HEADER TRANSFERASE 14-FEB-05 1YUM
TITLE CRYSTAL STRUCTURE OF NICOTINIC ACID MONONUCLEOTIDE ADENYLYLTRANSFERASE
TITLE 2 FROM PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 'PROBABLE NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: NICOTINIC ACID MONONUCLEOTIDE ADENYLYLTRANSFERASE, NAMN AT,
COMPND 5 DEAMIDO-NAD+, PYROPHOSPHORYLASE, DEAMIDO-NAD+, DIPHOSPHORYLASE,
COMPND 6 NICOTINATE MONONUCLEOTIDE ADENYLYLTRANSFERASE, NAMN
COMPND 7 ADENYLYLTRANSFERASE;
COMPND 8 EC: 2.7.7.18;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: NADD (PA4006);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28B(+)
KEYWDS ALPHA/BETA DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.YOON,H.L.KIM,B.MIKAMI,S.W.SUH
REVDAT 5 03-APR-24 1YUM 1 REMARK
REVDAT 4 13-MAR-24 1YUM 1 REMARK SEQADV
REVDAT 3 29-MAR-17 1YUM 1 VERSN
REVDAT 2 24-FEB-09 1YUM 1 VERSN
REVDAT 1 08-NOV-05 1YUM 0
JRNL AUTH H.J.YOON,H.L.KIM,B.MIKAMI,S.W.SUH
JRNL TITL CRYSTAL STRUCTURE OF NICOTINIC ACID MONONUCLEOTIDE
JRNL TITL 2 ADENYLYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA IN ITS APO
JRNL TITL 3 AND SUBSTRATE-COMPLEXED FORMS REVEALS A FULLY OPEN
JRNL TITL 4 CONFORMATION
JRNL REF J.MOL.BIOL. V. 351 258 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16009375
JRNL DOI 10.1016/J.JMB.2005.06.001
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.191
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 5252
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 92096
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.179
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 85016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6636
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 140
REMARK 3 SOLVENT ATOMS : 813
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 7590.1
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 26
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 31002
REMARK 3 NUMBER OF RESTRAINTS : 29215
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 ANGLE DISTANCES (A) : 0.028
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.038
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.046
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.038
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.095
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THIS IS A TWINNED STRUCTURE. THE
REMARK 3 TWINNING OPERATOR IS (H,K,L) -> (H,-K,-L) AND THE TWINNING
REMARK 3 FRACTION IS 0.49421
REMARK 4
REMARK 4 1YUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031935.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.85
REMARK 200 MONOCHROMATOR : QUASI-MONOCHROMATIC X-RAY
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118041
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.26600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHELXL
REMARK 200 STARTING MODEL: APO NAMN AT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS PROPANE, TRISODIUM CITRATE,
REMARK 280 GLYCEROL, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 55.32750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAINS. THE BIOLOGICAL UNIT IS NOT
REMARK 300 ASSIGNED.
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 HIS A 214
REMARK 465 LEU A 215
REMARK 465 GLU A 216
REMARK 465 HIS A 217
REMARK 465 HIS A 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 HIS B 214
REMARK 465 LEU B 215
REMARK 465 GLU B 216
REMARK 465 HIS B 217
REMARK 465 HIS B 218
REMARK 465 HIS B 219
REMARK 465 HIS B 220
REMARK 465 HIS B 221
REMARK 465 HIS B 222
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 HIS C 214
REMARK 465 LEU C 215
REMARK 465 GLU C 216
REMARK 465 HIS C 217
REMARK 465 HIS C 218
REMARK 465 HIS C 219
REMARK 465 HIS C 220
REMARK 465 HIS C 221
REMARK 465 HIS C 222
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 HIS D 214
REMARK 465 LEU D 215
REMARK 465 GLU D 216
REMARK 465 HIS D 217
REMARK 465 HIS D 218
REMARK 465 HIS D 219
REMARK 465 HIS D 220
REMARK 465 HIS D 221
REMARK 465 HIS D 222
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 NH2 ARG A 79 OG SER A 83 1.42
REMARK 500 NH2 ARG A 79 CB SER A 83 1.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG B 46 CA ARG B 46 CB 0.851
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 ARG A 21 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 134 CD - NE - CZ ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 134 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 134 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 152 CD - NE - CZ ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG A 193 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG B 21 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG B 46 N - CA - CB ANGL. DEV. = -14.9 DEGREES
REMARK 500 ARG B 75 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 TRP B 120 CA - CB - CG ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG C 21 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG C 46 CD - NE - CZ ANGL. DEV. = 10.9 DEGREES
REMARK 500 TYR C 84 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG C 152 CD - NE - CZ ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG C 152 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG D 21 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG D 21 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG D 56 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG D 62 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 79 -152.42 -74.28
REMARK 500 PRO A 82 76.55 -58.24
REMARK 500 SER A 83 -167.91 -58.38
REMARK 500 ASP A 136 -89.04 135.50
REMARK 500 ASP A 138 -179.82 -47.96
REMARK 500 SER A 139 41.44 -142.55
REMARK 500 ALA A 212 121.24 -37.71
REMARK 500 PHE B 12 69.00 60.35
REMARK 500 GLN B 78 61.01 -107.24
REMARK 500 ASP B 80 -72.79 -29.88
REMARK 500 PRO B 82 171.92 -59.42
REMARK 500 SER B 83 -142.07 -136.09
REMARK 500 ALA B 137 81.43 -159.11
REMARK 500 ASP B 138 -129.51 -4.72
REMARK 500 SER B 139 46.55 150.77
REMARK 500 GLU C 68 153.38 -49.04
REMARK 500 ARG C 69 -34.12 79.24
REMARK 500 GLN C 78 -70.29 -48.73
REMARK 500 ARG C 79 122.63 -30.64
REMARK 500 PRO C 82 160.38 -15.37
REMARK 500 PRO C 115 -8.99 -58.98
REMARK 500 ASP C 138 175.49 -37.51
REMARK 500 SER C 139 42.51 -145.65
REMARK 500 PRO C 174 158.28 -48.15
REMARK 500 ARG D 69 -16.53 77.23
REMARK 500 ASP D 80 -143.83 -59.72
REMARK 500 LYS D 81 154.07 -49.97
REMARK 500 PRO D 82 148.58 -19.92
REMARK 500 PRO D 135 -9.02 -49.34
REMARK 500 ALA D 137 -91.98 -62.67
REMARK 500 ASP D 138 -178.62 173.20
REMARK 500 THR D 173 75.55 -112.61
REMARK 500 TYR D 210 17.68 59.06
REMARK 500 ALA D 212 153.73 -44.09
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 CIT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCN B 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT C 2301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCN C 2302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT D 3301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCN D 3302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YUL RELATED DB: PDB
REMARK 900 THA SAME PROTEIN WITH CITRIC ACID
REMARK 900 RELATED ID: 1YUN RELATED DB: PDB
REMARK 900 THA SAME PROTEIN WITH ADENOSINE-5'-TRIPHOSPHATE AND MG
DBREF 1YUM A 1 214 UNP Q9HX21 NADD_PSEAE 1 214
DBREF 1YUM B 1 214 UNP Q9HX21 NADD_PSEAE 1 214
DBREF 1YUM C 1 214 UNP Q9HX21 NADD_PSEAE 1 214
DBREF 1YUM D 1 214 UNP Q9HX21 NADD_PSEAE 1 214
SEQADV 1YUM MET A -19 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY A -18 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER A -17 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER A -16 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A -15 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A -14 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A -13 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A -12 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A -11 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A -10 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER A -9 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER A -8 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY A -7 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM LEU A -6 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM VAL A -5 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM PRO A -4 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM ARG A -3 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY A -2 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER A -1 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A 0 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM LEU A 215 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLU A 216 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A 217 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A 218 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A 219 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A 220 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A 221 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS A 222 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM MET B -19 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY B -18 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER B -17 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER B -16 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B -15 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B -14 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B -13 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B -12 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B -11 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B -10 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER B -9 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER B -8 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY B -7 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM LEU B -6 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM VAL B -5 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM PRO B -4 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM ARG B -3 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY B -2 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER B -1 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B 0 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM LEU B 215 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLU B 216 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B 217 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B 218 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B 219 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B 220 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B 221 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS B 222 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM MET C -19 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY C -18 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER C -17 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER C -16 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C -15 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C -14 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C -13 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C -12 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C -11 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C -10 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER C -9 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER C -8 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY C -7 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM LEU C -6 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM VAL C -5 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM PRO C -4 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM ARG C -3 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY C -2 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER C -1 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C 0 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM LEU C 215 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLU C 216 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C 217 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C 218 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C 219 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C 220 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C 221 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS C 222 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM MET D -19 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY D -18 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER D -17 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER D -16 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D -15 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D -14 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D -13 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D -12 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D -11 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D -10 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER D -9 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER D -8 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY D -7 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM LEU D -6 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM VAL D -5 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM PRO D -4 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM ARG D -3 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLY D -2 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM SER D -1 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D 0 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM LEU D 215 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM GLU D 216 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D 217 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D 218 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D 219 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D 220 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D 221 UNP Q9HX21 EXPRESSION TAG
SEQADV 1YUM HIS D 222 UNP Q9HX21 EXPRESSION TAG
SEQRES 1 A 242 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 242 LEU VAL PRO ARG GLY SER HIS MET GLY LYS ARG ILE GLY
SEQRES 3 A 242 LEU PHE GLY GLY THR PHE ASP PRO VAL HIS ILE GLY HIS
SEQRES 4 A 242 MET ARG SER ALA VAL GLU MET ALA GLU GLN PHE ALA LEU
SEQRES 5 A 242 ASP GLU LEU ARG LEU LEU PRO ASN ALA ARG PRO PRO HIS
SEQRES 6 A 242 ARG GLU THR PRO GLN VAL SER ALA ALA GLN ARG LEU ALA
SEQRES 7 A 242 MET VAL GLU ARG ALA VAL ALA GLY VAL GLU ARG LEU THR
SEQRES 8 A 242 VAL ASP PRO ARG GLU LEU GLN ARG ASP LYS PRO SER TYR
SEQRES 9 A 242 THR ILE ASP THR LEU GLU SER VAL ARG ALA GLU LEU ALA
SEQRES 10 A 242 ALA ASP ASP GLN LEU PHE MET LEU ILE GLY TRP ASP ALA
SEQRES 11 A 242 PHE CYS GLY LEU PRO THR TRP HIS ARG TRP GLU ALA LEU
SEQRES 12 A 242 LEU ASP HIS CYS HIS ILE VAL VAL LEU GLN ARG PRO ASP
SEQRES 13 A 242 ALA ASP SER GLU PRO PRO GLU SER LEU ARG ASP LEU LEU
SEQRES 14 A 242 ALA ALA ARG SER VAL ALA ASP PRO GLN ALA LEU LYS GLY
SEQRES 15 A 242 PRO GLY GLY GLN ILE THR PHE VAL TRP GLN THR PRO LEU
SEQRES 16 A 242 ALA VAL SER ALA THR GLN ILE ARG ALA LEU LEU GLY ALA
SEQRES 17 A 242 GLY ARG SER VAL ARG PHE LEU VAL PRO ASP ALA VAL LEU
SEQRES 18 A 242 ASN TYR ILE GLU ALA HIS HIS LEU TYR ARG ALA PRO HIS
SEQRES 19 A 242 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 242 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 242 LEU VAL PRO ARG GLY SER HIS MET GLY LYS ARG ILE GLY
SEQRES 3 B 242 LEU PHE GLY GLY THR PHE ASP PRO VAL HIS ILE GLY HIS
SEQRES 4 B 242 MET ARG SER ALA VAL GLU MET ALA GLU GLN PHE ALA LEU
SEQRES 5 B 242 ASP GLU LEU ARG LEU LEU PRO ASN ALA ARG PRO PRO HIS
SEQRES 6 B 242 ARG GLU THR PRO GLN VAL SER ALA ALA GLN ARG LEU ALA
SEQRES 7 B 242 MET VAL GLU ARG ALA VAL ALA GLY VAL GLU ARG LEU THR
SEQRES 8 B 242 VAL ASP PRO ARG GLU LEU GLN ARG ASP LYS PRO SER TYR
SEQRES 9 B 242 THR ILE ASP THR LEU GLU SER VAL ARG ALA GLU LEU ALA
SEQRES 10 B 242 ALA ASP ASP GLN LEU PHE MET LEU ILE GLY TRP ASP ALA
SEQRES 11 B 242 PHE CYS GLY LEU PRO THR TRP HIS ARG TRP GLU ALA LEU
SEQRES 12 B 242 LEU ASP HIS CYS HIS ILE VAL VAL LEU GLN ARG PRO ASP
SEQRES 13 B 242 ALA ASP SER GLU PRO PRO GLU SER LEU ARG ASP LEU LEU
SEQRES 14 B 242 ALA ALA ARG SER VAL ALA ASP PRO GLN ALA LEU LYS GLY
SEQRES 15 B 242 PRO GLY GLY GLN ILE THR PHE VAL TRP GLN THR PRO LEU
SEQRES 16 B 242 ALA VAL SER ALA THR GLN ILE ARG ALA LEU LEU GLY ALA
SEQRES 17 B 242 GLY ARG SER VAL ARG PHE LEU VAL PRO ASP ALA VAL LEU
SEQRES 18 B 242 ASN TYR ILE GLU ALA HIS HIS LEU TYR ARG ALA PRO HIS
SEQRES 19 B 242 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 242 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 242 LEU VAL PRO ARG GLY SER HIS MET GLY LYS ARG ILE GLY
SEQRES 3 C 242 LEU PHE GLY GLY THR PHE ASP PRO VAL HIS ILE GLY HIS
SEQRES 4 C 242 MET ARG SER ALA VAL GLU MET ALA GLU GLN PHE ALA LEU
SEQRES 5 C 242 ASP GLU LEU ARG LEU LEU PRO ASN ALA ARG PRO PRO HIS
SEQRES 6 C 242 ARG GLU THR PRO GLN VAL SER ALA ALA GLN ARG LEU ALA
SEQRES 7 C 242 MET VAL GLU ARG ALA VAL ALA GLY VAL GLU ARG LEU THR
SEQRES 8 C 242 VAL ASP PRO ARG GLU LEU GLN ARG ASP LYS PRO SER TYR
SEQRES 9 C 242 THR ILE ASP THR LEU GLU SER VAL ARG ALA GLU LEU ALA
SEQRES 10 C 242 ALA ASP ASP GLN LEU PHE MET LEU ILE GLY TRP ASP ALA
SEQRES 11 C 242 PHE CYS GLY LEU PRO THR TRP HIS ARG TRP GLU ALA LEU
SEQRES 12 C 242 LEU ASP HIS CYS HIS ILE VAL VAL LEU GLN ARG PRO ASP
SEQRES 13 C 242 ALA ASP SER GLU PRO PRO GLU SER LEU ARG ASP LEU LEU
SEQRES 14 C 242 ALA ALA ARG SER VAL ALA ASP PRO GLN ALA LEU LYS GLY
SEQRES 15 C 242 PRO GLY GLY GLN ILE THR PHE VAL TRP GLN THR PRO LEU
SEQRES 16 C 242 ALA VAL SER ALA THR GLN ILE ARG ALA LEU LEU GLY ALA
SEQRES 17 C 242 GLY ARG SER VAL ARG PHE LEU VAL PRO ASP ALA VAL LEU
SEQRES 18 C 242 ASN TYR ILE GLU ALA HIS HIS LEU TYR ARG ALA PRO HIS
SEQRES 19 C 242 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 242 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 242 LEU VAL PRO ARG GLY SER HIS MET GLY LYS ARG ILE GLY
SEQRES 3 D 242 LEU PHE GLY GLY THR PHE ASP PRO VAL HIS ILE GLY HIS
SEQRES 4 D 242 MET ARG SER ALA VAL GLU MET ALA GLU GLN PHE ALA LEU
SEQRES 5 D 242 ASP GLU LEU ARG LEU LEU PRO ASN ALA ARG PRO PRO HIS
SEQRES 6 D 242 ARG GLU THR PRO GLN VAL SER ALA ALA GLN ARG LEU ALA
SEQRES 7 D 242 MET VAL GLU ARG ALA VAL ALA GLY VAL GLU ARG LEU THR
SEQRES 8 D 242 VAL ASP PRO ARG GLU LEU GLN ARG ASP LYS PRO SER TYR
SEQRES 9 D 242 THR ILE ASP THR LEU GLU SER VAL ARG ALA GLU LEU ALA
SEQRES 10 D 242 ALA ASP ASP GLN LEU PHE MET LEU ILE GLY TRP ASP ALA
SEQRES 11 D 242 PHE CYS GLY LEU PRO THR TRP HIS ARG TRP GLU ALA LEU
SEQRES 12 D 242 LEU ASP HIS CYS HIS ILE VAL VAL LEU GLN ARG PRO ASP
SEQRES 13 D 242 ALA ASP SER GLU PRO PRO GLU SER LEU ARG ASP LEU LEU
SEQRES 14 D 242 ALA ALA ARG SER VAL ALA ASP PRO GLN ALA LEU LYS GLY
SEQRES 15 D 242 PRO GLY GLY GLN ILE THR PHE VAL TRP GLN THR PRO LEU
SEQRES 16 D 242 ALA VAL SER ALA THR GLN ILE ARG ALA LEU LEU GLY ALA
SEQRES 17 D 242 GLY ARG SER VAL ARG PHE LEU VAL PRO ASP ALA VAL LEU
SEQRES 18 D 242 ASN TYR ILE GLU ALA HIS HIS LEU TYR ARG ALA PRO HIS
SEQRES 19 D 242 LEU GLU HIS HIS HIS HIS HIS HIS
HET CIT A 301 13
HET NCN A 302 22
HET CIT B1301 13
HET NCN B1302 22
HET CIT C2301 13
HET NCN C2302 22
HET CIT D3301 13
HET NCN D3302 22
HETNAM CIT CITRIC ACID
HETNAM NCN NICOTINATE MONONUCLEOTIDE
HETSYN NCN NAMN
FORMUL 5 CIT 4(C6 H8 O7)
FORMUL 6 NCN 4(C11 H14 N O9 P)
FORMUL 13 HOH *813(H2 O)
HELIX 1 1 HIS A 16 ALA A 31 1 16
HELIX 2 2 PRO A 43 GLU A 47 5 5
HELIX 3 3 SER A 52 ALA A 65 1 14
HELIX 4 4 PRO A 74 ARG A 79 5 6
HELIX 5 5 TYR A 84 LEU A 96 1 13
HELIX 6 6 TRP A 108 CYS A 112 1 5
HELIX 7 7 GLY A 113 TRP A 117 5 5
HELIX 8 8 ARG A 119 LEU A 123 5 5
HELIX 9 9 PRO A 142 SER A 144 5 3
HELIX 10 10 LEU A 145 SER A 153 1 9
HELIX 11 11 ASP A 156 LEU A 160 5 5
HELIX 12 12 SER A 178 ALA A 188 1 11
HELIX 13 13 PRO A 197 HIS A 207 1 11
HELIX 14 14 HIS B 16 PHE B 30 1 15
HELIX 15 15 PRO B 43 GLU B 47 5 5
HELIX 16 16 SER B 52 ALA B 65 1 14
HELIX 17 17 PRO B 74 GLN B 78 5 5
HELIX 18 18 TYR B 84 ARG B 93 1 10
HELIX 19 19 TRP B 108 GLY B 113 1 6
HELIX 20 20 LEU B 114 TRP B 117 5 4
HELIX 21 21 ARG B 119 HIS B 126 5 8
HELIX 22 22 PRO B 142 SER B 144 5 3
HELIX 23 23 LEU B 145 SER B 153 1 9
HELIX 24 24 ASP B 156 LEU B 160 5 5
HELIX 25 25 SER B 178 ALA B 188 1 11
HELIX 26 26 PRO B 197 HIS B 208 1 12
HELIX 27 27 HIS C 16 PHE C 30 1 15
HELIX 28 28 PRO C 43 GLU C 47 5 5
HELIX 29 29 SER C 52 ALA C 65 1 14
HELIX 30 30 PRO C 74 ARG C 79 1 6
HELIX 31 31 TYR C 84 LEU C 96 1 13
HELIX 32 32 TRP C 108 GLY C 113 1 6
HELIX 33 33 LEU C 114 TRP C 117 5 4
HELIX 34 34 ARG C 119 HIS C 126 5 8
HELIX 35 35 PRO C 142 SER C 144 5 3
HELIX 36 36 LEU C 145 SER C 153 1 9
HELIX 37 37 ASP C 156 LEU C 160 5 5
HELIX 38 38 SER C 178 ALA C 188 1 11
HELIX 39 39 PRO C 197 HIS C 208 1 12
HELIX 40 40 HIS D 16 ALA D 31 1 16
HELIX 41 41 PRO D 43 GLU D 47 5 5
HELIX 42 42 SER D 52 ALA D 65 1 14
HELIX 43 43 TYR D 84 LEU D 96 1 13
HELIX 44 44 TRP D 108 GLY D 113 1 6
HELIX 45 45 LEU D 114 TRP D 117 5 4
HELIX 46 46 ARG D 119 HIS D 126 5 8
HELIX 47 47 PRO D 142 SER D 153 1 12
HELIX 48 48 SER D 178 ALA D 188 1 11
HELIX 49 49 PRO D 197 HIS D 207 1 11
SHEET 1 A 6 LEU A 70 VAL A 72 0
SHEET 2 A 6 GLU A 34 PRO A 39 1 N LEU A 37 O THR A 71
SHEET 3 A 6 ARG A 4 GLY A 10 1 N PHE A 8 O LEU A 38
SHEET 4 A 6 GLN A 101 GLY A 107 1 O LEU A 105 N LEU A 7
SHEET 5 A 6 HIS A 128 GLN A 133 1 O LEU A 132 N ILE A 106
SHEET 6 A 6 ILE A 167 TRP A 171 1 O VAL A 170 N GLN A 133
SHEET 1 B 6 LEU B 70 VAL B 72 0
SHEET 2 B 6 GLU B 34 PRO B 39 1 N LEU B 37 O THR B 71
SHEET 3 B 6 ARG B 4 GLY B 10 1 N GLY B 6 O ARG B 36
SHEET 4 B 6 GLN B 101 GLY B 107 1 O GLN B 101 N ILE B 5
SHEET 5 B 6 HIS B 128 GLN B 133 1 O HIS B 128 N LEU B 102
SHEET 6 B 6 ILE B 167 TRP B 171 1 O VAL B 170 N GLN B 133
SHEET 1 C 6 LEU C 70 VAL C 72 0
SHEET 2 C 6 GLU C 34 PRO C 39 1 N LEU C 37 O THR C 71
SHEET 3 C 6 ARG C 4 GLY C 10 1 N GLY C 6 O ARG C 36
SHEET 4 C 6 GLN C 101 GLY C 107 1 O GLN C 101 N ILE C 5
SHEET 5 C 6 HIS C 128 GLN C 133 1 O VAL C 130 N MET C 104
SHEET 6 C 6 ILE C 167 TRP C 171 1 O VAL C 170 N GLN C 133
SHEET 1 D 6 LEU D 70 VAL D 72 0
SHEET 2 D 6 GLU D 34 PRO D 39 1 N LEU D 37 O THR D 71
SHEET 3 D 6 ARG D 4 GLY D 10 1 N PHE D 8 O LEU D 38
SHEET 4 D 6 GLN D 101 GLY D 107 1 O LEU D 105 N LEU D 7
SHEET 5 D 6 HIS D 128 GLN D 133 1 O LEU D 132 N ILE D 106
SHEET 6 D 6 ILE D 167 TRP D 171 1 O THR D 168 N VAL D 131
CISPEP 1 ASP A 13 PRO A 14 0 -5.30
CISPEP 2 ASP B 13 PRO B 14 0 0.30
CISPEP 3 ASP C 13 PRO C 14 0 0.17
CISPEP 4 ASP D 13 PRO D 14 0 -2.01
SITE 1 AC1 8 THR A 11 PHE A 12 HIS A 16 HIS A 19
SITE 2 AC1 8 SER A 178 ALA A 179 THR A 180 HOH A 455
SITE 1 AC2 7 ASN A 40 TYR A 84 THR A 85 ALA A 110
SITE 2 AC2 7 TRP A 117 HIS A 118 HOH A1174
SITE 1 AC3 8 HIS B 16 HIS B 19 SER B 178 ALA B 179
SITE 2 AC3 8 THR B 180 HOH B 497 HOH B 515 HOH B 532
SITE 1 AC4 8 ASN B 40 TYR B 84 THR B 85 TRP B 117
SITE 2 AC4 8 HIS B 118 HOH B 520 HOH B 556 HOH B 587
SITE 1 AC5 12 THR C 11 PHE C 12 ASP C 13 HIS C 16
SITE 2 AC5 12 HIS C 19 SER C 178 ALA C 179 THR C 180
SITE 3 AC5 12 HOH C 724 HOH C 814 HOH C 842 HOH C 861
SITE 1 AC6 10 ASN C 40 TYR C 84 THR C 85 TRP C 117
SITE 2 AC6 10 HIS C 118 HOH C 712 HOH C 751 HOH C 778
SITE 3 AC6 10 HOH C 827 HOH C1167
SITE 1 AC7 12 THR D 11 PHE D 12 HIS D 16 HIS D 19
SITE 2 AC7 12 SER D 178 ALA D 179 THR D 180 HOH D 888
SITE 3 AC7 12 HOH D 920 HOH D 942 HOH D1035 HOH D1160
SITE 1 AC8 7 ASN D 40 TYR D 84 THR D 85 TRP D 117
SITE 2 AC8 7 HIS D 118 HOH D 945 HOH D 970
CRYST1 65.179 110.655 65.203 90.00 89.99 90.00 P 1 21 1 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 0.015342 0.000000 -0.000003 0.00000
SCALE2 0.000000 0.009037 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015337 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
