HEADER LIGASE 12-JUN-09 3HTZ
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC FRAGMENT OF ALANYL-TRNA SYNTHETASE
TITLE 2 IN COMPLEX WITH L-SERINE: RE-REFINED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALANYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL CATALYTIC FRAGMENT, UNP RESIDUES 2-454;
COMPND 5 SYNONYM: ALANINE--TRNA LIGASE, ALARS;
COMPND 6 EC: 6.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: ALAS, AQ_1293;
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 ADENOSINE TRIPHOSPHATE, ALANINE-TRNA LIGASE, BINDING SITES, GENETIC
KEYWDS 2 CODE, PROTEIN CONFORMATION, AMINOACYL-TRNA SYNTHETASE, ATP-BINDING,
KEYWDS 3 CYTOPLASM, LIGASE, NUCLEOTIDE-BINDING, PROTEIN BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GUO,M.A.SWAIRJO,P.SCHIMMEL
REVDAT 2 06-SEP-23 3HTZ 1 SEQADV
REVDAT 1 30-JUN-09 3HTZ 0
JRNL AUTH M.GUO,P.SCHIMMEL
JRNL TITL SERINE PARADOX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.A.SWAIRJO,P.SCHIMMEL
REMARK 1 TITL BREAKING SIEVE FOR STERIC EXCLUSION OF A NONCOGNATE AMINO
REMARK 1 TITL 2 ACID FROM ACTIVE SITE OF A TRNA SYNTHETASE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 102 988 2005
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 16377
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 + TEST SET) : 0.253
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.315
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 882
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1202
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.4370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3631
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 59
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.28000
REMARK 3 B22 (A**2) : 1.28000
REMARK 3 B33 (A**2) : -2.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.969
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.383
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.311
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.933
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.898
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.847
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3714 ; 0.003 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5001 ; 0.763 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 445 ; 4.459 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 187 ;32.704 ;23.743
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 670 ;15.374 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;18.100 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 524 ; 0.053 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2837 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1832 ; 0.220 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2569 ; 0.325 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 241 ; 0.227 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 64 ; 0.186 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.220 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2259 ; 0.609 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3565 ; 0.990 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1624 ; 0.459 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1436 ; 0.678 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3HTZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053579.
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) : 100
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) : NULL
REMARK 200 MONOCHROMATOR : CURVED CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
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 (%) : 98.7
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) : 2.48
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1YFS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
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 298.0K
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 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: 3210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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 HIS A 427
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 OD1 ASN A 95 OG1 THR A 218 1.85
REMARK 500 O GLU A 422 N LYS A 426 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 17 10.11 -69.42
REMARK 500 LYS A 18 48.11 -148.82
REMARK 500 ARG A 22 96.04 -68.49
REMARK 500 ASP A 33 73.60 -166.96
REMARK 500 PRO A 57 -5.45 -58.66
REMARK 500 ASP A 100 -93.34 -97.54
REMARK 500 PHE A 102 -140.29 -119.05
REMARK 500 MET A 198 88.95 -65.20
REMARK 500 PHE A 315 -23.43 -143.90
REMARK 500 ASP A 409 94.46 -68.51
REMARK 500 LYS A 443 -24.94 94.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YGB RELATED DB: PDB
REMARK 900 THE SAME DIFFRACTION DATA, RE-REFINED
DBREF 3HTZ A 1 453 UNP O67323 SYA_AQUAE 2 454
SEQADV 3HTZ ALA A 454 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ ALA A 455 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ ALA A 456 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ LEU A 457 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ GLU A 458 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ HIS A 459 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ HIS A 460 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ HIS A 461 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ HIS A 462 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ HIS A 463 UNP O67323 EXPRESSION TAG
SEQADV 3HTZ HIS A 464 UNP O67323 EXPRESSION TAG
SEQRES 1 A 464 SER LEU SER ALA HIS GLU ILE ARG GLU LEU PHE LEU SER
SEQRES 2 A 464 PHE PHE GLU LYS LYS GLY HIS THR ARG VAL LYS SER ALA
SEQRES 3 A 464 PRO LEU VAL PRO GLU ASN ASP PRO THR LEU LEU PHE VAL
SEQRES 4 A 464 ASN ALA GLY MET VAL PRO PHE LYS ASN VAL PHE LEU GLY
SEQRES 5 A 464 LEU GLU LYS ARG PRO TYR LYS ARG ALA THR SER CYS GLN
SEQRES 6 A 464 LYS CYS LEU ARG VAL SER GLY LYS HIS ASN ASP LEU GLU
SEQRES 7 A 464 GLN VAL GLY TYR THR SER ARG HIS HIS THR PHE PHE GLU
SEQRES 8 A 464 MET LEU GLY ASN PHE SER PHE GLY ASP TYR PHE LYS LYS
SEQRES 9 A 464 GLU ALA ILE GLU TYR ALA TRP GLU PHE VAL THR GLU VAL
SEQRES 10 A 464 LEU LYS LEU PRO LYS GLU LYS LEU TYR VAL SER VAL TYR
SEQRES 11 A 464 LYS ASP ASP GLU GLU ALA TYR ARG ILE TRP ASN GLU HIS
SEQRES 12 A 464 ILE GLY ILE PRO SER GLU ARG ILE TRP ARG LEU GLY GLU
SEQRES 13 A 464 GLU ASP ASN PHE TRP GLN MET GLY ASP VAL GLY PRO CYS
SEQRES 14 A 464 GLY PRO SER SER GLU ILE TYR VAL ASP ARG GLY GLU GLU
SEQRES 15 A 464 TYR GLU GLY ASP GLU ARG TYR LEU GLU ILE TRP ASN LEU
SEQRES 16 A 464 VAL PHE MET GLN TYR ASN ARG ASP GLU ASN GLY VAL LEU
SEQRES 17 A 464 THR PRO LEU PRO HIS PRO ASN ILE ASP THR GLY MET GLY
SEQRES 18 A 464 LEU GLU ARG ILE ALA SER VAL LEU GLN GLY LYS ASN SER
SEQRES 19 A 464 ASN PHE GLU ILE ASP ILE ILE PHE PRO LEU ILE GLN PHE
SEQRES 20 A 464 GLY GLU GLU VAL SER GLY LYS LYS TYR GLY GLU LYS PHE
SEQRES 21 A 464 GLU THR ASP VAL ALA LEU ARG VAL ILE ALA ASP HIS LEU
SEQRES 22 A 464 ARG ALA ILE THR PHE ALA ILE SER ASP GLY VAL ILE PRO
SEQRES 23 A 464 SER ASN GLU GLY ARG GLY TYR VAL ILE ARG ARG ILE LEU
SEQRES 24 A 464 ARG ARG ALA MET ARG PHE GLY TYR LYS LEU GLY ILE GLU
SEQRES 25 A 464 ASN PRO PHE LEU TYR LYS GLY VAL ASP LEU VAL VAL ASP
SEQRES 26 A 464 ILE MET LYS GLU PRO TYR PRO GLU LEU GLU LEU SER ARG
SEQRES 27 A 464 GLU PHE VAL LYS GLY ILE VAL LYS GLY GLU GLU LYS ARG
SEQRES 28 A 464 PHE ILE LYS THR LEU LYS ALA GLY MET GLU TYR ILE GLN
SEQRES 29 A 464 GLU VAL ILE GLN LYS ALA LEU GLU GLU GLY ARG LYS THR
SEQRES 30 A 464 LEU SER GLY LYS GLU VAL PHE THR ALA TYR ASP THR TYR
SEQRES 31 A 464 GLY PHE PRO VAL ASP LEU ILE ASP GLU ILE ALA ARG GLU
SEQRES 32 A 464 LYS GLY LEU GLY ILE ASP LEU GLU GLY PHE GLN CYS GLU
SEQRES 33 A 464 LEU GLU GLU GLN ARG GLU ARG ALA ARG LYS HIS PHE LYS
SEQRES 34 A 464 VAL GLU ALA LYS LYS VAL LYS PRO VAL TYR SER HIS LEU
SEQRES 35 A 464 LYS GLU LEU GLY LYS THR SER ALA PHE VAL GLY ALA ALA
SEQRES 36 A 464 ALA LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *59(H2 O)
HELIX 1 1 SER A 3 LYS A 17 1 15
HELIX 2 2 MET A 43 LYS A 47 5 5
HELIX 3 3 LEU A 77 VAL A 80 5 4
HELIX 4 4 PHE A 102 GLU A 116 1 15
HELIX 5 5 PRO A 121 GLU A 123 5 3
HELIX 6 6 ASP A 133 GLU A 142 1 10
HELIX 7 7 PRO A 147 GLU A 149 5 3
HELIX 8 8 GLY A 155 ASN A 159 1 5
HELIX 9 9 GLU A 184 ARG A 188 1 5
HELIX 10 10 LEU A 222 GLN A 230 1 9
HELIX 11 11 SER A 234 ILE A 238 5 5
HELIX 12 12 ILE A 241 GLY A 253 1 13
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 PHE A 315 MET A 327 1 13
HELIX 16 16 GLU A 333 GLU A 373 1 41
HELIX 17 17 SER A 379 THR A 389 1 11
HELIX 18 18 PRO A 393 GLU A 403 1 11
HELIX 19 19 ASP A 409 LYS A 426 1 18
HELIX 20 20 GLU A 444 SER A 449 1 6
HELIX 21 21 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 ARG A 60 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 MET A 220 N LEU A 93
SHEET 5 A 8 TYR A 189 ARG A 202 -1 N VAL A 196 O ASP A 217
SHEET 6 A 8 GLY A 167 ASP A 178 -1 N GLY A 167 O ARG A 202
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 ARG A 60 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 MET A 220 N LEU A 93
SHEET 5 B 7 TYR A 189 ARG A 202 -1 N VAL A 196 O ASP A 217
SHEET 6 B 7 GLY A 167 ASP A 178 -1 N GLY A 167 O ARG A 202
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
CISPEP 1 PHE A 98 GLY A 99 0 -21.76
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
