HEADER TRANSLATION 07-OCT-13 4N3G
TITLE CRYSTAL STRUCTURE OF EUKARYOTIC TRANSLATION INITIATION FACTOR EIF5B
TITLE 2 (870-1116) FROM CHAETOMIUM THERMOPHILUM, DOMAINS III AND IV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 5B-LIKE PROTEIN,
COMPND 3 EIF5B(870-C);
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 517-1092;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHAETOMIUM THERMOPHILUM VAR. THERMOPHILUM;
SOURCE 3 ORGANISM_TAXID: 759272;
SOURCE 4 STRAIN: DSM 1495 / CBS 144.50 / IMI 039719;
SOURCE 5 GENE: CTHT_0029840;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS TRANSLATION INITIATION, GTPASE, EIF5B/IF2, SUBUNIT JOINING, RIBOSOME,
KEYWDS 2 TRANSLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR B.KUHLE,R.FICNER
REVDAT 5 15-NOV-23 4N3G 1 REMARK SEQADV ATOM
REVDAT 4 07-MAR-18 4N3G 1 REMARK
REVDAT 3 06-AUG-14 4N3G 1 AUTHOR
REVDAT 2 23-JUL-14 4N3G 1 REMARK
REVDAT 1 09-JUL-14 4N3G 0
JRNL AUTH B.KUHLE,R.FICNER
JRNL TITL EIF5B EMPLOYS A NOVEL DOMAIN RELEASE MECHANISM TO CATALYZE
JRNL TITL 2 RIBOSOMAL SUBUNIT JOINING.
JRNL REF EMBO J. V. 33 1177 2014
JRNL REFN ISSN 0261-4189
JRNL PMID 24686316
JRNL DOI 10.1002/EMBJ.201387344
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 9266
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 465
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 43.8607 - 4.6187 1.00 3009 159 0.1688 0.1894
REMARK 3 2 4.6187 - 3.6666 1.00 2920 153 0.1966 0.2339
REMARK 3 3 3.6666 - 3.2033 1.00 2872 153 0.2801 0.3445
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 117.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.77
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 : 0.003 1975
REMARK 3 ANGLE : 0.611 2666
REMARK 3 CHIRALITY : 0.044 309
REMARK 3 PLANARITY : 0.002 341
REMARK 3 DIHEDRAL : 15.076 753
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 870 THROUGH 953 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7176 74.1236 29.1659
REMARK 3 T TENSOR
REMARK 3 T11: 0.6141 T22: 0.6719
REMARK 3 T33: 0.6195 T12: 0.0688
REMARK 3 T13: -0.0503 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 2.0932 L22: 1.6610
REMARK 3 L33: 0.8362 L12: 0.6487
REMARK 3 L13: -1.1258 L23: -0.9810
REMARK 3 S TENSOR
REMARK 3 S11: 0.3495 S12: 0.0171 S13: -0.0465
REMARK 3 S21: 0.1039 S22: -0.3168 S23: 0.3880
REMARK 3 S31: -0.3250 S32: 0.0282 S33: -0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 954 THROUGH 979 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5765 58.1594 23.1497
REMARK 3 T TENSOR
REMARK 3 T11: 0.4620 T22: 0.5380
REMARK 3 T33: 1.0357 T12: 0.0111
REMARK 3 T13: 0.0615 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 0.3210 L22: 1.4920
REMARK 3 L33: 0.4361 L12: 0.6151
REMARK 3 L13: -0.3428 L23: -0.2418
REMARK 3 S TENSOR
REMARK 3 S11: 0.0879 S12: 0.0027 S13: -0.6419
REMARK 3 S21: 0.5560 S22: -0.3679 S23: -0.6355
REMARK 3 S31: 0.6320 S32: -0.2993 S33: -0.0130
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 980 THROUGH 1083 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.6687 31.3816 3.2568
REMARK 3 T TENSOR
REMARK 3 T11: 0.6115 T22: 0.8178
REMARK 3 T33: 0.6081 T12: -0.1563
REMARK 3 T13: 0.1347 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 2.1510 L22: 1.1553
REMARK 3 L33: 0.9680 L12: 0.2609
REMARK 3 L13: -0.5366 L23: -1.1003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0317 S12: -0.0501 S13: 0.1741
REMARK 3 S21: -0.1869 S22: -0.2266 S23: -0.1399
REMARK 3 S31: 0.2781 S32: -0.3760 S33: -0.0006
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1084 THROUGH 1116 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4658 47.4760 2.3637
REMARK 3 T TENSOR
REMARK 3 T11: 0.6595 T22: 0.6410
REMARK 3 T33: 0.8965 T12: -0.0705
REMARK 3 T13: 0.0687 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 2.0961 L22: 1.4645
REMARK 3 L33: 1.9286 L12: 1.1169
REMARK 3 L13: -1.0817 L23: -0.6424
REMARK 3 S TENSOR
REMARK 3 S11: -0.1105 S12: -0.2964 S13: 0.7471
REMARK 3 S21: -0.0791 S22: -0.1612 S23: 0.4260
REMARK 3 S31: -0.8429 S32: 0.5504 S33: -0.4276
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 4N3G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082703.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.826580
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9288
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 99.795
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.03400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.57400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.310
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 12% PEG 20000, 10 MM NA
REMARK 280 -LACTATE, PH 6.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.47333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 64.94667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 64.94667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.47333
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 SER A 514
REMARK 465 HIS A 515
REMARK 465 MET A 516
REMARK 465 ASN A 517
REMARK 465 LYS A 518
REMARK 465 ASP A 519
REMARK 465 ASN A 520
REMARK 465 LEU A 521
REMARK 465 ARG A 522
REMARK 465 SER A 523
REMARK 465 PRO A 524
REMARK 465 ILE A 525
REMARK 465 CYS A 526
REMARK 465 CYS A 527
REMARK 465 ILE A 528
REMARK 465 LEU A 529
REMARK 465 GLY A 530
REMARK 465 HIS A 531
REMARK 465 VAL A 532
REMARK 465 ASP A 533
REMARK 465 THR A 534
REMARK 465 GLY A 535
REMARK 465 LYS A 536
REMARK 465 THR A 537
REMARK 465 LYS A 538
REMARK 465 LEU A 539
REMARK 465 LEU A 540
REMARK 465 ASP A 541
REMARK 465 LYS A 542
REMARK 465 ILE A 543
REMARK 465 ARG A 544
REMARK 465 GLN A 545
REMARK 465 THR A 546
REMARK 465 ASN A 547
REMARK 465 VAL A 548
REMARK 465 GLN A 549
REMARK 465 GLU A 550
REMARK 465 GLY A 551
REMARK 465 GLU A 552
REMARK 465 ALA A 553
REMARK 465 GLY A 554
REMARK 465 GLY A 555
REMARK 465 ILE A 556
REMARK 465 THR A 557
REMARK 465 GLN A 558
REMARK 465 GLN A 559
REMARK 465 ILE A 560
REMARK 465 GLY A 561
REMARK 465 ALA A 562
REMARK 465 THR A 563
REMARK 465 TYR A 564
REMARK 465 PHE A 565
REMARK 465 PRO A 566
REMARK 465 VAL A 567
REMARK 465 GLU A 568
REMARK 465 ALA A 569
REMARK 465 ILE A 570
REMARK 465 LYS A 571
REMARK 465 GLN A 572
REMARK 465 LYS A 573
REMARK 465 THR A 574
REMARK 465 ALA A 575
REMARK 465 VAL A 576
REMARK 465 VAL A 577
REMARK 465 ASN A 578
REMARK 465 LYS A 579
REMARK 465 ASP A 580
REMARK 465 GLY A 581
REMARK 465 LYS A 582
REMARK 465 PHE A 583
REMARK 465 GLU A 584
REMARK 465 PHE A 585
REMARK 465 LYS A 586
REMARK 465 VAL A 587
REMARK 465 PRO A 588
REMARK 465 GLY A 589
REMARK 465 LEU A 590
REMARK 465 LEU A 591
REMARK 465 ILE A 592
REMARK 465 ILE A 593
REMARK 465 ASP A 594
REMARK 465 THR A 595
REMARK 465 PRO A 596
REMARK 465 GLY A 597
REMARK 465 HIS A 598
REMARK 465 GLU A 599
REMARK 465 SER A 600
REMARK 465 PHE A 601
REMARK 465 SER A 602
REMARK 465 ASN A 603
REMARK 465 LEU A 604
REMARK 465 ARG A 605
REMARK 465 SER A 606
REMARK 465 ARG A 607
REMARK 465 GLY A 608
REMARK 465 SER A 609
REMARK 465 SER A 610
REMARK 465 LEU A 611
REMARK 465 CYS A 612
REMARK 465 ASN A 613
REMARK 465 ILE A 614
REMARK 465 ALA A 615
REMARK 465 ILE A 616
REMARK 465 LEU A 617
REMARK 465 VAL A 618
REMARK 465 VAL A 619
REMARK 465 ASP A 620
REMARK 465 ILE A 621
REMARK 465 MET A 622
REMARK 465 HIS A 623
REMARK 465 GLY A 624
REMARK 465 LEU A 625
REMARK 465 GLU A 626
REMARK 465 PRO A 627
REMARK 465 GLN A 628
REMARK 465 THR A 629
REMARK 465 ILE A 630
REMARK 465 GLU A 631
REMARK 465 SER A 632
REMARK 465 LEU A 633
REMARK 465 ARG A 634
REMARK 465 LEU A 635
REMARK 465 LEU A 636
REMARK 465 ARG A 637
REMARK 465 GLU A 638
REMARK 465 ARG A 639
REMARK 465 LYS A 640
REMARK 465 THR A 641
REMARK 465 PRO A 642
REMARK 465 PHE A 643
REMARK 465 VAL A 644
REMARK 465 VAL A 645
REMARK 465 ALA A 646
REMARK 465 LEU A 647
REMARK 465 ASN A 648
REMARK 465 LYS A 649
REMARK 465 ILE A 650
REMARK 465 ASP A 651
REMARK 465 ARG A 652
REMARK 465 LEU A 653
REMARK 465 TYR A 654
REMARK 465 GLY A 655
REMARK 465 TRP A 656
REMARK 465 LYS A 657
REMARK 465 LYS A 658
REMARK 465 ILE A 659
REMARK 465 GLU A 660
REMARK 465 ASN A 661
REMARK 465 ASN A 662
REMARK 465 GLY A 663
REMARK 465 PHE A 664
REMARK 465 ARG A 665
REMARK 465 GLU A 666
REMARK 465 SER A 667
REMARK 465 PHE A 668
REMARK 465 ALA A 669
REMARK 465 LEU A 670
REMARK 465 GLN A 671
REMARK 465 ASN A 672
REMARK 465 LYS A 673
REMARK 465 ALA A 674
REMARK 465 VAL A 675
REMARK 465 GLN A 676
REMARK 465 ASN A 677
REMARK 465 GLU A 678
REMARK 465 PHE A 679
REMARK 465 ARG A 680
REMARK 465 ASN A 681
REMARK 465 ARG A 682
REMARK 465 LEU A 683
REMARK 465 ASP A 684
REMARK 465 GLN A 685
REMARK 465 VAL A 686
REMARK 465 LYS A 687
REMARK 465 LEU A 688
REMARK 465 GLN A 689
REMARK 465 PHE A 690
REMARK 465 ALA A 691
REMARK 465 GLU A 692
REMARK 465 GLN A 693
REMARK 465 GLY A 694
REMARK 465 PHE A 695
REMARK 465 ASN A 696
REMARK 465 SER A 697
REMARK 465 GLU A 698
REMARK 465 LEU A 699
REMARK 465 PHE A 700
REMARK 465 TYR A 701
REMARK 465 GLU A 702
REMARK 465 ASN A 703
REMARK 465 LYS A 704
REMARK 465 ASN A 705
REMARK 465 PHE A 706
REMARK 465 ALA A 707
REMARK 465 ARG A 708
REMARK 465 TYR A 709
REMARK 465 VAL A 710
REMARK 465 SER A 711
REMARK 465 LEU A 712
REMARK 465 VAL A 713
REMARK 465 PRO A 714
REMARK 465 THR A 715
REMARK 465 SER A 716
REMARK 465 ALA A 717
REMARK 465 HIS A 718
REMARK 465 THR A 719
REMARK 465 GLY A 720
REMARK 465 GLU A 721
REMARK 465 GLY A 722
REMARK 465 ILE A 723
REMARK 465 PRO A 724
REMARK 465 ASP A 725
REMARK 465 MET A 726
REMARK 465 LEU A 727
REMARK 465 LYS A 728
REMARK 465 LEU A 729
REMARK 465 ILE A 730
REMARK 465 VAL A 731
REMARK 465 GLN A 732
REMARK 465 LEU A 733
REMARK 465 CYS A 734
REMARK 465 GLN A 735
REMARK 465 GLU A 736
REMARK 465 ARG A 737
REMARK 465 MET A 738
REMARK 465 ALA A 739
REMARK 465 SER A 740
REMARK 465 SER A 741
REMARK 465 LEU A 742
REMARK 465 MET A 743
REMARK 465 TYR A 744
REMARK 465 LEU A 745
REMARK 465 SER A 746
REMARK 465 GLU A 747
REMARK 465 LEU A 748
REMARK 465 GLN A 749
REMARK 465 ALA A 750
REMARK 465 THR A 751
REMARK 465 VAL A 752
REMARK 465 LEU A 753
REMARK 465 GLU A 754
REMARK 465 VAL A 755
REMARK 465 LYS A 756
REMARK 465 ALA A 757
REMARK 465 ILE A 758
REMARK 465 GLU A 759
REMARK 465 GLY A 760
REMARK 465 PHE A 761
REMARK 465 GLY A 762
REMARK 465 VAL A 763
REMARK 465 THR A 764
REMARK 465 ILE A 765
REMARK 465 ASP A 766
REMARK 465 VAL A 767
REMARK 465 ILE A 768
REMARK 465 LEU A 769
REMARK 465 SER A 770
REMARK 465 ASN A 771
REMARK 465 GLY A 772
REMARK 465 ILE A 773
REMARK 465 LEU A 774
REMARK 465 ARG A 775
REMARK 465 GLU A 776
REMARK 465 GLY A 777
REMARK 465 ASP A 778
REMARK 465 ARG A 779
REMARK 465 ILE A 780
REMARK 465 VAL A 781
REMARK 465 LEU A 782
REMARK 465 CYS A 783
REMARK 465 GLY A 784
REMARK 465 LEU A 785
REMARK 465 GLU A 786
REMARK 465 GLY A 787
REMARK 465 PRO A 788
REMARK 465 ILE A 789
REMARK 465 LYS A 790
REMARK 465 THR A 791
REMARK 465 ASN A 792
REMARK 465 ILE A 793
REMARK 465 ARG A 794
REMARK 465 ALA A 795
REMARK 465 LEU A 796
REMARK 465 LEU A 797
REMARK 465 THR A 798
REMARK 465 PRO A 799
REMARK 465 ALA A 800
REMARK 465 PRO A 801
REMARK 465 MET A 802
REMARK 465 ARG A 803
REMARK 465 GLU A 804
REMARK 465 LEU A 805
REMARK 465 ARG A 806
REMARK 465 ILE A 807
REMARK 465 LYS A 808
REMARK 465 GLY A 809
REMARK 465 GLN A 810
REMARK 465 TYR A 811
REMARK 465 ILE A 812
REMARK 465 HIS A 813
REMARK 465 HIS A 814
REMARK 465 LYS A 815
REMARK 465 GLU A 816
REMARK 465 VAL A 817
REMARK 465 LYS A 818
REMARK 465 ALA A 819
REMARK 465 ALA A 820
REMARK 465 GLN A 821
REMARK 465 GLY A 822
REMARK 465 VAL A 823
REMARK 465 LYS A 824
REMARK 465 ILE A 825
REMARK 465 SER A 826
REMARK 465 ALA A 827
REMARK 465 PRO A 828
REMARK 465 GLY A 829
REMARK 465 LEU A 830
REMARK 465 GLU A 831
REMARK 465 GLY A 832
REMARK 465 ALA A 833
REMARK 465 ILE A 834
REMARK 465 ALA A 835
REMARK 465 GLY A 836
REMARK 465 SER A 837
REMARK 465 ARG A 838
REMARK 465 LEU A 839
REMARK 465 LEU A 840
REMARK 465 VAL A 841
REMARK 465 VAL A 842
REMARK 465 GLY A 843
REMARK 465 PRO A 844
REMARK 465 ASP A 845
REMARK 465 ASP A 846
REMARK 465 ASP A 847
REMARK 465 GLU A 848
REMARK 465 GLU A 849
REMARK 465 GLU A 850
REMARK 465 LEU A 851
REMARK 465 GLU A 852
REMARK 465 GLU A 853
REMARK 465 GLU A 854
REMARK 465 VAL A 855
REMARK 465 GLU A 856
REMARK 465 SER A 857
REMARK 465 ASP A 858
REMARK 465 LEU A 859
REMARK 465 GLN A 860
REMARK 465 SER A 861
REMARK 465 LEU A 862
REMARK 465 PHE A 863
REMARK 465 SER A 864
REMARK 465 ARG A 865
REMARK 465 VAL A 866
REMARK 465 GLU A 867
REMARK 465 LYS A 868
REMARK 465 THR A 869
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 1039 ND1 HIS A 1042 6555 2.19
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 HIS A1042 -3.57 83.59
REMARK 500 ARG A1070 -79.82 -126.28
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 LAC A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LAC A 1203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N3N RELATED DB: PDB
DBREF 4N3G A 517 1116 UNP G0S8G9 G0S8G9_CHATD 517 1092
SEQADV 4N3G SER A 514 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G HIS A 515 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G MET A 516 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G VAL A 576 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G VAL A 577 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G ASN A 578 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G LYS A 579 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G ASP A 580 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G GLY A 581 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G LYS A 582 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G PHE A 583 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G GLU A 584 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G PHE A 585 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G LYS A 586 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G VAL A 587 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G PRO A 588 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G GLY A 589 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G LEU A 590 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G LEU A 591 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G ILE A 592 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G ILE A 593 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G ASP A 594 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G THR A 595 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G PRO A 596 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G GLY A 597 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G HIS A 598 UNP G0S8G9 EXPRESSION TAG
SEQADV 4N3G GLU A 599 UNP G0S8G9 EXPRESSION TAG
SEQRES 1 A 603 SER HIS MET ASN LYS ASP ASN LEU ARG SER PRO ILE CYS
SEQRES 2 A 603 CYS ILE LEU GLY HIS VAL ASP THR GLY LYS THR LYS LEU
SEQRES 3 A 603 LEU ASP LYS ILE ARG GLN THR ASN VAL GLN GLU GLY GLU
SEQRES 4 A 603 ALA GLY GLY ILE THR GLN GLN ILE GLY ALA THR TYR PHE
SEQRES 5 A 603 PRO VAL GLU ALA ILE LYS GLN LYS THR ALA VAL VAL ASN
SEQRES 6 A 603 LYS ASP GLY LYS PHE GLU PHE LYS VAL PRO GLY LEU LEU
SEQRES 7 A 603 ILE ILE ASP THR PRO GLY HIS GLU SER PHE SER ASN LEU
SEQRES 8 A 603 ARG SER ARG GLY SER SER LEU CYS ASN ILE ALA ILE LEU
SEQRES 9 A 603 VAL VAL ASP ILE MET HIS GLY LEU GLU PRO GLN THR ILE
SEQRES 10 A 603 GLU SER LEU ARG LEU LEU ARG GLU ARG LYS THR PRO PHE
SEQRES 11 A 603 VAL VAL ALA LEU ASN LYS ILE ASP ARG LEU TYR GLY TRP
SEQRES 12 A 603 LYS LYS ILE GLU ASN ASN GLY PHE ARG GLU SER PHE ALA
SEQRES 13 A 603 LEU GLN ASN LYS ALA VAL GLN ASN GLU PHE ARG ASN ARG
SEQRES 14 A 603 LEU ASP GLN VAL LYS LEU GLN PHE ALA GLU GLN GLY PHE
SEQRES 15 A 603 ASN SER GLU LEU PHE TYR GLU ASN LYS ASN PHE ALA ARG
SEQRES 16 A 603 TYR VAL SER LEU VAL PRO THR SER ALA HIS THR GLY GLU
SEQRES 17 A 603 GLY ILE PRO ASP MET LEU LYS LEU ILE VAL GLN LEU CYS
SEQRES 18 A 603 GLN GLU ARG MET ALA SER SER LEU MET TYR LEU SER GLU
SEQRES 19 A 603 LEU GLN ALA THR VAL LEU GLU VAL LYS ALA ILE GLU GLY
SEQRES 20 A 603 PHE GLY VAL THR ILE ASP VAL ILE LEU SER ASN GLY ILE
SEQRES 21 A 603 LEU ARG GLU GLY ASP ARG ILE VAL LEU CYS GLY LEU GLU
SEQRES 22 A 603 GLY PRO ILE LYS THR ASN ILE ARG ALA LEU LEU THR PRO
SEQRES 23 A 603 ALA PRO MET ARG GLU LEU ARG ILE LYS GLY GLN TYR ILE
SEQRES 24 A 603 HIS HIS LYS GLU VAL LYS ALA ALA GLN GLY VAL LYS ILE
SEQRES 25 A 603 SER ALA PRO GLY LEU GLU GLY ALA ILE ALA GLY SER ARG
SEQRES 26 A 603 LEU LEU VAL VAL GLY PRO ASP ASP ASP GLU GLU GLU LEU
SEQRES 27 A 603 GLU GLU GLU VAL GLU SER ASP LEU GLN SER LEU PHE SER
SEQRES 28 A 603 ARG VAL GLU LYS THR GLY LYS GLY VAL SER VAL GLN ALA
SEQRES 29 A 603 SER THR LEU GLY SER LEU GLU ALA LEU LEU ASP PHE LEU
SEQRES 30 A 603 LYS ASP CYS LYS ILE PRO VAL ALA ASN VAL GLY ILE GLY
SEQRES 31 A 603 PRO VAL TYR LYS ARG ASP VAL MET GLN CYS GLY ILE MET
SEQRES 32 A 603 LEU GLU LYS ALA PRO ASP TYR ALA VAL MET LEU CYS PHE
SEQRES 33 A 603 ASP VAL LYS VAL ASP LYS GLU ALA GLN GLN TYR ALA ASP
SEQRES 34 A 603 GLU ASN GLY ILE LYS ILE PHE THR ALA ASP ILE ILE TYR
SEQRES 35 A 603 HIS LEU PHE ASP GLN PHE THR LYS HIS MET GLN GLU GLN
SEQRES 36 A 603 LEU GLU LYS LYS LYS GLU GLU SER LYS MET LEU ALA VAL
SEQRES 37 A 603 PHE PRO CYS VAL LEU ASN PRO VAL ALA VAL PHE ASN LYS
SEQRES 38 A 603 THR ASN PRO ILE VAL VAL GLY VAL ASP VAL VAL ASP GLY
SEQRES 39 A 603 GLN LEU LYS LEU ASN THR PRO ILE ALA ALA VAL LYS MET
SEQRES 40 A 603 ASN PRO THR THR GLY GLN LYS GLU ILE ILE SER LEU GLY
SEQRES 41 A 603 ARG VAL THR GLY ILE GLU ARG ASP HIS LYS PRO LEU GLN
SEQRES 42 A 603 VAL CYS LYS LYS GLY GLN PRO ALA VAL ALA ILE LYS ILE
SEQRES 43 A 603 GLU MET GLY GLY HIS GLN PRO ALA TYR GLY ARG HIS LEU
SEQRES 44 A 603 ASP GLU LYS ASP VAL LEU TYR SER HIS ILE SER ARG ALA
SEQRES 45 A 603 SER ILE ASP VAL LEU LYS GLN PHE TYR ARG ASP VAL VAL
SEQRES 46 A 603 THR THR ASP GLU TRP GLN LEU ILE ILE LYS LEU LYS SER
SEQRES 47 A 603 VAL PHE ASP VAL GLN
HET CL A1201 1
HET LAC A1202 6
HET LAC A1203 6
HETNAM CL CHLORIDE ION
HETNAM LAC LACTIC ACID
FORMUL 2 CL CL 1-
FORMUL 3 LAC 2(C3 H6 O3)
HELIX 1 1 THR A 879 CYS A 893 1 15
HELIX 2 2 TYR A 906 ALA A 920 1 15
HELIX 3 3 ASP A 934 ASN A 944 1 11
HELIX 4 4 ILE A 953 SER A 976 1 24
HELIX 5 5 SER A 1083 TYR A 1094 1 12
HELIX 6 6 THR A 1099 PHE A 1113 1 15
SHEET 1 A 4 VAL A 897 ASN A 899 0
SHEET 2 A 4 VAL A 873 ALA A 877 1 N VAL A 873 O ALA A 898
SHEET 3 A 4 VAL A 925 PHE A 929 1 O PHE A 929 N GLN A 876
SHEET 4 A 4 LYS A 947 ALA A 951 1 O PHE A 949 N MET A 926
SHEET 1 B 7 LYS A1043 PRO A1044 0
SHEET 2 B 7 LYS A1027 ARG A1040 -1 N ARG A1040 O LYS A1043
SHEET 3 B 7 PRO A1014 MET A1020 -1 N ILE A1015 O GLY A1033
SHEET 4 B 7 LEU A1078 SER A1080 -1 O TYR A1079 N ALA A1016
SHEET 5 B 7 CYS A 984 ASN A 993 -1 N LEU A 986 O LEU A1078
SHEET 6 B 7 ILE A 998 LYS A1010 -1 O GLY A1001 N VAL A 989
SHEET 7 B 7 VAL A1047 LYS A1049 -1 O CYS A1048 N LEU A1009
SHEET 1 C 5 LYS A1043 PRO A1044 0
SHEET 2 C 5 LYS A1027 ARG A1040 -1 N ARG A1040 O LYS A1043
SHEET 3 C 5 VAL A1055 GLU A1060 -1 O LYS A1058 N THR A1036
SHEET 4 C 5 ILE A 998 LYS A1010 -1 N VAL A1002 O VAL A1055
SHEET 5 C 5 VAL A1047 LYS A1049 -1 O CYS A1048 N LEU A1009
CISPEP 1 ASN A 996 PRO A 997 0 6.81
SITE 1 AC1 2 ASP A1041 HIS A1042
SITE 1 AC2 5 TYR A 955 ARG A1084 ILE A1087 LYS A1091
SITE 2 AC2 5 LYS A1110
CRYST1 98.230 98.230 97.420 90.00 90.00 120.00 P 31 2 1 6
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 0.010180 0.005878 0.000000 0.00000
SCALE2 0.000000 0.011755 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010265 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
