HEADER LIGASE 30-DEC-02 1NJ5
TITLE CRYSTAL STRUCTURE OF PROLYL-TRNA SYNTHETASE FROM METHANOTHERMOBACTER
TITLE 2 THERMAUTOTROPHICUS BOUND TO PROLINE SULFAMOYL ADENYLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N TERMINALLY HIS TAGGED ENZYME;
COMPND 5 SYNONYM: PROLYL-TRNA SYNTHETASE; PROLINE--TRNA LIGASE; PRORS;
COMPND 6 EC: 6.1.1.15;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 187420;
SOURCE 4 STRAIN: DELTA H;
SOURCE 5 GENE: MTH611;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3 RECA-;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 OTHER_DETAILS: STRAIN SUPPLEMENTED WITH ADDITIONAL PLASMID ENCODING
SOURCE 12 RARE TRNAS
KEYWDS PROTEIN-AMINOACYLADENYLATE COMPLEX CLASS-II TRNA SYNTHETASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KAMTEKAR,W.D.KENNEDY,J.WANG,C.STATHOPOULOS,D.SOLL,T.A.STEITZ
REVDAT 4 14-FEB-24 1NJ5 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1NJ5 1 VERSN
REVDAT 2 24-FEB-09 1NJ5 1 VERSN
REVDAT 1 04-MAR-03 1NJ5 0
JRNL AUTH S.KAMTEKAR,W.D.KENNEDY,J.WANG,C.STATHOPOULOS,D.SOLL,
JRNL AUTH 2 T.A.STEITZ
JRNL TITL THE STRUCTURAL BASIS OF CYSTEINE AMINOACYLATION OF TRNAPRO
JRNL TITL 2 BY PROLYL-TRNA SYNTHETASES
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 1673 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 12578991
JRNL DOI 10.1073/PNAS.0437911100
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
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) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 23633
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) : 0.222
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2380
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3023
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE : 0.3630
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 375
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3782
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 28
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 70.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.14000
REMARK 3 B22 (A**2) : 3.14000
REMARK 3 B33 (A**2) : -6.28000
REMARK 3 B12 (A**2) : 10.59000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.52
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.550 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.680 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.140 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.510 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 28.96
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : FI
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : FI
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98000
REMARK 200 MONOCHROMATOR : DIAMOND (111)
REMARK 200 OPTICS : NULL
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 : 25241
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.93000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: METHANOCALDOCOCCUS JANASCHII PROLINE TRNA
REMARK 200 SYNTHETASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, BETA-MERCAPTOETHANOL,
REMARK 280 MGCL2,NACL, PROLINE SULFAMOYL ADENYLATE, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 109.29067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 54.64533
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 81.96800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 27.32267
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 136.61333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 109.29067
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 54.64533
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 27.32267
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 81.96800
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 136.61333
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER CONSTRUCTED BY A TWOFOLD
REMARK 300 ROTATION.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -54.64533
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 GLN A 2
REMARK 465 LYS A 3
REMARK 465 PRO A 4
REMARK 465 ILE A 5
REMARK 465 LYS A 6
REMARK 465 LYS A 7
REMARK 465 ASP A 8
REMARK 465 PRO A 9
REMARK 465 ASN A 10
REMARK 465 ARG A 11
REMARK 465 TYR A 12
REMARK 465 HIS A 13
REMARK 465 GLY A 14
REMARK 465 GLU A 15
REMARK 465 LYS A 16
REMARK 465 MET A 17
REMARK 465 THR A 18
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 37 34.79 -71.67
REMARK 500 PRO A 39 -0.75 -52.60
REMARK 500 LEU A 73 102.90 -161.00
REMARK 500 ALA A 87 -71.78 -85.95
REMARK 500 GLU A 94 -71.42 -28.50
REMARK 500 ARG A 110 109.94 -174.49
REMARK 500 ARG A 131 -65.26 -132.10
REMARK 500 GLU A 150 -154.77 -128.68
REMARK 500 THR A 151 121.06 -33.11
REMARK 500 LYS A 152 -34.49 -38.41
REMARK 500 LEU A 157 0.95 58.02
REMARK 500 PRO A 208 -7.19 -52.42
REMARK 500 PRO A 226 -10.19 -49.03
REMARK 500 ASP A 282 169.40 178.51
REMARK 500 ARG A 359 -86.69 -48.33
REMARK 500 GLU A 362 46.85 -75.31
REMARK 500 LYS A 363 -8.80 -162.36
REMARK 500 LEU A 381 -9.54 -53.97
REMARK 500 ARG A 428 -141.73 59.62
REMARK 500 GLU A 439 -73.51 -50.54
REMARK 500 ARG A 450 70.16 53.05
REMARK 500 SER A 461 -170.95 -65.57
REMARK 500 ASN A 466 -65.36 -97.94
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 ZN A 511 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 436 SG
REMARK 620 2 CYS A 441 SG 107.3
REMARK 620 3 CYS A 464 SG 136.4 98.5
REMARK 620 4 CYS A 467 SG 102.5 108.1 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 512 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 446 OE2
REMARK 620 2 ASP A 452 OD2 50.2
REMARK 620 3 HOH A 491 O 64.9 114.6
REMARK 620 4 HOH A 492 O 55.9 59.3 80.3
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 ZN A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P5A A 510
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NJ1 RELATED DB: PDB
REMARK 900 RELATED ID: 1NJ2 RELATED DB: PDB
REMARK 900 RELATED ID: 1NJ6 RELATED DB: PDB
REMARK 900 RELATED ID: 1NJ8 RELATED DB: PDB
DBREF 1NJ5 A 1 481 UNP O26708 SYP_METTH 1 481
SEQADV 1NJ5 MET A -19 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 GLY A -18 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 SER A -17 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 SER A -16 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 HIS A -15 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 HIS A -14 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 HIS A -13 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 HIS A -12 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 HIS A -11 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 HIS A -10 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 SER A -9 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 SER A -8 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 GLY A -7 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 LEU A -6 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 VAL A -5 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 PRO A -4 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 ARG A -3 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 GLY A -2 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 SER A -1 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 HIS A 0 UNP O26708 EXPRESSION TAG
SEQADV 1NJ5 TYR A 473 UNP O26708 THR 473 SEE REMARK 999
SEQADV 1NJ5 ARG A 474 UNP O26708 GLY 474 SEE REMARK 999
SEQADV 1NJ5 ALA A 475 UNP O26708 LEU 475 SEE REMARK 999
SEQADV 1NJ5 TYR A 476 UNP O26708 THR 476 SEE REMARK 999
SEQADV 1NJ5 ALA A 478 UNP O26708 PRO 478 SEE REMARK 999
SEQADV 1NJ5 ARG A 479 UNP O26708 GLU 479 SEE REMARK 999
SEQADV 1NJ5 THR A 480 UNP O26708 HIS 480 SEE REMARK 999
SEQADV 1NJ5 TYR A 481 UNP O26708 ILE 481 SEE REMARK 999
SEQRES 1 A 501 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 501 LEU VAL PRO ARG GLY SER HIS MET GLN LYS PRO ILE LYS
SEQRES 3 A 501 LYS ASP PRO ASN ARG TYR HIS GLY GLU LYS MET THR GLU
SEQRES 4 A 501 PHE SER GLU TRP PHE HIS ASN ILE LEU GLU GLU ALA GLU
SEQRES 5 A 501 ILE ILE ASP GLN ARG TYR PRO VAL LYS GLY MET HIS VAL
SEQRES 6 A 501 TRP MET PRO HIS GLY PHE MET ILE ARG LYS ASN THR LEU
SEQRES 7 A 501 LYS ILE LEU ARG ARG ILE LEU ASP ARG ASP HIS GLU GLU
SEQRES 8 A 501 VAL LEU PHE PRO LEU LEU VAL PRO GLU ASP GLU LEU ALA
SEQRES 9 A 501 LYS GLU ALA ILE HIS VAL LYS GLY PHE GLU ASP GLU VAL
SEQRES 10 A 501 TYR TRP VAL THR HIS GLY GLY LEU SER LYS LEU GLN ARG
SEQRES 11 A 501 LYS LEU ALA LEU ARG PRO THR SER GLU THR VAL MET TYR
SEQRES 12 A 501 PRO MET PHE ALA LEU TRP VAL ARG SER HIS THR ASP LEU
SEQRES 13 A 501 PRO MET ARG PHE TYR GLN VAL VAL ASN THR PHE ARG TYR
SEQRES 14 A 501 GLU THR LYS HIS THR ARG PRO LEU ILE ARG VAL ARG GLU
SEQRES 15 A 501 ILE THR THR PHE LYS GLU ALA HIS THR ILE HIS ALA THR
SEQRES 16 A 501 ALA SER GLU ALA GLU GLU GLN VAL GLU ARG ALA VAL GLU
SEQRES 17 A 501 ILE TYR LYS GLU PHE PHE ASN SER LEU GLY ILE PRO TYR
SEQRES 18 A 501 LEU ILE THR ARG ARG PRO PRO TRP ASP LYS PHE PRO GLY
SEQRES 19 A 501 SER GLU TYR THR VAL ALA PHE ASP THR LEU MET PRO ASP
SEQRES 20 A 501 GLY LYS THR LEU GLN ILE GLY THR VAL HIS ASN LEU GLY
SEQRES 21 A 501 GLN THR PHE ALA ARG THR PHE GLU ILE LYS PHE GLU THR
SEQRES 22 A 501 PRO GLU GLY ASP HIS GLU TYR VAL HIS GLN THR CYS TYR
SEQRES 23 A 501 GLY LEU SER ASP ARG VAL ILE ALA SER VAL ILE ALA ILE
SEQRES 24 A 501 HIS GLY ASP GLU SER GLY LEU CYS LEU PRO PRO ASP VAL
SEQRES 25 A 501 ALA ALA HIS GLN VAL VAL ILE VAL PRO ILE ILE PHE LYS
SEQRES 26 A 501 LYS ALA ALA GLU GLU VAL MET GLU ALA CYS ARG GLU LEU
SEQRES 27 A 501 ARG SER ARG LEU GLU ALA ALA GLY PHE ARG VAL HIS LEU
SEQRES 28 A 501 ASP ASP ARG ASP ILE ARG ALA GLY ARG LYS TYR TYR GLU
SEQRES 29 A 501 TRP GLU MET ARG GLY VAL PRO LEU ARG VAL GLU ILE GLY
SEQRES 30 A 501 PRO ARG ASP LEU GLU LYS GLY ALA ALA VAL ILE SER ARG
SEQRES 31 A 501 ARG ASP THR GLY GLU LYS VAL THR ALA ASP LEU GLN GLY
SEQRES 32 A 501 ILE GLU GLU THR LEU ARG GLU LEU MET LYS ASP ILE LEU
SEQRES 33 A 501 GLU ASN LEU ARG THR ARG ALA TRP GLU ARG MET GLU SER
SEQRES 34 A 501 GLU ILE ARG GLU ALA GLU THR LEU GLU GLU ALA SER ARG
SEQRES 35 A 501 ILE VAL ASP GLU LYS ARG GLY ILE ILE SER PHE MET TRP
SEQRES 36 A 501 CYS GLY GLU GLU GLU CYS GLY MET ASP VAL GLU GLU LYS
SEQRES 37 A 501 VAL ARG VAL ASP ILE LEU GLY ILE GLN GLU GLU GLY SER
SEQRES 38 A 501 GLY THR CYS ILE ASN CYS GLY ARG GLU ALA PRO TYR ARG
SEQRES 39 A 501 ALA TYR LEU ALA ARG THR TYR
HET ZN A 511 1
HET MG A 512 1
HET P5A A 510 30
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM P5A '5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE
FORMUL 2 ZN ZN 2+
FORMUL 3 MG MG 2+
FORMUL 4 P5A C15 H21 N7 O7 S
FORMUL 5 HOH *28(H2 O)
HELIX 1 1 GLU A 19 ALA A 31 1 13
HELIX 2 2 MET A 47 ASP A 66 1 20
HELIX 3 3 GLU A 80 ALA A 84 1 5
HELIX 4 4 ALA A 87 GLU A 94 1 8
HELIX 5 5 ASP A 95 VAL A 97 5 3
HELIX 6 6 SER A 118 VAL A 130 1 13
HELIX 7 7 THR A 175 LEU A 197 1 23
HELIX 8 8 GLN A 241 GLU A 248 1 8
HELIX 9 9 ASP A 270 HIS A 280 1 11
HELIX 10 10 ALA A 307 ALA A 325 1 19
HELIX 11 11 ARG A 337 MET A 347 1 11
HELIX 12 12 GLY A 357 GLU A 362 1 6
HELIX 13 13 GLY A 383 SER A 409 1 27
HELIX 14 14 THR A 416 ARG A 428 1 13
HELIX 15 15 GLU A 438 ARG A 450 1 13
SHEET 1 A 2 ILE A 34 ASP A 35 0
SHEET 2 A 2 VAL A 45 TRP A 46 -1 O VAL A 45 N ASP A 35
SHEET 1 B 7 GLU A 70 GLU A 71 0
SHEET 2 B 7 MET A 138 PHE A 147 1 O ARG A 139 N GLU A 70
SHEET 3 B 7 GLU A 162 HIS A 173 -1 O HIS A 170 N PHE A 140
SHEET 4 B 7 HIS A 262 LEU A 268 -1 O THR A 264 N THR A 171
SHEET 5 B 7 THR A 230 GLY A 240 -1 N HIS A 237 O CYS A 265
SHEET 6 B 7 TYR A 217 LEU A 224 -1 N VAL A 219 O VAL A 236
SHEET 7 B 7 LEU A 202 ARG A 205 -1 N LEU A 202 O ASP A 222
SHEET 1 C 3 LEU A 77 PRO A 79 0
SHEET 2 C 3 SER A 106 LEU A 114 -1 O ALA A 113 N VAL A 78
SHEET 3 C 3 TRP A 99 GLY A 103 -1 N VAL A 100 O LEU A 112
SHEET 1 D 2 LYS A 250 GLU A 252 0
SHEET 2 D 2 HIS A 258 TYR A 260 -1 O GLU A 259 N PHE A 251
SHEET 1 E 2 LEU A 286 CYS A 287 0
SHEET 2 E 2 ARG A 348 GLY A 349 1 O GLY A 349 N LEU A 286
SHEET 1 F 5 VAL A 329 LEU A 331 0
SHEET 2 F 5 VAL A 297 PRO A 301 1 N ILE A 299 O HIS A 330
SHEET 3 F 5 LEU A 352 ILE A 356 1 O VAL A 354 N VAL A 300
SHEET 4 F 5 ALA A 365 ARG A 370 -1 O VAL A 367 N GLU A 355
SHEET 5 F 5 LYS A 376 ASP A 380 -1 O VAL A 377 N ILE A 368
SHEET 1 G 4 ILE A 411 GLU A 413 0
SHEET 2 G 4 ILE A 430 TRP A 435 1 O ILE A 430 N ARG A 412
SHEET 3 G 4 TYR A 473 ALA A 478 -1 O ALA A 475 N PHE A 433
SHEET 4 G 4 ASP A 452 GLU A 458 -1 N ASP A 452 O ALA A 478
LINK SG CYS A 436 ZN ZN A 511 1555 1555 2.33
LINK SG CYS A 441 ZN ZN A 511 1555 1555 2.32
LINK OE2 GLU A 446 MG MG A 512 1555 1555 3.10
LINK OD2 ASP A 452 MG MG A 512 1555 1555 2.27
LINK SG CYS A 464 ZN ZN A 511 1555 1555 2.27
LINK SG CYS A 467 ZN ZN A 511 1555 1555 2.53
LINK O HOH A 491 MG MG A 512 1555 1555 2.43
LINK O HOH A 492 MG MG A 512 1555 1555 2.61
CISPEP 1 LEU A 136 PRO A 137 0 0.29
SITE 1 AC1 4 CYS A 436 CYS A 441 CYS A 464 CYS A 467
SITE 1 AC2 5 ASP A 210 GLU A 446 ASP A 452 HOH A 491
SITE 2 AC2 5 HOH A 492
SITE 1 AC3 20 THR A 117 GLU A 119 ARG A 148 GLU A 150
SITE 2 AC3 20 ILE A 158 ARG A 159 VAL A 160 ILE A 163
SITE 3 AC3 20 PHE A 166 GLU A 168 PHE A 212 GLN A 232
SITE 4 AC3 20 GLY A 234 THR A 235 HIS A 237 TYR A 266
SITE 5 AC3 20 GLY A 267 SER A 269 ARG A 271 HOH A 487
CRYST1 143.955 143.955 163.936 90.00 90.00 120.00 P 65 2 2 12
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 0.006947 0.004011 0.000000 0.00000
SCALE2 0.000000 0.008021 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006100 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
