 A A 937 MG MG A1564 1555 1555 2.43
LINK OP1 G A 944 MG MG A1546 1555 1555 2.19
LINK OP2 G A 945 MG MG A1546 1555 1555 2.37
LINK OP1 A A 964 MG MG A1568 1555 1555 2.30
LINK OP1 C A 972 MG MG A1618 1555 1555 2.19
LINK OP1 G A 973 MG MG J 449 1555 1555 3.05
LINK O2' G A1053 MG MG A1570 1555 1555 3.14
LINK OP2 C A1054 MG MG A1570 1555 1555 2.12
LINK OP1 C A1054 MG MG A1571 1555 1555 2.33
LINK O3' A A1067 MG MG A1578 1555 1555 2.52
LINK OP1 G A1068 MG MG A1578 1555 1555 2.82
LINK O6 G A1079 MG MG A1577 1555 1555 2.49
LINK O6 G A1088 MG MG A1610 1555 1555 2.30
LINK N7 G A1088 MG MG A1610 1555 1555 2.73
LINK OP1 G A1094 MG MG A1578 1555 1555 2.06
LINK OP2 U A1095 MG MG A1579 1555 1555 2.02
LINK O6 G A1108 MG MG A1579 1555 1555 2.09
LINK OP2 A A1110 MG MG A1576 1555 1555 2.09
LINK O3' U A1196 MG MG A1571 1555 1555 2.55
LINK OP1 G A1197 MG MG A1570 1555 1555 2.71
LINK OP1 G A1197 MG MG A1571 1555 1555 2.58
LINK OP2 G A1198 MG MG A1571 1555 1555 2.15
LINK OP1 U A1199 MG MG A1568 1555 1555 2.12
LINK OP1 A A1204 MG MG A1619 1555 1555 2.86
LINK OP2 A A1204 MG MG A1619 1555 1555 2.54
LINK OP1 G A1224 MG MG A1547 1555 1555 1.79
LINK OP2 A A1238 MG MG A1611 1555 1555 2.44
LINK OP1 C A1303 MG MG A1591 1555 1555 2.17
LINK OP2 G A1304 MG MG A1591 1555 1555 2.22
LINK O2 C A1335 MG MG A1611 1555 1555 2.82
LINK O4 U A1390 MG MG A1620 1555 1555 2.76
LINK O3' G A1401 MG MG A1635 1555 1555 3.13
LINK OP1 G A1401 MG MG A1635 1555 1555 3.08
LINK OP1 C A1402 MG MG A1635 1555 1555 3.03
LINK OP2 C A1402 MG MG A1635 1555 1555 1.98
LINK O3' A A1499 MG MG A1582 1555 1555 2.74
LINK OP2 A A1499 MG MG A1583 1555 1555 2.19
LINK OP1 A A1500 MG MG A1582 1555 1555 2.68
LINK OP2 A A1500 MG MG A1583 1555 1555 2.06
LINK OP1 A A1500 MG MG A1584 1555 1555 1.95
LINK O2' G A1504 MG MG A1583 1555 1555 3.15
LINK O3' G A1504 MG MG A1584 1555 1555 2.75
LINK OP2 G A1505 MG MG A1583 1555 1555 2.53
LINK OP1 G A1505 MG MG A1583 1555 1555 3.10
LINK OP1 G A1505 MG MG A1584 1555 1555 2.88
LINK OP1 G A1508 MG MG A1582 1555 1555 2.72
LINK OP1 G A1508 MG MG A1584 1555 1555 2.35
LINK OP1 G A1521 MG MG A1582 1555 1555 2.97
LINK MG MG A1597 O PRO L 48 1555 1555 2.56
LINK MG MG A1597 ND2 ASN L 49 1555 1555 2.76
LINK MG MG A1606 O2' A W 3 1555 1555 3.03
LINK MG MG A1618 NZ LYS J 57 1555 1555 2.46
LINK O2' C X 35 MG MG X 500 1555 1555 2.26
LINK O4' C X 35 MG MG X 500 1555 1555 2.85
LINK N4 C X 35 MG MG X 502 1555 1555 2.74
LINK O6 G X 36 MG MG X 502 1555 1555 2.89
LINK SG CYS D 9 ZN ZN D 306 1555 1555 2.28
LINK SG CYS D 12 ZN ZN D 306 1555 1555 2.92
LINK SG CYS D 26 ZN ZN D 306 1555 1555 2.42
LINK SG CYS D 31 ZN ZN D 306 1555 1555 2.20
LINK NH2 ARG J 60 MG MG J 449 1555 1555 2.60
LINK SG CYS N 24 ZN ZN N 307 1555 1555 2.45
LINK SG CYS N 27 ZN ZN N 307 1555 1555 2.03
LINK SG CYS N 40 ZN ZN N 307 1555 1555 2.47
LINK SG CYS N 43 ZN ZN N 307 1555 1555 2.08
SITE 1 AC1 10 G A1405 U A1406 C A1407 A A1408
SITE 2 AC1 10 C A1409 G A1491 A A1492 A A1493
SITE 3 AC1 10 G A1494 U A1495
SITE 1 AC2 2 G A 944 G A 945
SITE 1 AC3 1 G A1224
SITE 1 AC4 2 U A 14 U A 17
SITE 1 AC5 2 C A 749 G A 750
SITE 1 AC6 1 A A 766
SITE 1 AC7 1 A A 768
SITE 1 AC8 1 U A 772
SITE 1 AC9 1 A A 780
SITE 1 BC1 2 G A 576 C A 578
SITE 1 BC2 1 MG A 441
SITE 1 BC3 3 C A 508 A A 509 A A 510
SITE 1 BC4 2 U A 560 C A 562
SITE 1 BC5 1 A A 16
SITE 1 BC6 1 G A 21
SITE 1 BC7 4 G A 595 C A 596 G A 597 U A 598
SITE 1 BC8 2 G A 858 G A 869
SITE 1 BC9 1 A A 860
SITE 1 CC1 1 A A 937
SITE 1 CC2 2 C A 934 U A1345
SITE 1 CC3 2 G A 587 G A 588
SITE 1 CC4 2 A A 964 U A1199
SITE 1 CC5 3 G A1053 C A1054 G A1197
SITE 1 CC6 4 C A1054 U A1196 G A1197 G A1198
SITE 1 CC7 5 G A 299 A A 300 G A 558 U A 560
SITE 2 CC7 5 G A 566
SITE 1 CC8 1 G A 324
SITE 1 CC9 3 A A 572 A A 573 A A 574
SITE 1 DC1 2 G A 898 A A 900
SITE 1 DC2 2 A A1110 C A1189
SITE 1 DC3 3 A A 865 C A 866 G A1079
SITE 1 DC4 4 A A1067 G A1068 G A1094 G A1387
SITE 1 DC5 2 U A1095 G A1108
SITE 1 DC6 4 A A1499 A A1500 G A1508 G A1521
SITE 1 DC7 4 A A1499 A A1500 G A1504 G A1505
SITE 1 DC8 5 A A1500 G A1504 G A1505 A A1507
SITE 2 DC8 5 G A1508
SITE 1 DC9 1 G A 168
SITE 1 EC1 1 A A 195
SITE 1 EC2 3 A A 116 G A 117 G A 289
SITE 1 EC3 1 C A 352
SITE 1 EC4 2 A A 782 A A 794
SITE 1 EC5 2 C A1303 G A1304
SITE 1 EC6 4 A A 563 C A 564 U A 565 G A 567
SITE 1 EC7 4 G A 604 U A 605 G A 633 C A 634
SITE 1 EC8 2 G A 584 U A 757
SITE 1 EC9 3 C A 403 A A 547 G A 548
SITE 1 FC1 2 G A 407 GLY D 6
SITE 1 FC2 3 U A 512 U A 534 A A 535
SITE 1 FC3 2 C A 504 G A 505
SITE 1 FC4 4 C A 518 G A 529 PRO L 48 ASN L 49
SITE 1 FC5 6 C A 121 G A 124 U A 125 G A 126
SITE 2 FC5 6 C A 235 G A 236
SITE 1 FC6 2 C A 174 C A 175
SITE 1 FC7 2 A A 109 G A 331
SITE 1 FC8 4 G A 69 G A 70 G A 97 U A 98
SITE 1 FC9 4 G A 61 U A 62 G A 105 C A 106
SITE 1 GC1 1 C A 962
SITE 1 GC2 4 C A 518 G A 530 PRO L 48 A W 3
SITE 1 GC3 2 G A 594 G A 595
SITE 1 GC4 1 G A 888
SITE 1 GC5 1 A A 915
SITE 1 GC6 2 G A1087 G A1088
SITE 1 GC7 3 A A1238 A A1299 C A1335
SITE 1 GC8 1 A A 608
SITE 1 GC9 1 A A 101
SITE 1 HC1 3 C A 328 A A 329 C A 330
SITE 1 HC2 1 A A 315
SITE 1 HC3 2 G A 462 A A 463
SITE 1 HC4 4 U A 516 G A 517 A A 532 A A 533
SITE 1 HC5 2 C A 972 LYS J 57
SITE 1 HC6 2 C A1203 A A1204
SITE 1 HC7 5 C A 924 G A 925 G A 927 U A1390
SITE 2 HC7 5 U A1391
SITE 1 HC8 4 U A 833 G A 852 G A 853 MG A1556
SITE 1 HC9 2 G A 649 G A 650
SITE 1 IC1 3 G A 973 LYS J 57 ARG J 60
SITE 1 IC2 1 G A 362
SITE 1 IC3 2 A A 53 A A 353
SITE 1 IC4 2 C A 48 G A 115
SITE 1 IC5 3 C A 352 A A 356 G A 357
SITE 1 IC6 3 G A 44 U A 45 G A 396
SITE 1 IC7 1 G A 903
SITE 1 IC8 2 A A 572 A A 819
SITE 1 IC9 2 G A 138 G A 139
SITE 1 JC1 4 G A 107 G A 324 A A 325 G A 326
SITE 1 JC2 4 C A 58 A A 59 C A 386 U A 387
SITE 1 JC3 2 G A 575 G A 576
SITE 1 JC4 2 G A1300 U A1301
SITE 1 JC5 3 G A 450 A A 451 A A 452
SITE 1 JC6 3 U A 45 G A 46 G A 394
SITE 1 JC7 1 U A 561
SITE 1 JC8 2 G A1343 C A1344
SITE 1 JC9 2 G A 530 C X 35
SITE 1 KC1 2 G A1401 C A1402
SITE 1 KC2 5 CYS D 9 CYS D 12 LEU D 19 CYS D 26
SITE 2 KC2 5 CYS D 31
SITE 1 KC3 4 CYS N 24 CYS N 27 CYS N 40 CYS N 43
SITE 1 KC4 2 C X 35 G X 36
CRYST1 401.135 401.135 175.193 90.00 90.00 90.00 P 41 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.002493 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002493 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005708 0.00000
(ATOM LINES ARE NOT SHOWN.)
END