HEADER SIGNALING PROTEIN/TRANSFERASE 26-MAR-01 1IB1
TITLE CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 ZETA ISOFORM;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN-1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SEROTONIN N-ACETYLTRANSFERASE;
COMPND 8 CHAIN: E, F, G, H;
COMPND 9 SYNONYM: ARALKYLAMINE N-ACETYLTRANSFERASE, AA-NAT, SEROTONIN
COMPND 10 ACETYLASE;
COMPND 11 EC: 2.3.1.87;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: YWHAZ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE 13 ORGANISM_COMMON: SHEEP;
SOURCE 14 ORGANISM_TAXID: 9940;
SOURCE 15 GENE: AANAT OR SNAT;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS N-ACETYL TRANSFERASE, 14-3-3, SIGNAL TRANSDUCTION, PROTEIN-PROTEIN
KEYWDS 2 COMPLEX, PHOSPHORYLATION, SIGNALING PROTEIN-TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.OBSIL,R.GHIRLANDO,D.C.KLEIN,S.GANGULY,F.DYDA
REVDAT 5 09-AUG-23 1IB1 1 REMARK SEQADV LINK
REVDAT 4 04-OCT-17 1IB1 1 REMARK
REVDAT 3 24-FEB-09 1IB1 1 VERSN
REVDAT 2 01-APR-03 1IB1 1 JRNL
REVDAT 1 02-MAY-01 1IB1 0
JRNL AUTH T.OBSIL,R.GHIRLANDO,D.C.KLEIN,S.GANGULY,F.DYDA
JRNL TITL CRYSTAL STRUCTURE OF THE 14-3-3ZETA:SEROTONIN
JRNL TITL 2 N-ACETYLTRANSFERASE COMPLEX. A ROLE FOR SCAFFOLDING IN
JRNL TITL 3 ENZYME REGULATION.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 105 257 2001
JRNL REFN ISSN 0092-8674
JRNL PMID 11336675
JRNL DOI 10.1016/S0092-8674(01)00316-6
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 44626
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 SET) : 0.204
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2231
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE : 0.2950
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 198
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12944
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 252
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.30
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) : NULL
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) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
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 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 1IB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013114.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : TOTAL REFLECTION MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44944
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.9
REMARK 200 DATA REDUNDANCY : 1.740
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : 0.10200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : 0.25100
REMARK 200 R SYM FOR SHELL (I) : 0.25100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.090
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1A4O AND 1CJW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, LITHIUM
REMARK 280 SULFATE, DTT, EDTA, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 229
REMARK 465 SER A 230
REMARK 465 ASP A 231
REMARK 465 THR A 232
REMARK 465 GLN A 233
REMARK 465 GLY A 234
REMARK 465 ASP A 235
REMARK 465 GLU A 236
REMARK 465 ALA A 237
REMARK 465 GLU A 238
REMARK 465 ALA A 239
REMARK 465 GLY A 240
REMARK 465 GLU A 241
REMARK 465 GLY A 242
REMARK 465 GLY A 243
REMARK 465 GLU A 244
REMARK 465 ASN A 245
REMARK 465 MET B 1
REMARK 465 THR B 229
REMARK 465 SER B 230
REMARK 465 ASP B 231
REMARK 465 THR B 232
REMARK 465 GLN B 233
REMARK 465 GLY B 234
REMARK 465 ASP B 235
REMARK 465 GLU B 236
REMARK 465 ALA B 237
REMARK 465 GLU B 238
REMARK 465 ALA B 239
REMARK 465 GLY B 240
REMARK 465 GLU B 241
REMARK 465 GLY B 242
REMARK 465 GLY B 243
REMARK 465 GLU B 244
REMARK 465 ASN B 245
REMARK 465 MET C 1
REMARK 465 THR C 229
REMARK 465 SER C 230
REMARK 465 ASP C 231
REMARK 465 THR C 232
REMARK 465 GLN C 233
REMARK 465 GLY C 234
REMARK 465 ASP C 235
REMARK 465 GLU C 236
REMARK 465 ALA C 237
REMARK 465 GLU C 238
REMARK 465 ALA C 239
REMARK 465 GLY C 240
REMARK 465 GLU C 241
REMARK 465 GLY C 242
REMARK 465 GLY C 243
REMARK 465 GLU C 244
REMARK 465 ASN C 245
REMARK 465 MET D 1
REMARK 465 THR D 229
REMARK 465 SER D 230
REMARK 465 ASP D 231
REMARK 465 THR D 232
REMARK 465 GLN D 233
REMARK 465 GLY D 234
REMARK 465 ASP D 235
REMARK 465 GLU D 236
REMARK 465 ALA D 237
REMARK 465 GLU D 238
REMARK 465 ALA D 239
REMARK 465 GLY D 240
REMARK 465 GLU D 241
REMARK 465 GLY D 242
REMARK 465 GLY D 243
REMARK 465 GLU D 244
REMARK 465 ASN D 245
REMARK 465 SER E 2
REMARK 465 THR E 3
REMARK 465 PRO E 4
REMARK 465 SER E 5
REMARK 465 VAL E 6
REMARK 465 HIS E 7
REMARK 465 CYS E 8
REMARK 465 LEU E 9
REMARK 465 LYS E 10
REMARK 465 PRO E 11
REMARK 465 SER E 12
REMARK 465 PRO E 13
REMARK 465 LEU E 14
REMARK 465 HIS E 15
REMARK 465 LEU E 16
REMARK 465 PRO E 17
REMARK 465 GLY E 197
REMARK 465 HIS E 198
REMARK 465 ALA E 199
REMARK 465 ALA E 200
REMARK 465 LEU E 201
REMARK 465 SER F 2
REMARK 465 THR F 3
REMARK 465 PRO F 4
REMARK 465 SER F 5
REMARK 465 VAL F 6
REMARK 465 HIS F 7
REMARK 465 CYS F 8
REMARK 465 LEU F 9
REMARK 465 LYS F 10
REMARK 465 PRO F 11
REMARK 465 SER F 12
REMARK 465 PRO F 13
REMARK 465 LEU F 14
REMARK 465 HIS F 15
REMARK 465 LEU F 16
REMARK 465 PRO F 17
REMARK 465 GLY F 197
REMARK 465 HIS F 198
REMARK 465 ALA F 199
REMARK 465 ALA F 200
REMARK 465 LEU F 201
REMARK 465 SER G 2
REMARK 465 THR G 3
REMARK 465 PRO G 4
REMARK 465 SER G 5
REMARK 465 VAL G 6
REMARK 465 HIS G 7
REMARK 465 CYS G 8
REMARK 465 LEU G 9
REMARK 465 LYS G 10
REMARK 465 PRO G 11
REMARK 465 SER G 12
REMARK 465 PRO G 13
REMARK 465 LEU G 14
REMARK 465 HIS G 15
REMARK 465 LEU G 16
REMARK 465 PRO G 17
REMARK 465 GLY G 197
REMARK 465 HIS G 198
REMARK 465 ALA G 199
REMARK 465 ALA G 200
REMARK 465 LEU G 201
REMARK 465 SER H 2
REMARK 465 THR H 3
REMARK 465 PRO H 4
REMARK 465 SER H 5
REMARK 465 VAL H 6
REMARK 465 HIS H 7
REMARK 465 CYS H 8
REMARK 465 LEU H 9
REMARK 465 LYS H 10
REMARK 465 PRO H 11
REMARK 465 SER H 12
REMARK 465 PRO H 13
REMARK 465 LEU H 14
REMARK 465 HIS H 15
REMARK 465 LEU H 16
REMARK 465 PRO H 17
REMARK 465 GLY H 197
REMARK 465 HIS H 198
REMARK 465 ALA H 199
REMARK 465 ALA H 200
REMARK 465 LEU H 201
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 GLY G 96 O HOH G 2928 2.13
REMARK 500 N ARG E 115 O HOH E 3009 2.16
REMARK 500 NH1 ARG F 154 O HOH F 3100 2.18
REMARK 500 OE1 GLU A 35 O HOH A 3725 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 N GLY F 177 O HOH C 2713 1554 2.05
REMARK 500 O GLU B 31 O HOH D 4373 1464 2.09
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 E 151 C - N - CA ANGL. DEV. = 12.7 DEGREES
REMARK 500 PRO F 151 C - N - CA ANGL. DEV. = 11.9 DEGREES
REMARK 500 PRO G 151 C - N - CA ANGL. DEV. = 12.4 DEGREES
REMARK 500 PRO H 151 C - N - CA ANGL. DEV. = 13.3 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 ARG A 18 72.17 -106.72
REMARK 500 THR A 69 118.35 -31.27
REMARK 500 ALA A 72 -136.45 -93.51
REMARK 500 LYS A 75 1.76 51.33
REMARK 500 ALA A 109 98.85 -63.33
REMARK 500 LYS A 212 15.31 50.10
REMARK 500 ARG B 18 70.64 -104.59
REMARK 500 ALA B 72 87.29 -52.48
REMARK 500 PHE B 104 -50.17 -125.97
REMARK 500 ALA B 109 97.14 -64.70
REMARK 500 LEU B 206 71.96 62.23
REMARK 500 SER B 210 96.62 -61.25
REMARK 500 TYR B 211 -68.23 -20.29
REMARK 500 ARG C 18 73.72 -107.70
REMARK 500 LYS C 68 2.25 -67.99
REMARK 500 PHE C 104 -51.99 -126.09
REMARK 500 ALA C 134 -98.63 -67.59
REMARK 500 LEU C 206 28.90 49.39
REMARK 500 ARG D 18 71.59 -104.57
REMARK 500 PHE D 104 -51.12 -127.39
REMARK 500 ALA D 109 97.90 -62.85
REMARK 500 GLU D 208 27.48 -77.69
REMARK 500 LYS D 212 10.33 51.39
REMARK 500 ASN E 35 115.14 65.54
REMARK 500 PHE E 56 -58.86 -127.71
REMARK 500 PRO E 151 -5.09 -42.77
REMARK 500 LEU E 195 -121.15 -121.92
REMARK 500 ASN F 35 112.94 64.32
REMARK 500 PRO F 151 -1.63 -41.96
REMARK 500 LEU F 195 -120.21 -123.94
REMARK 500 ASN G 35 113.44 64.26
REMARK 500 PRO G 151 -2.99 -43.86
REMARK 500 LEU G 195 -122.12 -122.85
REMARK 500 ASN H 35 113.20 62.96
REMARK 500 PHE H 56 -71.46 -108.18
REMARK 500 PRO H 151 -3.62 -42.54
REMARK 500 LEU H 195 -120.04 -121.74
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 TYR B 125 0.07 SIDE CHAIN
REMARK 500 TYR C 125 0.06 SIDE CHAIN
REMARK 500 TYR D 125 0.07 SIDE CHAIN
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 COT F 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COT E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COT G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COT H 403
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEROTONIN N-ACETYLTRANSFERASE (CHAINS E,F,G,H)
REMARK 999 WAS EXPRESSED TRUNCATED (ONLY RESIDUES 1-201).
DBREF 1IB1 A 1 245 UNP P63104 1433Z_HUMAN 1 245
DBREF 1IB1 B 1 245 UNP P63104 1433Z_HUMAN 1 245
DBREF 1IB1 C 1 245 UNP P63104 1433Z_HUMAN 1 245
DBREF 1IB1 D 1 245 UNP P63104 1433Z_HUMAN 1 245
DBREF 1IB1 E 2 201 UNP Q29495 SNAT_SHEEP 2 201
DBREF 1IB1 F 2 201 UNP Q29495 SNAT_SHEEP 2 201
DBREF 1IB1 G 2 201 UNP Q29495 SNAT_SHEEP 2 201
DBREF 1IB1 H 2 201 UNP Q29495 SNAT_SHEEP 2 201
SEQADV 1IB1 TPO E 31 UNP Q29495 THR 31 MODIFIED RESIDUE
SEQADV 1IB1 TPO F 31 UNP Q29495 THR 31 MODIFIED RESIDUE
SEQADV 1IB1 TPO G 31 UNP Q29495 THR 31 MODIFIED RESIDUE
SEQADV 1IB1 TPO H 31 UNP Q29495 THR 31 MODIFIED RESIDUE
SEQRES 1 A 245 MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA
SEQRES 2 A 245 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET
SEQRES 3 A 245 LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU
SEQRES 4 A 245 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 A 245 GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE
SEQRES 6 A 245 GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET
SEQRES 7 A 245 ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG
SEQRES 8 A 245 ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE
SEQRES 9 A 245 LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE
SEQRES 10 A 245 TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA
SEQRES 11 A 245 GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP
SEQRES 12 A 245 GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER
SEQRES 13 A 245 LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY
SEQRES 14 A 245 LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU
SEQRES 15 A 245 ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA
SEQRES 16 A 245 PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU
SEQRES 17 A 245 GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU
SEQRES 18 A 245 ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY
SEQRES 19 A 245 ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN
SEQRES 1 B 245 MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA
SEQRES 2 B 245 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET
SEQRES 3 B 245 LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU
SEQRES 4 B 245 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 B 245 GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE
SEQRES 6 B 245 GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET
SEQRES 7 B 245 ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG
SEQRES 8 B 245 ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE
SEQRES 9 B 245 LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE
SEQRES 10 B 245 TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA
SEQRES 11 B 245 GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP
SEQRES 12 B 245 GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER
SEQRES 13 B 245 LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY
SEQRES 14 B 245 LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU
SEQRES 15 B 245 ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA
SEQRES 16 B 245 PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU
SEQRES 17 B 245 GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU
SEQRES 18 B 245 ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY
SEQRES 19 B 245 ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN
SEQRES 1 C 245 MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA
SEQRES 2 C 245 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET
SEQRES 3 C 245 LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU
SEQRES 4 C 245 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 C 245 GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE
SEQRES 6 C 245 GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET
SEQRES 7 C 245 ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG
SEQRES 8 C 245 ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE
SEQRES 9 C 245 LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE
SEQRES 10 C 245 TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA
SEQRES 11 C 245 GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP
SEQRES 12 C 245 GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER
SEQRES 13 C 245 LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY
SEQRES 14 C 245 LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU
SEQRES 15 C 245 ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA
SEQRES 16 C 245 PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU
SEQRES 17 C 245 GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU
SEQRES 18 C 245 ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY
SEQRES 19 C 245 ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN
SEQRES 1 D 245 MET ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA
SEQRES 2 D 245 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CYS MET
SEQRES 3 D 245 LYS SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU
SEQRES 4 D 245 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 D 245 GLY ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE
SEQRES 6 D 245 GLU GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET
SEQRES 7 D 245 ALA ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG
SEQRES 8 D 245 ASP ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE
SEQRES 9 D 245 LEU ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE
SEQRES 10 D 245 TYR LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA
SEQRES 11 D 245 GLU VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP
SEQRES 12 D 245 GLN SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER
SEQRES 13 D 245 LYS LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY
SEQRES 14 D 245 LEU ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU
SEQRES 15 D 245 ASN SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA
SEQRES 16 D 245 PHE ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU
SEQRES 17 D 245 GLU SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU
SEQRES 18 D 245 ARG ASP ASN LEU THR LEU TRP THR SER ASP THR GLN GLY
SEQRES 19 D 245 ASP GLU ALA GLU ALA GLY GLU GLY GLY GLU ASN
SEQRES 1 E 200 SER THR PRO SER VAL HIS CYS LEU LYS PRO SER PRO LEU
SEQRES 2 E 200 HIS LEU PRO SER GLY ILE PRO GLY SER PRO GLY ARG GLN
SEQRES 3 E 200 ARG ARG HIS TPO LEU PRO ALA ASN GLU PHE ARG CYS LEU
SEQRES 4 E 200 THR PRO GLU ASP ALA ALA GLY VAL PHE GLU ILE GLU ARG
SEQRES 5 E 200 GLU ALA PHE ILE SER VAL SER GLY ASN CYS PRO LEU ASN
SEQRES 6 E 200 LEU ASP GLU VAL GLN HIS PHE LEU THR LEU CYS PRO GLU
SEQRES 7 E 200 LEU SER LEU GLY TRP PHE VAL GLU GLY ARG LEU VAL ALA
SEQRES 8 E 200 PHE ILE ILE GLY SER LEU TRP ASP GLU GLU ARG LEU THR
SEQRES 9 E 200 GLN GLU SER LEU ALA LEU HIS ARG PRO ARG GLY HIS SER
SEQRES 10 E 200 ALA HIS LEU HIS ALA LEU ALA VAL HIS ARG SER PHE ARG
SEQRES 11 E 200 GLN GLN GLY LYS GLY SER VAL LEU LEU TRP ARG TYR LEU
SEQRES 12 E 200 HIS HIS VAL GLY ALA GLN PRO ALA VAL ARG ARG ALA VAL
SEQRES 13 E 200 LEU MET CYS GLU ASP ALA LEU VAL PRO PHE TYR GLN ARG
SEQRES 14 E 200 PHE GLY PHE HIS PRO ALA GLY PRO CYS ALA ILE VAL VAL
SEQRES 15 E 200 GLY SER LEU THR PHE THR GLU MET HIS CYS SER LEU ARG
SEQRES 16 E 200 GLY HIS ALA ALA LEU
SEQRES 1 F 200 SER THR PRO SER VAL HIS CYS LEU LYS PRO SER PRO LEU
SEQRES 2 F 200 HIS LEU PRO SER GLY ILE PRO GLY SER PRO GLY ARG GLN
SEQRES 3 F 200 ARG ARG HIS TPO LEU PRO ALA ASN GLU PHE ARG CYS LEU
SEQRES 4 F 200 THR PRO GLU ASP ALA ALA GLY VAL PHE GLU ILE GLU ARG
SEQRES 5 F 200 GLU ALA PHE ILE SER VAL SER GLY ASN CYS PRO LEU ASN
SEQRES 6 F 200 LEU ASP GLU VAL GLN HIS PHE LEU THR LEU CYS PRO GLU
SEQRES 7 F 200 LEU SER LEU GLY TRP PHE VAL GLU GLY ARG LEU VAL ALA
SEQRES 8 F 200 PHE ILE ILE GLY SER LEU TRP ASP GLU GLU ARG LEU THR
SEQRES 9 F 200 GLN GLU SER LEU ALA LEU HIS ARG PRO ARG GLY HIS SER
SEQRES 10 F 200 ALA HIS LEU HIS ALA LEU ALA VAL HIS ARG SER PHE ARG
SEQRES 11 F 200 GLN GLN GLY LYS GLY SER VAL LEU LEU TRP ARG TYR LEU
SEQRES 12 F 200 HIS HIS VAL GLY ALA GLN PRO ALA VAL ARG ARG ALA VAL
SEQRES 13 F 200 LEU MET CYS GLU ASP ALA LEU VAL PRO PHE TYR GLN ARG
SEQRES 14 F 200 PHE GLY PHE HIS PRO ALA GLY PRO CYS ALA ILE VAL VAL
SEQRES 15 F 200 GLY SER LEU THR PHE THR GLU MET HIS CYS SER LEU ARG
SEQRES 16 F 200 GLY HIS ALA ALA LEU
SEQRES 1 G 200 SER THR PRO SER VAL HIS CYS LEU LYS PRO SER PRO LEU
SEQRES 2 G 200 HIS LEU PRO SER GLY ILE PRO GLY SER PRO GLY ARG GLN
SEQRES 3 G 200 ARG ARG HIS TPO LEU PRO ALA ASN GLU PHE ARG CYS LEU
SEQRES 4 G 200 THR PRO GLU ASP ALA ALA GLY VAL PHE GLU ILE GLU ARG
SEQRES 5 G 200 GLU ALA PHE ILE SER VAL SER GLY ASN CYS PRO LEU ASN
SEQRES 6 G 200 LEU ASP GLU VAL GLN HIS PHE LEU THR LEU CYS PRO GLU
SEQRES 7 G 200 LEU SER LEU GLY TRP PHE VAL GLU GLY ARG LEU VAL ALA
SEQRES 8 G 200 PHE ILE ILE GLY SER LEU TRP ASP GLU GLU ARG LEU THR
SEQRES 9 G 200 GLN GLU SER LEU ALA LEU HIS ARG PRO ARG GLY HIS SER
SEQRES 10 G 200 ALA HIS LEU HIS ALA LEU ALA VAL HIS ARG SER PHE ARG
SEQRES 11 G 200 GLN GLN GLY LYS GLY SER VAL LEU LEU TRP ARG TYR LEU
SEQRES 12 G 200 HIS HIS VAL GLY ALA GLN PRO ALA VAL ARG ARG ALA VAL
SEQRES 13 G 200 LEU MET CYS GLU ASP ALA LEU VAL PRO PHE TYR GLN ARG
SEQRES 14 G 200 PHE GLY PHE HIS PRO ALA GLY PRO CYS ALA ILE VAL VAL
SEQRES 15 G 200 GLY SER LEU THR PHE THR GLU MET HIS CYS SER LEU ARG
SEQRES 16 G 200 GLY HIS ALA ALA LEU
SEQRES 1 H 200 SER THR PRO SER VAL HIS CYS LEU LYS PRO SER PRO LEU
SEQRES 2 H 200 HIS LEU PRO SER GLY ILE PRO GLY SER PRO GLY ARG GLN
SEQRES 3 H 200 ARG ARG HIS TPO LEU PRO ALA ASN GLU PHE ARG CYS LEU
SEQRES 4 H 200 THR PRO GLU ASP ALA ALA GLY VAL PHE GLU ILE GLU ARG
SEQRES 5 H 200 GLU ALA PHE ILE SER VAL SER GLY ASN CYS PRO LEU ASN
SEQRES 6 H 200 LEU ASP GLU VAL GLN HIS PHE LEU THR LEU CYS PRO GLU
SEQRES 7 H 200 LEU SER LEU GLY TRP PHE VAL GLU GLY ARG LEU VAL ALA
SEQRES 8 H 200 PHE ILE ILE GLY SER LEU TRP ASP GLU GLU ARG LEU THR
SEQRES 9 H 200 GLN GLU SER LEU ALA LEU HIS ARG PRO ARG GLY HIS SER
SEQRES 10 H 200 ALA HIS LEU HIS ALA LEU ALA VAL HIS ARG SER PHE ARG
SEQRES 11 H 200 GLN GLN GLY LYS GLY SER VAL LEU LEU TRP ARG TYR LEU
SEQRES 12 H 200 HIS HIS VAL GLY ALA GLN PRO ALA VAL ARG ARG ALA VAL
SEQRES 13 H 200 LEU MET CYS GLU ASP ALA LEU VAL PRO PHE TYR GLN ARG
SEQRES 14 H 200 PHE GLY PHE HIS PRO ALA GLY PRO CYS ALA ILE VAL VAL
SEQRES 15 H 200 GLY SER LEU THR PHE THR GLU MET HIS CYS SER LEU ARG
SEQRES 16 H 200 GLY HIS ALA ALA LEU
MODRES 1IB1 TPO E 31 THR PHOSPHOTHREONINE
MODRES 1IB1 TPO F 31 THR PHOSPHOTHREONINE
MODRES 1IB1 TPO G 31 THR PHOSPHOTHREONINE
MODRES 1IB1 TPO H 31 THR PHOSPHOTHREONINE
HET TPO E 31 11
HET TPO F 31 11
HET TPO G 31 11
HET TPO H 31 11
HET COT E 401 63
HET COT F 400 63
HET COT G 402 63
HET COT H 403 63
HETNAM TPO PHOSPHOTHREONINE
HETNAM COT COA-S-ACETYL TRYPTAMINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 5 TPO 4(C4 H10 N O6 P)
FORMUL 9 COT 4(C33 H48 N9 O17 P3 S)
FORMUL 13 HOH *211(H2 O)
HELIX 1 1 ASP A 2 ALA A 16 1 15
HELIX 2 2 ARG A 18 GLU A 31 1 14
HELIX 3 3 SER A 37 THR A 69 1 33
HELIX 4 4 LYS A 75 PHE A 104 1 30
HELIX 5 5 GLN A 111 ALA A 133 1 23
HELIX 6 6 ASP A 136 MET A 160 1 25
HELIX 7 7 HIS A 164 ILE A 181 1 18
HELIX 8 8 SER A 184 THR A 205 1 22
HELIX 9 9 SER A 214 TRP A 228 1 15
HELIX 10 10 ASP B 2 ALA B 16 1 15
HELIX 11 11 ARG B 18 GLU B 31 1 14
HELIX 12 12 SER B 37 LYS B 68 1 32
HELIX 13 13 ALA B 72 PHE B 104 1 33
HELIX 14 14 PHE B 104 ALA B 109 1 6
HELIX 15 15 GLN B 111 ALA B 133 1 23
HELIX 16 16 ASP B 136 MET B 160 1 25
HELIX 17 17 HIS B 164 ILE B 181 1 18
HELIX 18 18 SER B 184 ASP B 204 1 21
HELIX 19 19 SER B 214 TRP B 228 1 15
HELIX 20 20 ASP C 2 ALA C 16 1 15
HELIX 21 21 ARG C 18 GLU C 31 1 14
HELIX 22 22 SER C 37 LYS C 68 1 32
HELIX 23 23 ALA C 72 LYS C 75 5 4
HELIX 24 24 GLN C 76 PHE C 104 1 29
HELIX 25 25 PHE C 104 ALA C 109 1 6
HELIX 26 26 GLN C 111 VAL C 132 1 22
HELIX 27 27 GLY C 135 MET C 160 1 26
HELIX 28 28 HIS C 164 ILE C 181 1 18
HELIX 29 29 SER C 184 THR C 205 1 22
HELIX 30 30 SER C 214 TRP C 228 1 15
HELIX 31 31 ASP D 2 ALA D 16 1 15
HELIX 32 32 ARG D 18 GLU D 31 1 14
HELIX 33 33 SER D 37 THR D 69 1 33
HELIX 34 34 ALA D 72 PHE D 104 1 33
HELIX 35 35 PHE D 104 ALA D 109 1 6
HELIX 36 36 GLN D 111 VAL D 132 1 22
HELIX 37 37 ALA D 133 ALA D 133 5 1
HELIX 38 38 ALA D 134 GLY D 135 5 2
HELIX 39 39 ASP D 136 MET D 160 1 25
HELIX 40 40 HIS D 164 ILE D 181 1 18
HELIX 41 41 SER D 184 THR D 205 1 22
HELIX 42 42 SER D 214 TRP D 228 1 15
HELIX 43 43 THR E 41 GLU E 43 5 3
HELIX 44 44 ASP E 44 PHE E 56 1 13
HELIX 45 45 PHE E 56 GLY E 61 1 6
HELIX 46 46 ASN E 66 CYS E 77 1 12
HELIX 47 47 PRO E 78 SER E 81 5 4
HELIX 48 48 THR E 105 LEU E 111 5 7
HELIX 49 49 ARG E 128 ARG E 131 5 4
HELIX 50 50 GLY E 134 ALA E 149 1 16
HELIX 51 51 GLU E 161 ALA E 163 5 3
HELIX 52 52 LEU E 164 ARG E 170 1 7
HELIX 53 53 THR F 41 GLU F 43 5 3
HELIX 54 54 ASP F 44 PHE F 56 1 13
HELIX 55 55 PHE F 56 GLY F 61 1 6
HELIX 56 56 ASN F 66 CYS F 77 1 12
HELIX 57 57 PRO F 78 SER F 81 5 4
HELIX 58 58 THR F 105 LEU F 111 5 7
HELIX 59 59 GLY F 134 ALA F 149 1 16
HELIX 60 60 GLU F 161 ALA F 163 5 3
HELIX 61 61 LEU F 164 ARG F 170 1 7
HELIX 62 62 THR G 41 GLU G 43 5 3
HELIX 63 63 ASP G 44 PHE G 56 1 13
HELIX 64 64 PHE G 56 GLY G 61 1 6
HELIX 65 65 ASN G 66 CYS G 77 1 12
HELIX 66 66 THR G 105 LEU G 111 5 7
HELIX 67 67 ARG G 128 ARG G 131 5 4
HELIX 68 68 GLY G 134 ALA G 149 1 16
HELIX 69 69 GLU G 161 ALA G 163 5 3
HELIX 70 70 LEU G 164 ARG G 170 1 7
HELIX 71 71 THR H 41 GLU H 43 5 3
HELIX 72 72 ASP H 44 PHE H 56 1 13
HELIX 73 73 PHE H 56 GLY H 61 1 6
HELIX 74 74 ASN H 66 CYS H 77 1 12
HELIX 75 75 PRO H 78 SER H 81 5 4
HELIX 76 76 THR H 105 LEU H 111 5 7
HELIX 77 77 GLY H 134 ALA H 149 1 16
HELIX 78 78 GLU H 161 ALA H 163 5 3
HELIX 79 79 LEU H 164 ARG H 170 1 7
SHEET 1 A 7 GLU E 36 ARG E 38 0
SHEET 2 A 7 LEU E 82 VAL E 86 -1 N GLY E 83 O ARG E 38
SHEET 3 A 7 ARG E 89 TRP E 99 -1 O ARG E 89 N VAL E 86
SHEET 4 A 7 SER E 118 VAL E 126 -1 O SER E 118 N TRP E 99
SHEET 5 A 7 ARG E 155 CYS E 160 1 O ARG E 155 N ALA E 119
SHEET 6 A 7 THR E 189 SER E 194 -1 N THR E 189 O CYS E 160
SHEET 7 A 7 HIS E 174 PRO E 178 -1 O HIS E 174 N HIS E 192
SHEET 1 B 7 GLU F 36 ARG F 38 0
SHEET 2 B 7 LEU F 82 VAL F 86 -1 N GLY F 83 O ARG F 38
SHEET 3 B 7 ARG F 89 TRP F 99 -1 O ARG F 89 N VAL F 86
SHEET 4 B 7 SER F 118 VAL F 126 -1 O SER F 118 N TRP F 99
SHEET 5 B 7 ARG F 155 CYS F 160 1 O ARG F 155 N ALA F 119
SHEET 6 B 7 THR F 189 SER F 194 -1 N THR F 189 O CYS F 160
SHEET 7 B 7 HIS F 174 PRO F 178 -1 O HIS F 174 N HIS F 192
SHEET 1 C 7 GLU G 36 ARG G 38 0
SHEET 2 C 7 SER G 81 VAL G 86 -1 N GLY G 83 O ARG G 38
SHEET 3 C 7 ARG G 89 TRP G 99 -1 O ARG G 89 N VAL G 86
SHEET 4 C 7 SER G 118 VAL G 126 -1 O SER G 118 N TRP G 99
SHEET 5 C 7 ARG G 155 CYS G 160 1 O ARG G 155 N ALA G 119
SHEET 6 C 7 THR G 189 SER G 194 -1 N THR G 189 O CYS G 160
SHEET 7 C 7 HIS G 174 PRO G 178 -1 N HIS G 174 O HIS G 192
SHEET 1 D 7 GLU H 36 ARG H 38 0
SHEET 2 D 7 LEU H 82 VAL H 86 -1 N GLY H 83 O ARG H 38
SHEET 3 D 7 ARG H 89 TRP H 99 -1 O ARG H 89 N VAL H 86
SHEET 4 D 7 SER H 118 VAL H 126 -1 O SER H 118 N TRP H 99
SHEET 5 D 7 ARG H 155 CYS H 160 1 O ARG H 155 N ALA H 119
SHEET 6 D 7 THR H 189 SER H 194 -1 N THR H 189 O CYS H 160
SHEET 7 D 7 HIS H 174 PRO H 178 -1 N HIS H 174 O HIS H 192
LINK C HIS E 30 N TPO E 31 1555 1555 1.33
LINK C TPO E 31 N LEU E 32 1555 1555 1.32
LINK C HIS F 30 N TPO F 31 1555 1555 1.32
LINK C TPO F 31 N LEU F 32 1555 1555 1.32
LINK C HIS G 30 N TPO G 31 1555 1555 1.32
LINK C TPO G 31 N LEU G 32 1555 1555 1.32
LINK C HIS H 30 N TPO H 31 1555 1555 1.33
LINK C TPO H 31 N LEU H 32 1555 1555 1.32
SITE 1 AC1 25 PHE F 56 SER F 60 CYS F 63 PRO F 64
SITE 2 AC1 25 HIS F 122 ALA F 123 LEU F 124 ALA F 125
SITE 3 AC1 25 VAL F 126 ARG F 131 GLN F 132 GLN F 133
SITE 4 AC1 25 GLY F 134 GLY F 136 SER F 137 MET F 159
SITE 5 AC1 25 CYS F 160 GLU F 161 ALA F 163 LEU F 164
SITE 6 AC1 25 PHE F 167 TYR F 168 ARG F 170 PHE F 188
SITE 7 AC1 25 HOH F2129
SITE 1 AC2 27 PHE E 56 SER E 60 ASN E 62 CYS E 63
SITE 2 AC2 27 PRO E 64 HIS E 122 ALA E 123 LEU E 124
SITE 3 AC2 27 ALA E 125 VAL E 126 ARG E 131 GLN E 132
SITE 4 AC2 27 GLN E 133 GLY E 134 GLY E 136 SER E 137
SITE 5 AC2 27 MET E 159 CYS E 160 GLU E 161 ALA E 163
SITE 6 AC2 27 LEU E 164 PHE E 167 TYR E 168 ARG E 170
SITE 7 AC2 27 HOH E3192 HOH E3491 ARG G 115
SITE 1 AC3 27 ARG E 115 PHE G 56 SER G 60 ASN G 62
SITE 2 AC3 27 CYS G 63 PRO G 64 HIS G 122 ALA G 123
SITE 3 AC3 27 LEU G 124 ALA G 125 VAL G 126 ARG G 131
SITE 4 AC3 27 GLN G 132 GLN G 133 GLY G 134 GLY G 136
SITE 5 AC3 27 SER G 137 MET G 159 CYS G 160 GLU G 161
SITE 6 AC3 27 ALA G 163 LEU G 164 PHE G 167 TYR G 168
SITE 7 AC3 27 ARG G 170 VAL G 183 HOH G2839
SITE 1 AC4 28 PHE H 56 SER H 60 CYS H 63 PRO H 64
SITE 2 AC4 28 HIS H 122 ALA H 123 LEU H 124 ALA H 125
SITE 3 AC4 28 VAL H 126 ARG H 131 GLN H 132 GLN H 133
SITE 4 AC4 28 GLY H 134 GLY H 136 SER H 137 MET H 159
SITE 5 AC4 28 CYS H 160 GLU H 161 ALA H 163 LEU H 164
SITE 6 AC4 28 PHE H 167 TYR H 168 ARG H 170 VAL H 183
SITE 7 AC4 28 PHE H 188 HOH H1431 HOH H1537 HOH H1655
CRYST1 74.717 75.078 101.780 90.14 90.06 63.04 P 1 4
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 0.013384 -0.006807 -0.000001 0.00000
SCALE2 0.000000 0.014943 0.000034 0.00000
SCALE3 0.000000 0.000000 0.009825 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
