HEADER LIGASE 19-SEP-08 2ZT5
TITLE CRYSTAL STRUCTURE OF HUMAN GLYCYL-TRNA SYNTHETASE (GLYRS) IN COMPLEX
TITLE 2 WITH AP4A (COCRYSTALLIZED WITH ATP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 55-739;
COMPND 5 SYNONYM: GLYCINE-TRNA LIGASE, GLYRS;
COMPND 6 EC: 6.1.1.14;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GARS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS LIGASE, AP4A, GLYCINE, ATP, GLY-AMP, TRNA, AMINOACYL-TRNA SYNTHETASE,
KEYWDS 2 ATP-BINDING, CHARCOT-MARIE-TOOTH DISEASE, DISEASE MUTATION,
KEYWDS 3 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, PROTEIN BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR R.T.GUO,X.L.YANG,P.SCHIMMEL
REVDAT 2 01-NOV-23 2ZT5 1 SEQADV
REVDAT 1 25-AUG-09 2ZT5 0
JRNL AUTH R.T.GUO,Y.E.CHONG,M.GUO,X.L.YANG
JRNL TITL CRYSTAL STRUCTURES AND BIOCHEMICAL ANALYSES SUGGEST UNIQUE
JRNL TITL 2 MECHANISM AND ROLE FOR HUMAN GLYRS IN AP4A HOMEOSTASIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
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) (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 34682
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) : 0.233
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1718
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3730
REMARK 3 BIN FREE R VALUE : 0.4030
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 128
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 : 4228
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 335
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.24
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) : 0.52
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) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.100
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 2ZT5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000028393.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-08
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 : 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) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
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 : 36185
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.28700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2PME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM TRIS-HCL, 150MM NACL, 10MM MGCL2,
REMARK 280 4M SODIUM FORMATE, PH7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.47150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.47150
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 57.93050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.92000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 57.93050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.92000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.47150
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 57.93050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.92000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 66.47150
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 57.93050
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 69.92000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 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
REMARK 350 TOTAL BURIED SURFACE AREA: 7630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.7 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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 132.94300
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 GLY A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 GLU A 8
REMARK 465 VAL A 9
REMARK 465 LEU A 10
REMARK 465 ALA A 11
REMARK 465 PRO A 12
REMARK 465 LEU A 13
REMARK 465 ARG A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 VAL A 17
REMARK 465 ARG A 18
REMARK 465 GLN A 19
REMARK 465 GLN A 20
REMARK 465 GLY A 21
REMARK 465 ASP A 22
REMARK 465 LEU A 23
REMARK 465 VAL A 24
REMARK 465 ARG A 25
REMARK 465 LYS A 26
REMARK 465 LEU A 27
REMARK 465 LYS A 28
REMARK 465 GLU A 29
REMARK 465 ASP A 30
REMARK 465 LYS A 31
REMARK 465 ALA A 32
REMARK 465 PRO A 33
REMARK 465 GLN A 34
REMARK 465 VAL A 35
REMARK 465 ASP A 36
REMARK 465 VAL A 37
REMARK 465 ASP A 38
REMARK 465 LYS A 39
REMARK 465 ALA A 40
REMARK 465 VAL A 41
REMARK 465 ALA A 42
REMARK 465 GLU A 43
REMARK 465 LEU A 44
REMARK 465 LYS A 45
REMARK 465 ALA A 46
REMARK 465 ARG A 47
REMARK 465 LYS A 48
REMARK 465 ARG A 49
REMARK 465 VAL A 50
REMARK 465 LEU A 51
REMARK 465 GLU A 52
REMARK 465 ALA A 53
REMARK 465 LYS A 54
REMARK 465 GLU A 55
REMARK 465 LEU A 56
REMARK 465 ALA A 57
REMARK 465 LEU A 58
REMARK 465 GLN A 59
REMARK 465 PRO A 60
REMARK 465 LYS A 61
REMARK 465 ASP A 62
REMARK 465 ASP A 63
REMARK 465 LEU A 432
REMARK 465 LYS A 433
REMARK 465 GLU A 434
REMARK 465 PRO A 435
REMARK 465 LYS A 436
REMARK 465 THR A 437
REMARK 465 VAL A 438
REMARK 465 ASN A 439
REMARK 465 VAL A 440
REMARK 465 VAL A 441
REMARK 465 GLN A 442
REMARK 465 PHE A 443
REMARK 465 GLU A 444
REMARK 465 PRO A 445
REMARK 465 SER A 446
REMARK 465 LYS A 447
REMARK 465 GLY A 448
REMARK 465 ALA A 449
REMARK 465 ILE A 450
REMARK 465 GLY A 451
REMARK 465 LYS A 452
REMARK 465 ALA A 453
REMARK 465 TYR A 454
REMARK 465 LYS A 455
REMARK 465 LYS A 456
REMARK 465 ASP A 457
REMARK 465 ALA A 458
REMARK 465 LYS A 459
REMARK 465 LEU A 460
REMARK 465 VAL A 461
REMARK 465 MET A 462
REMARK 465 GLU A 463
REMARK 465 TYR A 464
REMARK 465 LEU A 465
REMARK 465 ALA A 466
REMARK 465 ILE A 467
REMARK 465 CYS A 468
REMARK 465 ASP A 469
REMARK 465 GLU A 470
REMARK 465 CYS A 471
REMARK 465 TYR A 472
REMARK 465 ILE A 473
REMARK 465 THR A 474
REMARK 465 GLU A 475
REMARK 465 MET A 476
REMARK 465 GLU A 477
REMARK 465 MET A 478
REMARK 465 LEU A 479
REMARK 465 LEU A 480
REMARK 465 ASN A 481
REMARK 465 GLU A 482
REMARK 465 LYS A 483
REMARK 465 GLY A 484
REMARK 465 GLU A 485
REMARK 465 PHE A 486
REMARK 465 THR A 487
REMARK 465 ILE A 488
REMARK 465 GLU A 489
REMARK 465 THR A 490
REMARK 465 GLU A 491
REMARK 465 GLY A 492
REMARK 465 LYS A 493
REMARK 465 THR A 494
REMARK 465 PHE A 495
REMARK 465 GLN A 496
REMARK 465 LEU A 497
REMARK 465 THR A 498
REMARK 465 LYS A 499
REMARK 465 ASP A 500
REMARK 465 MET A 501
REMARK 465 ILE A 502
REMARK 465 ASN A 503
REMARK 465 VAL A 504
REMARK 465 LYS A 505
REMARK 465 ARG A 506
REMARK 465 PHE A 507
REMARK 465 GLN A 508
REMARK 465 LYS A 509
REMARK 465 THR A 510
REMARK 465 LEU A 511
REMARK 465 GLY A 674
REMARK 465 GLN A 675
REMARK 465 GLU A 676
REMARK 465 THR A 677
REMARK 465 GLY A 678
REMARK 465 LYS A 679
REMARK 465 LYS A 680
REMARK 465 GLU A 681
REMARK 465 THR A 682
REMARK 465 ILE A 683
REMARK 465 GLU A 684
REMARK 465 GLU A 685
REMARK 465 LEU A 686
REMARK 465 GLU A 687
REMARK 465 HIS A 688
REMARK 465 HIS A 689
REMARK 465 HIS A 690
REMARK 465 HIS A 691
REMARK 465 HIS A 692
REMARK 465 HIS A 693
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 ILE A 86 5.75 -64.56
REMARK 500 PHE A 115 -71.43 -111.93
REMARK 500 LYS A 153 -92.97 -61.45
REMARK 500 GLN A 191 13.59 -147.61
REMARK 500 THR A 214 55.02 37.07
REMARK 500 ASN A 261 31.73 -96.23
REMARK 500 ARG A 283 39.84 -149.09
REMARK 500 LYS A 306 53.03 -68.73
REMARK 500 ASN A 348 -81.04 -29.18
REMARK 500 ASN A 349 -165.58 -114.69
REMARK 500 MET A 383 142.10 -39.61
REMARK 500 ARG A 410 77.13 -54.08
REMARK 500 SER A 411 -112.39 -17.23
REMARK 500 GLN A 571 3.19 -61.16
REMARK 500 SER A 596 148.55 -39.80
REMARK 500 ASP A 619 -169.02 -101.94
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 B4P A1101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PME RELATED DB: PDB
REMARK 900 THE SAMPLE PROTEIN (APO FORM)
REMARK 900 RELATED ID: 2PMF RELATED DB: PDB
REMARK 900 G526R MUTANT
REMARK 900 RELATED ID: 2ZT6 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZT7 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZT8 RELATED DB: PDB
DBREF 2ZT5 A 1 685 UNP P41250 SYG_HUMAN 55 739
SEQADV 2ZT5 LEU A 686 UNP P41250 EXPRESSION TAG
SEQADV 2ZT5 GLU A 687 UNP P41250 EXPRESSION TAG
SEQADV 2ZT5 HIS A 688 UNP P41250 EXPRESSION TAG
SEQADV 2ZT5 HIS A 689 UNP P41250 EXPRESSION TAG
SEQADV 2ZT5 HIS A 690 UNP P41250 EXPRESSION TAG
SEQADV 2ZT5 HIS A 691 UNP P41250 EXPRESSION TAG
SEQADV 2ZT5 HIS A 692 UNP P41250 EXPRESSION TAG
SEQADV 2ZT5 HIS A 693 UNP P41250 EXPRESSION TAG
SEQRES 1 A 693 MET ASP GLY ALA GLY ALA GLU GLU VAL LEU ALA PRO LEU
SEQRES 2 A 693 ARG LEU ALA VAL ARG GLN GLN GLY ASP LEU VAL ARG LYS
SEQRES 3 A 693 LEU LYS GLU ASP LYS ALA PRO GLN VAL ASP VAL ASP LYS
SEQRES 4 A 693 ALA VAL ALA GLU LEU LYS ALA ARG LYS ARG VAL LEU GLU
SEQRES 5 A 693 ALA LYS GLU LEU ALA LEU GLN PRO LYS ASP ASP ILE VAL
SEQRES 6 A 693 ASP ARG ALA LYS MET GLU ASP THR LEU LYS ARG ARG PHE
SEQRES 7 A 693 PHE TYR ASP GLN ALA PHE ALA ILE TYR GLY GLY VAL SER
SEQRES 8 A 693 GLY LEU TYR ASP PHE GLY PRO VAL GLY CYS ALA LEU LYS
SEQRES 9 A 693 ASN ASN ILE ILE GLN THR TRP ARG GLN HIS PHE ILE GLN
SEQRES 10 A 693 GLU GLU GLN ILE LEU GLU ILE ASP CYS THR MET LEU THR
SEQRES 11 A 693 PRO GLU PRO VAL LEU LYS THR SER GLY HIS VAL ASP LYS
SEQRES 12 A 693 PHE ALA ASP PHE MET VAL LYS ASP VAL LYS ASN GLY GLU
SEQRES 13 A 693 CYS PHE ARG ALA ASP HIS LEU LEU LYS ALA HIS LEU GLN
SEQRES 14 A 693 LYS LEU MET SER ASP LYS LYS CYS SER VAL GLU LYS LYS
SEQRES 15 A 693 SER GLU MET GLU SER VAL LEU ALA GLN LEU ASP ASN TYR
SEQRES 16 A 693 GLY GLN GLN GLU LEU ALA ASP LEU PHE VAL ASN TYR ASN
SEQRES 17 A 693 VAL LYS SER PRO ILE THR GLY ASN ASP LEU SER PRO PRO
SEQRES 18 A 693 VAL SER PHE ASN LEU MET PHE LYS THR PHE ILE GLY PRO
SEQRES 19 A 693 GLY GLY ASN MET PRO GLY TYR LEU ARG PRO GLU THR ALA
SEQRES 20 A 693 GLN GLY ILE PHE LEU ASN PHE LYS ARG LEU LEU GLU PHE
SEQRES 21 A 693 ASN GLN GLY LYS LEU PRO PHE ALA ALA ALA GLN ILE GLY
SEQRES 22 A 693 ASN SER PHE ARG ASN GLU ILE SER PRO ARG SER GLY LEU
SEQRES 23 A 693 ILE ARG VAL ARG GLU PHE THR MET ALA GLU ILE GLU HIS
SEQRES 24 A 693 PHE VAL ASP PRO SER GLU LYS ASP HIS PRO LYS PHE GLN
SEQRES 25 A 693 ASN VAL ALA ASP LEU HIS LEU TYR LEU TYR SER ALA LYS
SEQRES 26 A 693 ALA GLN VAL SER GLY GLN SER ALA ARG LYS MET ARG LEU
SEQRES 27 A 693 GLY ASP ALA VAL GLU GLN GLY VAL ILE ASN ASN THR VAL
SEQRES 28 A 693 LEU GLY TYR PHE ILE GLY ARG ILE TYR LEU TYR LEU THR
SEQRES 29 A 693 LYS VAL GLY ILE SER PRO ASP LYS LEU ARG PHE ARG GLN
SEQRES 30 A 693 HIS MET GLU ASN GLU MET ALA HIS TYR ALA CYS ASP CYS
SEQRES 31 A 693 TRP ASP ALA GLU SER LYS THR SER TYR GLY TRP ILE GLU
SEQRES 32 A 693 ILE VAL GLY CYS ALA ASP ARG SER CYS TYR ASP LEU SER
SEQRES 33 A 693 CYS HIS ALA ARG ALA THR LYS VAL PRO LEU VAL ALA GLU
SEQRES 34 A 693 LYS PRO LEU LYS GLU PRO LYS THR VAL ASN VAL VAL GLN
SEQRES 35 A 693 PHE GLU PRO SER LYS GLY ALA ILE GLY LYS ALA TYR LYS
SEQRES 36 A 693 LYS ASP ALA LYS LEU VAL MET GLU TYR LEU ALA ILE CYS
SEQRES 37 A 693 ASP GLU CYS TYR ILE THR GLU MET GLU MET LEU LEU ASN
SEQRES 38 A 693 GLU LYS GLY GLU PHE THR ILE GLU THR GLU GLY LYS THR
SEQRES 39 A 693 PHE GLN LEU THR LYS ASP MET ILE ASN VAL LYS ARG PHE
SEQRES 40 A 693 GLN LYS THR LEU TYR VAL GLU GLU VAL VAL PRO ASN VAL
SEQRES 41 A 693 ILE GLU PRO SER PHE GLY LEU GLY ARG ILE MET TYR THR
SEQRES 42 A 693 VAL PHE GLU HIS THR PHE HIS VAL ARG GLU GLY ASP GLU
SEQRES 43 A 693 GLN ARG THR PHE PHE SER PHE PRO ALA VAL VAL ALA PRO
SEQRES 44 A 693 PHE LYS CYS SER VAL LEU PRO LEU SER GLN ASN GLN GLU
SEQRES 45 A 693 PHE MET PRO PHE VAL LYS GLU LEU SER GLU ALA LEU THR
SEQRES 46 A 693 ARG HIS GLY VAL SER HIS LYS VAL ASP ASP SER SER GLY
SEQRES 47 A 693 SER ILE GLY ARG ARG TYR ALA ARG THR ASP GLU ILE GLY
SEQRES 48 A 693 VAL ALA PHE GLY VAL THR ILE ASP PHE ASP THR VAL ASN
SEQRES 49 A 693 LYS THR PRO HIS THR ALA THR LEU ARG ASP ARG ASP SER
SEQRES 50 A 693 MET ARG GLN ILE ARG ALA GLU ILE SER GLU LEU PRO SER
SEQRES 51 A 693 ILE VAL GLN ASP LEU ALA ASN GLY ASN ILE THR TRP ALA
SEQRES 52 A 693 ASP VAL GLU ALA ARG TYR PRO LEU PHE GLU GLY GLN GLU
SEQRES 53 A 693 THR GLY LYS LYS GLU THR ILE GLU GLU LEU GLU HIS HIS
SEQRES 54 A 693 HIS HIS HIS HIS
HET B4P A1101 53
HETNAM B4P BIS(ADENOSINE)-5'-TETRAPHOSPHATE
FORMUL 2 B4P C20 H28 N10 O19 P4
FORMUL 3 HOH *335(H2 O)
HELIX 1 1 ASP A 66 ARG A 77 1 12
HELIX 2 2 PHE A 84 GLY A 88 5 5
HELIX 3 3 GLY A 97 PHE A 115 1 19
HELIX 4 4 PHE A 115 GLN A 120 1 6
HELIX 5 5 GLU A 132 SER A 138 1 7
HELIX 6 6 GLY A 139 PHE A 144 1 6
HELIX 7 7 ALA A 160 ASP A 174 1 15
HELIX 8 8 SER A 178 ALA A 190 1 13
HELIX 9 9 GLY A 196 TYR A 207 1 12
HELIX 10 10 THR A 246 LEU A 252 1 7
HELIX 11 11 ASN A 253 ASN A 261 1 9
HELIX 12 12 SER A 284 ARG A 288 5 5
HELIX 13 13 LYS A 310 VAL A 314 5 5
HELIX 14 14 SER A 323 SER A 329 1 7
HELIX 15 15 LEU A 338 GLN A 344 1 7
HELIX 16 16 ASN A 349 GLY A 367 1 19
HELIX 17 17 SER A 369 ASP A 371 5 3
HELIX 18 18 MET A 379 MET A 383 5 5
HELIX 19 19 CYS A 412 LYS A 423 1 12
HELIX 20 20 LEU A 527 THR A 538 1 12
HELIX 21 21 PHE A 573 HIS A 587 1 15
HELIX 22 22 SER A 599 ILE A 610 1 12
HELIX 23 23 ASP A 619 ASN A 624 1 6
HELIX 24 24 GLU A 647 ASN A 657 1 11
HELIX 25 25 THR A 661 TYR A 669 1 9
SHEET 1 A 2 TYR A 80 GLN A 82 0
SHEET 2 A 2 TYR A 94 PHE A 96 -1 O ASP A 95 N ASP A 81
SHEET 1 B 9 LEU A 122 GLU A 123 0
SHEET 2 B 9 PHE A 267 PHE A 276 1 O ALA A 270 N LEU A 122
SHEET 3 B 9 GLU A 291 VAL A 301 -1 O GLU A 298 N ALA A 269
SHEET 4 B 9 ASN A 519 GLY A 526 -1 O ASN A 519 N VAL A 301
SHEET 5 B 9 GLY A 400 ALA A 408 -1 N GLY A 406 O SER A 524
SHEET 6 B 9 CYS A 390 THR A 397 -1 N ALA A 393 O VAL A 405
SHEET 7 B 9 LEU A 373 GLN A 377 -1 N ARG A 374 O GLU A 394
SHEET 8 B 9 HIS A 318 TYR A 322 1 N TYR A 320 O PHE A 375
SHEET 9 B 9 ARG A 334 ARG A 337 -1 O ARG A 334 N LEU A 321
SHEET 1 C 3 LEU A 129 PRO A 131 0
SHEET 2 C 3 PRO A 239 LEU A 242 -1 O TYR A 241 N THR A 130
SHEET 3 C 3 LYS A 229 PHE A 231 -1 N THR A 230 O GLY A 240
SHEET 1 D 3 CYS A 157 ARG A 159 0
SHEET 2 D 3 ALA A 145 LYS A 150 -1 N VAL A 149 O PHE A 158
SHEET 3 D 3 VAL A 222 ASN A 225 -1 O VAL A 222 N MET A 148
SHEET 1 E 2 ALA A 428 LYS A 430 0
SHEET 2 E 2 GLU A 514 VAL A 516 -1 O GLU A 514 N LYS A 430
SHEET 1 F 2 PHE A 539 VAL A 541 0
SHEET 2 F 2 THR A 549 PHE A 551 -1 O PHE A 550 N HIS A 540
SHEET 1 G 5 HIS A 591 VAL A 593 0
SHEET 2 G 5 CYS A 562 PRO A 566 1 N VAL A 564 O LYS A 592
SHEET 3 G 5 PHE A 614 ILE A 618 1 O PHE A 614 N SER A 563
SHEET 4 G 5 THR A 629 ASP A 634 -1 O THR A 631 N THR A 617
SHEET 5 G 5 GLN A 640 GLU A 644 -1 O ALA A 643 N ALA A 630
CISPEP 1 LEU A 265 PRO A 266 0 -0.05
CISPEP 2 THR A 626 PRO A 627 0 -0.03
SITE 1 AC1 23 ASP A 146 ARG A 159 ASP A 193 LEU A 226
SITE 2 AC1 23 ARG A 277 GLU A 279 ILE A 287 ARG A 288
SITE 3 AC1 23 VAL A 289 PHE A 292 MET A 294 ASN A 381
SITE 4 AC1 23 GLU A 382 GLU A 403 ILE A 404 VAL A 405
SITE 5 AC1 23 GLY A 406 GLY A 526 ARG A 529 HOH A 918
SITE 6 AC1 23 HOH A 919 HOH A 920 HOH A1021
CRYST1 115.861 139.840 132.943 90.00 90.00 90.00 C 2 2 21 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 0.008631 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007151 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007522 0.00000
(ATOM LINES ARE NOT SHOWN.)
END