HEADER LIGASE 04-JAN-05 1YGB
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC FRAGMENT OF ALANYL-TRNA SYNTHETASE
TITLE 2 IN COMPLEX WITH L-SERINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALANYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALANINE-TRNA LIGASE, ALARS;
COMPND 5 EC: 6.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: ALAS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET20B+
KEYWDS HELIX-TURN-HELIX MOTIF, ALPHA-BETA FOLD, AMINO ACID BINDING, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.SWAIRJO,P.R.SCHIMMEL
REVDAT 4 23-AUG-23 1YGB 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1YGB 1 VERSN
REVDAT 2 08-FEB-05 1YGB 1 JRNL
REVDAT 1 25-JAN-05 1YGB 0
JRNL AUTH M.A.SWAIRJO,P.R.SCHIMMEL
JRNL TITL BREAKING SIEVE FOR STERIC EXCLUSION OF A NONCOGNATE AMINO
JRNL TITL 2 ACID FROM ACTIVE SITE OF A TRNA SYNTHETASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 988 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15657145
JRNL DOI 10.1073/PNAS.0409024102
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.A.SWAIRJO,F.J.OTERO,X.-L.YANG,M.A.LOVATO,R.J.SKENE,
REMARK 1 AUTH 2 D.E.MCREE,L.RIBAS DE POUPLANA,P.SCHIMMEL
REMARK 1 TITL ALANYL-TRNA SYNTHETASE CRYSTAL STRUCTURE AND DESIGN FOR
REMARK 1 TITL 2 ACCEPTOR-STEM RECOGNITION
REMARK 1 REF MOL.CELL V. 13 829 2004
REMARK 1 REFN ISSN 1097-2765
REMARK 1 PMID 15053876
REMARK 1 DOI 10.1016/S1097-2765(04)00126-1
REMARK 2
REMARK 2 RESOLUTION. 2.48 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) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 17674
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) : 0.199
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1761
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 : 3641
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.70
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) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 1.257
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 1YGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97976
REMARK 200 MONOCHROMATOR : CURVED CRYSTAL
REMARK 200 OPTICS : CURVED CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BLU-ICE
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17674
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1RIQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000 MME, NACL, TRIS-CL, TRIS
REMARK 280 -BASE, L-SERINE , PH 6.2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 86.79750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.04550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.04550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.39875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.04550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.04550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 130.19625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.04550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.04550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 43.39875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.04550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.04550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 130.19625
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 86.79750
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 173.59500
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 0
REMARK 465 PHE A 428
REMARK 465 LYS A 429
REMARK 465 VAL A 430
REMARK 465 GLU A 431
REMARK 465 ALA A 432
REMARK 465 LYS A 433
REMARK 465 LYS A 434
REMARK 465 VAL A 435
REMARK 465 LYS A 436
REMARK 465 GLU A 458
REMARK 465 HIS A 459
REMARK 465 HIS A 460
REMARK 465 HIS A 461
REMARK 465 HIS A 462
REMARK 465 HIS A 463
REMARK 465 HIS A 464
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 CD ARG A 296 NH2 ARG A 300 2.16
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 LEU A 2 134.92 63.68
REMARK 500 LYS A 17 8.90 -67.99
REMARK 500 LYS A 24 158.21 -48.88
REMARK 500 THR A 35 -71.48 -61.25
REMARK 500 LEU A 37 -77.68 -48.10
REMARK 500 LYS A 55 -176.73 -65.95
REMARK 500 ARG A 56 128.01 -173.00
REMARK 500 SER A 63 -179.64 174.11
REMARK 500 ARG A 69 57.99 -109.46
REMARK 500 THR A 83 -149.65 -145.87
REMARK 500 SER A 84 15.77 -144.93
REMARK 500 THR A 88 -73.88 -85.50
REMARK 500 ASP A 100 -125.73 -102.26
REMARK 500 PHE A 102 -139.91 -124.13
REMARK 500 LYS A 131 -80.14 -39.16
REMARK 500 ASP A 132 22.29 -67.76
REMARK 500 GLU A 142 -78.51 -79.53
REMARK 500 GLU A 157 9.26 -63.09
REMARK 500 ASP A 158 -20.64 -145.01
REMARK 500 ASN A 159 49.73 -155.45
REMARK 500 GLU A 184 -170.40 -172.89
REMARK 500 MET A 198 98.90 -54.06
REMARK 500 ASP A 203 -167.43 -71.39
REMARK 500 ASN A 205 -149.80 -111.49
REMARK 500 PRO A 212 12.70 -63.40
REMARK 500 HIS A 213 58.33 -154.15
REMARK 500 SER A 252 -85.79 -76.18
REMARK 500 GLU A 258 -54.20 -142.24
REMARK 500 PHE A 260 -76.50 -58.16
REMARK 500 PHE A 315 -14.92 -147.56
REMARK 500 MET A 327 19.90 -144.38
REMARK 500 GLU A 333 -3.03 -58.09
REMARK 500 ARG A 338 -84.15 -34.04
REMARK 500 GLU A 349 -65.50 -95.65
REMARK 500 PHE A 352 12.21 -164.40
REMARK 500 ASP A 388 -64.81 -102.34
REMARK 500 VAL A 394 7.16 -63.90
REMARK 500 LYS A 426 -85.09 -142.39
REMARK 500 LYS A 443 -20.04 168.92
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 A 439 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 SER A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RIQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC FRAGMENT OF A. AEOLICUS ALANYL-TRNA
REMARK 900 SYNTHETASE, APO ENZYME.
REMARK 900 RELATED ID: 1YFS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC FRAGMENT OF A. AEOLICUS ALANYL-TRNA
REMARK 900 SYNTHETASE IN COMPLEX WITH L-ALANINE
REMARK 900 RELATED ID: 1YFT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC FRAGMENT OF A. AEOLICUS ALANYL-TRNA
REMARK 900 SYNTHETASE IN COMPLEX WITH GLYCINE
REMARK 900 RELATED ID: 1YFR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC FRAGMENT OF A. AQOLICUS ALANYL-TRNA
REMARK 900 SYNTHETASE IN COMPLEX WITH ATP AND MAGNESIUM.
DBREF 1YGB A 0 453 UNP O67323 SYA_AQUAE 1 454
SEQADV 1YGB ALA A 454 UNP O67323 CLONING ARTIFACT
SEQADV 1YGB ALA A 455 UNP O67323 CLONING ARTIFACT
SEQADV 1YGB ALA A 456 UNP O67323 CLONING ARTIFACT
SEQADV 1YGB LEU A 457 UNP O67323 CLONING ARTIFACT
SEQADV 1YGB GLU A 458 UNP O67323 CLONING ARTIFACT
SEQADV 1YGB HIS A 459 UNP O67323 EXPRESSION TAG
SEQADV 1YGB HIS A 460 UNP O67323 EXPRESSION TAG
SEQADV 1YGB HIS A 461 UNP O67323 EXPRESSION TAG
SEQADV 1YGB HIS A 462 UNP O67323 EXPRESSION TAG
SEQADV 1YGB HIS A 463 UNP O67323 EXPRESSION TAG
SEQADV 1YGB HIS A 464 UNP O67323 EXPRESSION TAG
SEQRES 1 A 465 MET SER LEU SER ALA HIS GLU ILE ARG GLU LEU PHE LEU
SEQRES 2 A 465 SER PHE PHE GLU LYS LYS GLY HIS THR ARG VAL LYS SER
SEQRES 3 A 465 ALA PRO LEU VAL PRO GLU ASN ASP PRO THR LEU LEU PHE
SEQRES 4 A 465 VAL ASN ALA GLY MET VAL PRO PHE LYS ASN VAL PHE LEU
SEQRES 5 A 465 GLY LEU GLU LYS ARG PRO TYR LYS ARG ALA THR SER CYS
SEQRES 6 A 465 GLN LYS CYS LEU ARG VAL SER GLY LYS HIS ASN ASP LEU
SEQRES 7 A 465 GLU GLN VAL GLY TYR THR SER ARG HIS HIS THR PHE PHE
SEQRES 8 A 465 GLU MET LEU GLY ASN PHE SER PHE GLY ASP TYR PHE LYS
SEQRES 9 A 465 LYS GLU ALA ILE GLU TYR ALA TRP GLU PHE VAL THR GLU
SEQRES 10 A 465 VAL LEU LYS LEU PRO LYS GLU LYS LEU TYR VAL SER VAL
SEQRES 11 A 465 TYR LYS ASP ASP GLU GLU ALA TYR ARG ILE TRP ASN GLU
SEQRES 12 A 465 HIS ILE GLY ILE PRO SER GLU ARG ILE TRP ARG LEU GLY
SEQRES 13 A 465 GLU GLU ASP ASN PHE TRP GLN MET GLY ASP VAL GLY PRO
SEQRES 14 A 465 CYS GLY PRO SER SER GLU ILE TYR VAL ASP ARG GLY GLU
SEQRES 15 A 465 GLU TYR GLU GLY ASP GLU ARG TYR LEU GLU ILE TRP ASN
SEQRES 16 A 465 LEU VAL PHE MET GLN TYR ASN ARG ASP GLU ASN GLY VAL
SEQRES 17 A 465 LEU THR PRO LEU PRO HIS PRO ASN ILE ASP THR GLY MET
SEQRES 18 A 465 GLY LEU GLU ARG ILE ALA SER VAL LEU GLN GLY LYS ASN
SEQRES 19 A 465 SER ASN PHE GLU ILE ASP ILE ILE PHE PRO LEU ILE GLN
SEQRES 20 A 465 PHE GLY GLU GLU VAL SER GLY LYS LYS TYR GLY GLU LYS
SEQRES 21 A 465 PHE GLU THR ASP VAL ALA LEU ARG VAL ILE ALA ASP HIS
SEQRES 22 A 465 LEU ARG ALA ILE THR PHE ALA ILE SER ASP GLY VAL ILE
SEQRES 23 A 465 PRO SER ASN GLU GLY ARG GLY TYR VAL ILE ARG ARG ILE
SEQRES 24 A 465 LEU ARG ARG ALA MET ARG PHE GLY TYR LYS LEU GLY ILE
SEQRES 25 A 465 GLU ASN PRO PHE LEU TYR LYS GLY VAL ASP LEU VAL VAL
SEQRES 26 A 465 ASP ILE MET LYS GLU PRO TYR PRO GLU LEU GLU LEU SER
SEQRES 27 A 465 ARG GLU PHE VAL LYS GLY ILE VAL LYS GLY GLU GLU LYS
SEQRES 28 A 465 ARG PHE ILE LYS THR LEU LYS ALA GLY MET GLU TYR ILE
SEQRES 29 A 465 GLN GLU VAL ILE GLN LYS ALA LEU GLU GLU GLY ARG LYS
SEQRES 30 A 465 THR LEU SER GLY LYS GLU VAL PHE THR ALA TYR ASP THR
SEQRES 31 A 465 TYR GLY PHE PRO VAL ASP LEU ILE ASP GLU ILE ALA ARG
SEQRES 32 A 465 GLU LYS GLY LEU GLY ILE ASP LEU GLU GLY PHE GLN CYS
SEQRES 33 A 465 GLU LEU GLU GLU GLN ARG GLU ARG ALA ARG LYS HIS PHE
SEQRES 34 A 465 LYS VAL GLU ALA LYS LYS VAL LYS PRO VAL TYR SER HIS
SEQRES 35 A 465 LEU LYS GLU LEU GLY LYS THR SER ALA PHE VAL GLY ALA
SEQRES 36 A 465 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET SER A 501 7
HETNAM SER SERINE
FORMUL 2 SER C3 H7 N O3
FORMUL 3 HOH *146(H2 O)
HELIX 1 1 SER A 3 PHE A 15 1 13
HELIX 2 2 GLU A 16 GLY A 19 5 4
HELIX 3 3 MET A 43 PRO A 45 5 3
HELIX 4 4 PHE A 46 GLY A 52 1 7
HELIX 5 5 LEU A 77 VAL A 80 5 4
HELIX 6 6 PHE A 102 GLU A 116 1 15
HELIX 7 7 ASP A 133 GLU A 142 1 10
HELIX 8 8 PRO A 147 GLU A 149 5 3
HELIX 9 9 GLY A 155 ASN A 159 1 5
HELIX 10 10 GLU A 184 ARG A 188 5 5
HELIX 11 11 LEU A 222 LEU A 229 1 8
HELIX 12 12 ILE A 241 SER A 252 1 12
HELIX 13 13 LYS A 259 ASP A 282 1 24
HELIX 14 14 GLU A 289 LEU A 309 1 21
HELIX 15 15 LEU A 316 VAL A 324 1 9
HELIX 16 16 TYR A 331 GLU A 335 5 5
HELIX 17 17 SER A 337 ARG A 351 1 15
HELIX 18 18 PHE A 352 GLY A 359 1 8
HELIX 19 19 GLY A 359 GLU A 373 1 15
HELIX 20 20 SER A 379 THR A 389 1 11
HELIX 21 21 ASP A 395 GLY A 405 1 11
HELIX 22 22 ASP A 409 ARG A 425 1 17
HELIX 23 23 GLU A 444 ALA A 450 1 7
HELIX 24 24 GLY A 453 LEU A 457 5 5
SHEET 1 A 8 THR A 21 ARG A 22 0
SHEET 2 A 8 ARG A 60 LEU A 68 1 O THR A 62 N THR A 21
SHEET 3 A 8 PHE A 89 PHE A 98 -1 O MET A 92 N GLN A 65
SHEET 4 A 8 LEU A 208 GLY A 221 -1 O ILE A 216 N SER A 97
SHEET 5 A 8 LEU A 190 ARG A 202 -1 N VAL A 196 O ASP A 217
SHEET 6 A 8 PRO A 168 VAL A 177 -1 N CYS A 169 O TYR A 200
SHEET 7 A 8 LEU A 125 TYR A 130 -1 N TYR A 126 O TYR A 176
SHEET 8 A 8 ILE A 151 LEU A 154 1 O TRP A 152 N VAL A 129
SHEET 1 B 7 THR A 21 ARG A 22 0
SHEET 2 B 7 ARG A 60 LEU A 68 1 O THR A 62 N THR A 21
SHEET 3 B 7 PHE A 89 PHE A 98 -1 O MET A 92 N GLN A 65
SHEET 4 B 7 LEU A 208 GLY A 221 -1 O ILE A 216 N SER A 97
SHEET 5 B 7 LEU A 190 ARG A 202 -1 N VAL A 196 O ASP A 217
SHEET 6 B 7 PRO A 168 VAL A 177 -1 N CYS A 169 O TYR A 200
SHEET 7 B 7 PHE A 160 GLN A 162 -1 N TRP A 161 O GLY A 170
SHEET 1 C 2 VAL A 70 SER A 71 0
SHEET 2 C 2 HIS A 74 ASN A 75 -1 O HIS A 74 N SER A 71
SHEET 1 D 2 THR A 377 LEU A 378 0
SHEET 2 D 2 GLY A 407 ILE A 408 1 O GLY A 407 N LEU A 378
SITE 1 AC1 10 ALA A 41 MET A 43 MET A 92 TRP A 161
SITE 2 AC1 10 ASN A 194 ASP A 217 THR A 218 GLY A 219
SITE 3 AC1 10 HOH A 502 HOH A 592
CRYST1 74.091 74.091 173.595 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 0.013497 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013497 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005761 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
