HEADER LIGASE 23-FEB-15 4YE8
TITLE THE CRYSTAL STRUCTURE OF THE Y57H MUTANT OF HUMAN GLNRS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMINE--TRNA LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLUTAMINYL-TRNA SYNTHETASE,GLNRS;
COMPND 5 EC: 6.1.1.18;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: QARS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS AMINOACYL-TRNA SYNTHETASE, CLASS I AARS, GLUTAMINE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OGNJENOVIC,J.WU,J.LING,M.SIMONOVIC
REVDAT 6 27-SEP-23 4YE8 1 REMARK
REVDAT 5 25-DEC-19 4YE8 1 REMARK
REVDAT 4 27-SEP-17 4YE8 1 JRNL REMARK
REVDAT 3 04-MAY-16 4YE8 1 JRNL
REVDAT 2 24-FEB-16 4YE8 1 JRNL
REVDAT 1 17-FEB-16 4YE8 0
JRNL AUTH J.OGNJENOVIC,J.WU,D.MATTHIES,U.BAXA,S.SUBRAMANIAM,J.LING,
JRNL AUTH 2 M.SIMONOVIC
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN GLNRS PROVIDES BASIS FOR THE
JRNL TITL 2 DEVELOPMENT OF NEUROLOGICAL DISORDERS.
JRNL REF NUCLEIC ACIDS RES. V. 44 3420 2016
JRNL REFN ESSN 1362-4962
JRNL PMID 26869582
JRNL DOI 10.1093/NAR/GKW082
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25874
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.720
REMARK 3 FREE R VALUE TEST SET COUNT : 1997
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.8762 - 7.9219 0.99 1845 155 0.1839 0.2257
REMARK 3 2 7.9219 - 6.3011 1.00 1771 148 0.2382 0.2806
REMARK 3 3 6.3011 - 5.5084 1.00 1726 144 0.2322 0.2850
REMARK 3 4 5.5084 - 5.0065 1.00 1706 143 0.2238 0.2845
REMARK 3 5 5.0065 - 4.6486 1.00 1714 145 0.1906 0.2720
REMARK 3 6 4.6486 - 4.3752 1.00 1699 141 0.1925 0.2343
REMARK 3 7 4.3752 - 4.1565 1.00 1666 139 0.2036 0.2630
REMARK 3 8 4.1565 - 3.9758 1.00 1711 144 0.2147 0.2660
REMARK 3 9 3.9758 - 3.8230 1.00 1662 139 0.2285 0.2890
REMARK 3 10 3.8230 - 3.6912 1.00 1673 140 0.2254 0.2935
REMARK 3 11 3.6912 - 3.5759 1.00 1715 143 0.2544 0.2951
REMARK 3 12 3.5759 - 3.4738 1.00 1659 139 0.2715 0.2964
REMARK 3 13 3.4738 - 3.3825 1.00 1663 140 0.3016 0.3559
REMARK 3 14 3.3825 - 3.3000 1.00 1667 137 0.3046 0.3721
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 74.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.015 5271
REMARK 3 ANGLE : 1.927 7197
REMARK 3 CHIRALITY : 0.098 814
REMARK 3 PLANARITY : 0.010 952
REMARK 3 DIHEDRAL : 14.681 1784
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4YE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25952
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.18900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.92600
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: PHASER
REMARK 200 STARTING MODEL: 4YE6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE, BIS-TRIS, 17% (W/V)
REMARK 280 PEG 10,000, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 166.54400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.12950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 166.54400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.12950
REMARK 290 SMTRY3 4 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: 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 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 ALA A 183
REMARK 465 ASP A 184
REMARK 465 LEU A 185
REMARK 465 GLU A 186
REMARK 465 LYS A 187
REMARK 465 LYS A 188
REMARK 465 PHE A 189
REMARK 465 LYS A 190
REMARK 465 VAL A 191
REMARK 465 ALA A 192
REMARK 465 LYS A 193
REMARK 465 ALA A 194
REMARK 465 ARG A 195
REMARK 465 LEU A 196
REMARK 465 GLU A 197
REMARK 465 GLU A 198
REMARK 465 THR A 199
REMARK 465 ASP A 200
REMARK 465 ARG A 201
REMARK 465 ARG A 202
REMARK 465 THR A 203
REMARK 465 ALA A 204
REMARK 465 LYS A 205
REMARK 465 ASP A 206
REMARK 465 VAL A 207
REMARK 465 VAL A 208
REMARK 465 GLU A 209
REMARK 465 ASN A 210
REMARK 465 GLY A 211
REMARK 465 GLU A 212
REMARK 465 THR A 213
REMARK 465 ALA A 214
REMARK 465 ASP A 215
REMARK 465 GLN A 216
REMARK 465 GLU A 363
REMARK 465 GLU A 364
REMARK 465 LEU A 365
REMARK 465 LYS A 366
REMARK 465 GLY A 367
REMARK 465 HIS A 368
REMARK 465 ASN A 369
REMARK 465 GLU A 459
REMARK 465 PHE A 460
REMARK 465 GLN A 461
REMARK 465 ALA A 585
REMARK 465 LYS A 586
REMARK 465 SER A 587
REMARK 465 LEU A 588
REMARK 465 PRO A 625
REMARK 465 LEU A 630
REMARK 465 ALA A 631
REMARK 465 TRP A 632
REMARK 465 GLY A 633
REMARK 465 GLN A 634
REMARK 465 PRO A 635
REMARK 465 VAL A 636
REMARK 465 GLY A 637
REMARK 465 LEU A 638
REMARK 465 ASP A 669
REMARK 465 ALA A 670
REMARK 465 GLY A 671
REMARK 465 GLU A 672
REMARK 465 LYS A 673
REMARK 465 PRO A 772
REMARK 465 GLY A 773
REMARK 465 LYS A 774
REMARK 465 VAL A 775
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 0 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 64 CG CD NE CZ NH1 NH2
REMARK 470 SER A 78 OG
REMARK 470 ARG A 95 NE CZ NH1 NH2
REMARK 470 LEU A 99 CG CD1 CD2
REMARK 470 ILE A 102 CG1 CG2 CD1
REMARK 470 VAL A 105 CG1 CG2
REMARK 470 ARG A 109 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 158 CD CE NZ
REMARK 470 LYS A 163 CG CD CE NZ
REMARK 470 GLU A 182 CG CD OE1 OE2
REMARK 470 THR A 217 OG1 CG2
REMARK 470 LEU A 218 CD1 CD2
REMARK 470 GLU A 222 CG CD OE1 OE2
REMARK 470 LYS A 230 CG CD CE NZ
REMARK 470 LYS A 233 CE NZ
REMARK 470 LYS A 309 CD CE NZ
REMARK 470 LYS A 313 CD CE NZ
REMARK 470 THR A 370 OG1 CG2
REMARK 470 LYS A 392 CD CE NZ
REMARK 470 GLU A 409 CG CD OE1 OE2
REMARK 470 LYS A 412 CD CE NZ
REMARK 470 LYS A 458 CG CD CE NZ
REMARK 470 ARG A 463 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 486 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 487 CG CD1 CD2
REMARK 470 ASN A 488 CG OD1 ND2
REMARK 470 LEU A 489 CG CD1 CD2
REMARK 470 TYR A 491 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 495 OG
REMARK 470 LYS A 498 CG CD CE NZ
REMARK 470 ARG A 509 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 515 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 538 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 539 CG1 CG2
REMARK 470 VAL A 541 CG1 CG2
REMARK 470 THR A 542 OG1 CG2
REMARK 470 VAL A 543 CG1 CG2
REMARK 470 GLN A 545 CG CD OE1 NE2
REMARK 470 THR A 546 OG1 CG2
REMARK 470 THR A 547 OG1 CG2
REMARK 470 GLU A 549 CG CD OE1 OE2
REMARK 470 LEU A 552 CG CD1 CD2
REMARK 470 THR A 564 OG1 CG2
REMARK 470 ARG A 567 NE CZ NH1 NH2
REMARK 470 MET A 569 CG SD CE
REMARK 470 LEU A 572 CG CD1 CD2
REMARK 470 GLU A 573 CG CD OE1 OE2
REMARK 470 SER A 574 OG
REMARK 470 LEU A 575 CG CD1 CD2
REMARK 470 ARG A 576 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 577 CG1 CG2
REMARK 470 ILE A 578 CG1 CG2 CD1
REMARK 470 ILE A 579 CG1 CG2 CD1
REMARK 470 THR A 580 OG1 CG2
REMARK 470 ASN A 581 CG OD1 ND2
REMARK 470 ASP A 589 CG OD1 OD2
REMARK 470 ILE A 590 CG1 CG2 CD1
REMARK 470 VAL A 592 CG1 CG2
REMARK 470 GLU A 599 CG CD OE1 OE2
REMARK 470 THR A 600 OG1 CG2
REMARK 470 LYS A 601 CG CD CE NZ
REMARK 470 GLN A 605 CG CD OE1 NE2
REMARK 470 VAL A 606 CG1 CG2
REMARK 470 PHE A 608 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO A 610 CG CD
REMARK 470 ILE A 611 CG1 CG2 CD1
REMARK 470 VAL A 612 CG1 CG2
REMARK 470 PHE A 613 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 614 CG1 CG2 CD1
REMARK 470 GLU A 615 CG CD OE1 OE2
REMARK 470 ARG A 616 CG CD NE CZ NH1 NH2
REMARK 470 THR A 617 OG1 CG2
REMARK 470 PHE A 619 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 620 CG CD CE NZ
REMARK 470 GLU A 621 CG CD OE1 OE2
REMARK 470 GLU A 622 CG CD OE1 OE2
REMARK 470 GLU A 624 CG CD OE1 OE2
REMARK 470 PHE A 627 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 628 CG CD CE NZ
REMARK 470 ARG A 629 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 639 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 640 CG ND1 CD2 CE1 NE2
REMARK 470 THR A 641 OG1 CG2
REMARK 470 TYR A 643 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 644 CG1 CG2
REMARK 470 ILE A 645 CG1 CG2 CD1
REMARK 470 GLU A 646 CG CD OE1 OE2
REMARK 470 LEU A 647 CG CD1 CD2
REMARK 470 GLN A 648 CG CD OE1 NE2
REMARK 470 HIS A 649 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 650 CG1 CG2
REMARK 470 VAL A 651 CG1 CG2
REMARK 470 LYS A 652 CG CD CE NZ
REMARK 470 PRO A 654 CG CD
REMARK 470 SER A 655 OG
REMARK 470 CYS A 657 SG
REMARK 470 GLU A 659 CG CD OE1 OE2
REMARK 470 SER A 660 OG
REMARK 470 LEU A 661 CG CD1 CD2
REMARK 470 GLU A 662 CG CD OE1 OE2
REMARK 470 VAL A 663 CG1 CG2
REMARK 470 THR A 664 OG1 CG2
REMARK 470 ARG A 666 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 667 CG CD NE CZ NH1 NH2
REMARK 470 PRO A 674 CG CD
REMARK 470 LYS A 675 CG CD CE NZ
REMARK 470 PHE A 677 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 678 CG1 CG2 CD1
REMARK 470 VAL A 681 CG1 CG2
REMARK 470 SER A 682 OG
REMARK 470 GLN A 683 CG CD OE1 NE2
REMARK 470 LEU A 685 CG CD1 CD2
REMARK 470 MET A 686 CG SD CE
REMARK 470 ARG A 690 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 691 CG CD1 CD2
REMARK 470 GLU A 693 CG CD OE1 OE2
REMARK 470 ARG A 694 CD NE CZ NH1 NH2
REMARK 470 LEU A 695 CG CD1 CD2
REMARK 470 GLN A 697 CG CD OE1 NE2
REMARK 470 HIS A 698 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 699 CG CD CE NZ
REMARK 470 ASN A 700 CG OD1 ND2
REMARK 470 GLU A 702 CG CD OE1 OE2
REMARK 470 ASP A 703 CG OD1 OD2
REMARK 470 THR A 705 OG1 CG2
REMARK 470 GLU A 706 CG CD OE1 OE2
REMARK 470 VAL A 707 CG1 CG2
REMARK 470 PHE A 711 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 712 CG CD1 CD2
REMARK 470 SER A 713 OG
REMARK 470 ASP A 714 CG OD1 OD2
REMARK 470 LEU A 715 CG CD1 CD2
REMARK 470 ASN A 716 CG OD1 ND2
REMARK 470 LEU A 717 CG CD1 CD2
REMARK 470 LEU A 720 CG CD1 CD2
REMARK 470 HIS A 721 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 722 CG1 CG2
REMARK 470 ASP A 724 CG OD1 OD2
REMARK 470 LEU A 727 CG CD1 CD2
REMARK 470 VAL A 728 CG1 CG2
REMARK 470 VAL A 732 CG1 CG2
REMARK 470 LEU A 734 CG CD1 CD2
REMARK 470 LYS A 736 CG CD CE NZ
REMARK 470 LYS A 740 CG CD CE NZ
REMARK 470 PHE A 741 CE1 CE2 CZ
REMARK 470 GLU A 744 CG CD OE1 OE2
REMARK 470 ARG A 745 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 746 CG CD1 CD2
REMARK 470 SER A 750 OG
REMARK 470 LYS A 759 CG CD CE NZ
REMARK 470 LEU A 760 CD1 CD2
REMARK 470 LYS A 769 CG CD CE NZ
REMARK 470 GLU A 770 CG CD OE1 OE2
REMARK 470 ASP A 771 CG OD1 OD2
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 ASP A 106 OE2 GLU A 110 2.12
REMARK 500 OH TYR A 338 OE2 GLU A 449 2.18
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 PRO A 708 CD PRO A 708 N 0.090
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 LYS A 80 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 ALA A 507 CB - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO A 593 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 PRO A 607 CB - CA - C ANGL. DEV. = -21.8 DEGREES
REMARK 500 PHE A 608 N - CA - CB ANGL. DEV. = -16.8 DEGREES
REMARK 500 PHE A 627 N - CA - C ANGL. DEV. = -21.4 DEGREES
REMARK 500 LYS A 628 N - CA - CB ANGL. DEV. = -19.7 DEGREES
REMARK 500 PRO A 704 N - CA - C ANGL. DEV. = -17.9 DEGREES
REMARK 500 THR A 705 N - CA - CB ANGL. DEV. = 11.5 DEGREES
REMARK 500 THR A 705 N - CA - C ANGL. DEV. = -20.3 DEGREES
REMARK 500 GLU A 706 N - CA - C ANGL. DEV. = -20.0 DEGREES
REMARK 500 VAL A 707 N - CA - CB ANGL. DEV. = -22.3 DEGREES
REMARK 500 VAL A 707 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 VAL A 723 CB - CA - C ANGL. DEV. = 18.4 DEGREES
REMARK 500 ASP A 724 N - CA - CB ANGL. DEV. = -18.4 DEGREES
REMARK 500 ASP A 724 N - CA - C ANGL. DEV. = 20.7 DEGREES
REMARK 500 LYS A 740 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 PHE A 741 CB - CA - C ANGL. DEV. = -15.0 DEGREES
REMARK 500 GLN A 742 N - CA - CB ANGL. DEV. = -10.8 DEGREES
REMARK 500 PHE A 743 N - CA - C ANGL. DEV. = -31.7 DEGREES
REMARK 500 GLU A 744 N - CA - CB ANGL. DEV. = -22.1 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 ALA A 2 21.43 -73.59
REMARK 500 LEU A 63 106.72 -58.97
REMARK 500 LYS A 80 -43.70 -138.39
REMARK 500 HIS A 82 29.13 -145.68
REMARK 500 SER A 96 -166.64 -103.90
REMARK 500 CYS A 111 21.18 -147.47
REMARK 500 ARG A 132 0.15 -68.13
REMARK 500 ARG A 141 -136.71 58.47
REMARK 500 ALA A 155 22.90 -72.52
REMARK 500 TRP A 159 45.80 -109.09
REMARK 500 ASP A 161 104.16 -59.96
REMARK 500 PRO A 247 10.73 -68.50
REMARK 500 PRO A 269 67.34 -119.43
REMARK 500 ASN A 273 36.39 -97.58
REMARK 500 ILE A 278 -38.81 -36.66
REMARK 500 ASP A 304 46.50 -104.27
REMARK 500 ARG A 361 -76.05 -135.67
REMARK 500 LYS A 392 1.64 -67.77
REMARK 500 ASP A 414 74.25 38.12
REMARK 500 HIS A 442 32.05 -84.70
REMARK 500 SER A 495 108.90 -58.87
REMARK 500 LYS A 496 -38.01 -37.85
REMARK 500 VAL A 541 -162.68 -161.05
REMARK 500 ALA A 568 -156.95 -157.71
REMARK 500 ALA A 570 158.53 178.36
REMARK 500 PRO A 583 -47.97 -27.99
REMARK 500 PHE A 627 -164.94 -105.54
REMARK 500 LYS A 628 -143.87 -119.22
REMARK 500 TYR A 643 -152.76 -127.30
REMARK 500 GLN A 648 -79.20 -98.59
REMARK 500 SER A 655 -136.08 60.83
REMARK 500 CYS A 665 51.90 -115.69
REMARK 500 LYS A 675 -123.46 62.24
REMARK 500 VAL A 681 112.55 -160.05
REMARK 500 GLN A 683 58.50 38.38
REMARK 500 PRO A 704 105.60 -54.79
REMARK 500 THR A 705 -59.21 -126.41
REMARK 500 SER A 719 -114.92 61.02
REMARK 500 VAL A 732 56.20 -93.13
REMARK 500 ASP A 739 56.11 -104.30
REMARK 500 PHE A 741 -169.74 -128.57
REMARK 500 PRO A 753 32.74 -68.38
REMARK 500 LYS A 769 -165.62 -164.18
REMARK 500 GLU A 770 -77.10 -135.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 485 ARG A 486 136.36
REMARK 500 ASP A 724 ALA A 725 -140.72
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 ARG A 267 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YE6 RELATED DB: PDB
REMARK 900 RELATED ID: 4YE9 RELATED DB: PDB
DBREF 4YE8 A 1 775 UNP P47897 SYQ_HUMAN 1 775
SEQADV 4YE8 HIS A 0 UNP P47897 EXPRESSION TAG
SEQADV 4YE8 HIS A 57 UNP P47897 TYR 57 ENGINEERED MUTATION
SEQRES 1 A 776 HIS MET ALA ALA LEU ASP SER LEU SER LEU PHE THR SER
SEQRES 2 A 776 LEU GLY LEU SER GLU GLN LYS ALA ARG GLU THR LEU LYS
SEQRES 3 A 776 ASN SER ALA LEU SER ALA GLN LEU ARG GLU ALA ALA THR
SEQRES 4 A 776 GLN ALA GLN GLN THR LEU GLY SER THR ILE ASP LYS ALA
SEQRES 5 A 776 THR GLY ILE LEU LEU HIS GLY LEU ALA SER ARG LEU ARG
SEQRES 6 A 776 ASP THR ARG ARG LEU SER PHE LEU VAL SER TYR ILE ALA
SEQRES 7 A 776 SER LYS LYS ILE HIS THR GLU PRO GLN LEU SER ALA ALA
SEQRES 8 A 776 LEU GLU TYR VAL ARG SER HIS PRO LEU ASP PRO ILE ASP
SEQRES 9 A 776 THR VAL ASP PHE GLU ARG GLU CYS GLY VAL GLY VAL ILE
SEQRES 10 A 776 VAL THR PRO GLU GLN ILE GLU GLU ALA VAL GLU ALA ALA
SEQRES 11 A 776 ILE ASN ARG HIS ARG PRO GLN LEU LEU VAL GLU ARG TYR
SEQRES 12 A 776 HIS PHE ASN MET GLY LEU LEU MET GLY GLU ALA ARG ALA
SEQRES 13 A 776 VAL LEU LYS TRP ALA ASP GLY LYS MET ILE LYS ASN GLU
SEQRES 14 A 776 VAL ASP MET GLN VAL LEU HIS LEU LEU GLY PRO LYS LEU
SEQRES 15 A 776 GLU ALA ASP LEU GLU LYS LYS PHE LYS VAL ALA LYS ALA
SEQRES 16 A 776 ARG LEU GLU GLU THR ASP ARG ARG THR ALA LYS ASP VAL
SEQRES 17 A 776 VAL GLU ASN GLY GLU THR ALA ASP GLN THR LEU SER LEU
SEQRES 18 A 776 MET GLU GLN LEU ARG GLY GLU ALA LEU LYS PHE HIS LYS
SEQRES 19 A 776 PRO GLY GLU ASN TYR LYS THR PRO GLY TYR VAL VAL THR
SEQRES 20 A 776 PRO HIS THR MET ASN LEU LEU LYS GLN HIS LEU GLU ILE
SEQRES 21 A 776 THR GLY GLY GLN VAL ARG THR ARG PHE PRO PRO GLU PRO
SEQRES 22 A 776 ASN GLY ILE LEU HIS ILE GLY HIS ALA LYS ALA ILE ASN
SEQRES 23 A 776 PHE ASN PHE GLY TYR ALA LYS ALA ASN ASN GLY ILE CYS
SEQRES 24 A 776 PHE LEU ARG PHE ASP ASP THR ASN PRO GLU LYS GLU GLU
SEQRES 25 A 776 ALA LYS PHE PHE THR ALA ILE CYS ASP MET VAL ALA TRP
SEQRES 26 A 776 LEU GLY TYR THR PRO TYR LYS VAL THR TYR ALA SER ASP
SEQRES 27 A 776 TYR PHE ASP GLN LEU TYR ALA TRP ALA VAL GLU LEU ILE
SEQRES 28 A 776 ARG ARG GLY LEU ALA TYR VAL CYS HIS GLN ARG GLY GLU
SEQRES 29 A 776 GLU LEU LYS GLY HIS ASN THR LEU PRO SER PRO TRP ARG
SEQRES 30 A 776 ASP ARG PRO MET GLU GLU SER LEU LEU LEU PHE GLU ALA
SEQRES 31 A 776 MET ARG LYS GLY LYS PHE SER GLU GLY GLU ALA THR LEU
SEQRES 32 A 776 ARG MET LYS LEU VAL MET GLU ASP GLY LYS MET ASP PRO
SEQRES 33 A 776 VAL ALA TYR ARG VAL LYS TYR THR PRO HIS HIS ARG THR
SEQRES 34 A 776 GLY ASP LYS TRP CYS ILE TYR PRO THR TYR ASP TYR THR
SEQRES 35 A 776 HIS CYS LEU CYS ASP SER ILE GLU HIS ILE THR HIS SER
SEQRES 36 A 776 LEU CYS THR LYS GLU PHE GLN ALA ARG ARG SER SER TYR
SEQRES 37 A 776 PHE TRP LEU CYS ASN ALA LEU ASP VAL TYR CYS PRO VAL
SEQRES 38 A 776 GLN TRP GLU TYR GLY ARG LEU ASN LEU HIS TYR ALA VAL
SEQRES 39 A 776 VAL SER LYS ARG LYS ILE LEU GLN LEU VAL ALA THR GLY
SEQRES 40 A 776 ALA VAL ARG ASP TRP ASP ASP PRO ARG LEU PHE THR LEU
SEQRES 41 A 776 THR ALA LEU ARG ARG ARG GLY PHE PRO PRO GLU ALA ILE
SEQRES 42 A 776 ASN ASN PHE CYS ALA ARG VAL GLY VAL THR VAL ALA GLN
SEQRES 43 A 776 THR THR MET GLU PRO HIS LEU LEU GLU ALA CYS VAL ARG
SEQRES 44 A 776 ASP VAL LEU ASN ASP THR ALA PRO ARG ALA MET ALA VAL
SEQRES 45 A 776 LEU GLU SER LEU ARG VAL ILE ILE THR ASN PHE PRO ALA
SEQRES 46 A 776 ALA LYS SER LEU ASP ILE GLN VAL PRO ASN PHE PRO ALA
SEQRES 47 A 776 ASP GLU THR LYS GLY PHE HIS GLN VAL PRO PHE ALA PRO
SEQRES 48 A 776 ILE VAL PHE ILE GLU ARG THR ASP PHE LYS GLU GLU PRO
SEQRES 49 A 776 GLU PRO GLY PHE LYS ARG LEU ALA TRP GLY GLN PRO VAL
SEQRES 50 A 776 GLY LEU ARG HIS THR GLY TYR VAL ILE GLU LEU GLN HIS
SEQRES 51 A 776 VAL VAL LYS GLY PRO SER GLY CYS VAL GLU SER LEU GLU
SEQRES 52 A 776 VAL THR CYS ARG ARG ALA ASP ALA GLY GLU LYS PRO LYS
SEQRES 53 A 776 ALA PHE ILE HIS TRP VAL SER GLN PRO LEU MET CYS GLU
SEQRES 54 A 776 VAL ARG LEU TYR GLU ARG LEU PHE GLN HIS LYS ASN PRO
SEQRES 55 A 776 GLU ASP PRO THR GLU VAL PRO GLY GLY PHE LEU SER ASP
SEQRES 56 A 776 LEU ASN LEU ALA SER LEU HIS VAL VAL ASP ALA ALA LEU
SEQRES 57 A 776 VAL ASP CYS SER VAL ALA LEU ALA LYS PRO PHE ASP LYS
SEQRES 58 A 776 PHE GLN PHE GLU ARG LEU GLY TYR PHE SER VAL ASP PRO
SEQRES 59 A 776 ASP SER HIS GLN GLY LYS LEU VAL PHE ASN ARG THR VAL
SEQRES 60 A 776 THR LEU LYS GLU ASP PRO GLY LYS VAL
FORMUL 2 HOH *18(H2 O)
HELIX 1 AA1 ASP A 5 SER A 12 1 8
HELIX 2 AA2 SER A 16 ASN A 26 1 11
HELIX 3 AA3 ALA A 28 GLN A 39 1 12
HELIX 4 AA4 ASP A 49 LEU A 63 1 15
HELIX 5 AA5 ASP A 65 ARG A 67 5 3
HELIX 6 AA6 ARG A 68 SER A 78 1 11
HELIX 7 AA7 THR A 83 SER A 96 1 14
HELIX 8 AA8 ASP A 103 GLU A 110 1 8
HELIX 9 AA9 THR A 118 ARG A 132 1 15
HELIX 10 AB1 HIS A 133 ARG A 141 1 9
HELIX 11 AB2 TYR A 142 PHE A 144 5 3
HELIX 12 AB3 ASN A 145 ALA A 155 1 11
HELIX 13 AB4 ASP A 161 GLY A 178 1 18
HELIX 14 AB5 ARG A 225 LEU A 229 5 5
HELIX 15 AB6 GLU A 236 THR A 240 5 5
HELIX 16 AB7 HIS A 248 GLY A 261 1 14
HELIX 17 AB8 GLY A 279 ALA A 293 1 15
HELIX 18 AB9 GLU A 311 LEU A 325 1 15
HELIX 19 AC1 TYR A 338 ARG A 352 1 15
HELIX 20 AC2 PRO A 379 LYS A 392 1 14
HELIX 21 AC3 THR A 437 GLU A 449 1 13
HELIX 22 AC4 SER A 466 LEU A 474 1 9
HELIX 23 AC5 SER A 495 LEU A 500 1 6
HELIX 24 AC6 THR A 518 ARG A 525 1 8
HELIX 25 AC7 PRO A 528 VAL A 539 1 12
HELIX 26 AC8 PRO A 550 ALA A 565 1 16
HELIX 27 AC9 CYS A 730 ALA A 733 5 4
SHEET 1 AA1 3 ARG A 265 PHE A 268 0
SHEET 2 AA1 3 ILE A 297 PHE A 302 1 O ILE A 297 N THR A 266
SHEET 3 AA1 3 VAL A 332 TYR A 334 1 O THR A 333 N PHE A 302
SHEET 1 AA2 4 ALA A 355 CYS A 358 0
SHEET 2 AA2 4 THR A 401 MET A 404 -1 O THR A 401 N CYS A 358
SHEET 3 AA2 4 VAL A 416 VAL A 420 -1 O ALA A 417 N LEU A 402
SHEET 4 AA2 4 ILE A 434 PRO A 436 -1 O TYR A 435 N ARG A 419
SHEET 1 AA3 2 HIS A 453 LEU A 455 0
SHEET 2 AA3 2 VAL A 480 TRP A 482 1 O VAL A 480 N SER A 454
SHEET 1 AA4 2 ASN A 488 LEU A 489 0
SHEET 2 AA4 2 THR A 547 MET A 548 1 O MET A 548 N ASN A 488
SHEET 1 AA5 2 ARG A 567 ALA A 568 0
SHEET 2 AA5 2 GLN A 742 PHE A 743 1 O GLN A 742 N ALA A 568
SHEET 1 AA6 4 ALA A 570 VAL A 571 0
SHEET 2 AA6 4 ALA A 726 VAL A 728 -1 O LEU A 727 N VAL A 571
SHEET 3 AA6 4 LEU A 685 TYR A 692 -1 N CYS A 687 O ALA A 726
SHEET 4 AA6 4 LEU A 720 VAL A 722 -1 O HIS A 721 N LEU A 691
SHEET 1 AA7 5 ALA A 570 VAL A 571 0
SHEET 2 AA7 5 ALA A 726 VAL A 728 -1 O LEU A 727 N VAL A 571
SHEET 3 AA7 5 LEU A 685 TYR A 692 -1 N CYS A 687 O ALA A 726
SHEET 4 AA7 5 VAL A 761 VAL A 766 1 O ARG A 764 N ARG A 690
SHEET 5 AA7 5 TYR A 748 VAL A 751 -1 N SER A 750 O ASN A 763
SHEET 1 AA8 2 SER A 574 ARG A 576 0
SHEET 2 AA8 2 PHE A 613 GLU A 615 -1 O ILE A 614 N LEU A 575
SHEET 1 AA9 3 ILE A 578 ILE A 579 0
SHEET 2 AA9 3 LEU A 661 VAL A 663 1 O LEU A 661 N ILE A 578
SHEET 3 AA9 3 LEU A 647 VAL A 650 -1 N GLN A 648 O GLU A 662
CRYST1 333.088 58.259 85.132 90.00 90.00 90.00 P 21 21 2 4
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 0.003002 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017165 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011746 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
