HEADER CELL CYCLE 03-JUL-08 3DNY
TITLE FITTING OF THE EEF2 CRYSTAL STRUCTURE INTO THE CRYO-EM DENSITY MAP OF
TITLE 2 THE EEF2.80S.ALF4-.GDP COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR 2;
COMPND 3 CHAIN: T;
COMPND 4 SYNONYM: EF-2, TRANSLATION ELONGATION FACTOR 2, EUKARYOTIC ELONGATION
COMPND 5 FACTOR 2, EEF2, RIBOSOMAL TRANSLOCASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE
KEYWDS EEF2 TRANSITION STATE COMPLEX, 80S RIBOSOME, ALF4-, GDP, GTPASE,
KEYWDS 2 TRANSLOCATION, ELONGATION FACTOR, GTP-BINDING, NUCLEOTIDE-BINDING,
KEYWDS 3 PHOSPHOPROTEIN, PROTEIN BIOSYNTHESIS, RNA-BINDING, RRNA-BINDING,
KEYWDS 4 CELL CYCLE
EXPDTA ELECTRON MICROSCOPY
MDLTYP CA ATOMS ONLY, CHAIN T
AUTHOR J.SENGUPTA,J.FRANK
REVDAT 6 21-FEB-24 3DNY 1 REMARK
REVDAT 5 18-JUL-18 3DNY 1 REMARK
REVDAT 4 24-FEB-09 3DNY 1 VERSN
REVDAT 3 02-SEP-08 3DNY 1 JRNL
REVDAT 2 19-AUG-08 3DNY 1 REMARK
REVDAT 1 05-AUG-08 3DNY 0
JRNL AUTH J.SENGUPTA,J.NILSSON,R.GURSKY,M.KJELDGAARD,P.NISSEN,J.FRANK
JRNL TITL VISUALIZATION OF THE EEF2-80S RIBOSOME TRANSITION-STATE
JRNL TITL 2 COMPLEX BY CRYO-ELECTRON MICROSCOPY.
JRNL REF J.MOL.BIOL. V. 382 179 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18644383
JRNL DOI 10.1016/J.JMB.2008.07.004
REMARK 2
REMARK 2 RESOLUTION. 12.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : O, SPIDER
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 1N0U
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : METHOD--EACH DOMAIN FITTED AS RIGID BODY,
REMARK 3 DOMAINS I (G AND G), II,IV, AND V WERE FITTED. DOMAIN III, AND
REMARK 3 DOMAIN IV INSERTIONS WERE NOT INCLUDED IN THIS FITTING MODEL.
REMARK 3 THE COORDINATES FOR THIS ENTRY ARE BASED ON MANUAL FITTING OF
REMARK 3 THE COORDINATES OF THE CRYSTAL STRUCTURE 1N0U INTO CRYO-EM
REMARK 3 DENSITY MAP. THEREFORE, AUTHORS DID NOT DEPOSIT NEW STRUCTURE
REMARK 3 FACTORS.
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 2.820
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 12.60
REMARK 3 NUMBER OF PARTICLES : NULL
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: SUPERVISED CLASSIFICATION WAS USED (REF. VALLE, M.
REMARK 3 ET AL, 2002, EMBO J.)
REMARK 4
REMARK 4 3DNY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048272.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : EEF2-BOUND 80S COMPLEX IN
REMARK 245 PRESENCE OF ALF4-, AND GDP
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : 20 MM HEPES-NH3, 100 MM KCL, 20
REMARK 245 MM MGCL2
REMARK 245 PH : 7.20
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 93.00
REMARK 245 MICROSCOPE MODEL : FEI TECNAI F20
REMARK 245 DETECTOR TYPE : KODAK SO-163 FILM
REMARK 245 MINIMUM DEFOCUS (NM) : 4500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 1000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 50000
REMARK 245 CALIBRATED MAGNIFICATION : 49650
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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 APPLY THE FOLLOWING TO CHAINS: T
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 MET T 1
REMARK 465 VAL T 2
REMARK 465 ALA T 49
REMARK 465 LYS T 50
REMARK 465 ALA T 51
REMARK 465 GLY T 52
REMARK 465 GLU T 53
REMARK 465 ALA T 54
REMARK 465 ARG T 55
REMARK 465 PHE T 56
REMARK 465 THR T 57
REMARK 465 ASP T 58
REMARK 465 THR T 59
REMARK 465 ARG T 60
REMARK 465 LYS T 61
REMARK 465 ASP T 62
REMARK 465 GLU T 63
REMARK 465 GLN T 64
REMARK 465 GLU T 65
REMARK 465 ARG T 66
REMARK 465 MET T 481
REMARK 465 LYS T 482
REMARK 465 PHE T 483
REMARK 465 SER T 484
REMARK 465 VAL T 485
REMARK 465 SER T 486
REMARK 465 PRO T 487
REMARK 465 VAL T 488
REMARK 465 VAL T 489
REMARK 465 GLN T 490
REMARK 465 VAL T 491
REMARK 465 ALA T 492
REMARK 465 VAL T 493
REMARK 465 GLU T 494
REMARK 465 VAL T 495
REMARK 465 LYS T 496
REMARK 465 ASN T 497
REMARK 465 ALA T 498
REMARK 465 ASN T 499
REMARK 465 ASP T 500
REMARK 465 LEU T 501
REMARK 465 PRO T 502
REMARK 465 LYS T 503
REMARK 465 LEU T 504
REMARK 465 VAL T 505
REMARK 465 GLU T 506
REMARK 465 GLY T 507
REMARK 465 LEU T 508
REMARK 465 LYS T 509
REMARK 465 ARG T 510
REMARK 465 LEU T 511
REMARK 465 SER T 512
REMARK 465 LYS T 513
REMARK 465 SER T 514
REMARK 465 ASP T 515
REMARK 465 PRO T 516
REMARK 465 CYS T 517
REMARK 465 VAL T 518
REMARK 465 LEU T 519
REMARK 465 THR T 520
REMARK 465 TYR T 521
REMARK 465 MET T 522
REMARK 465 SER T 523
REMARK 465 GLU T 524
REMARK 465 SER T 525
REMARK 465 GLY T 526
REMARK 465 GLU T 527
REMARK 465 HIS T 528
REMARK 465 ILE T 529
REMARK 465 VAL T 530
REMARK 465 ALA T 531
REMARK 465 GLY T 532
REMARK 465 THR T 533
REMARK 465 GLY T 534
REMARK 465 GLU T 535
REMARK 465 LEU T 536
REMARK 465 HIS T 537
REMARK 465 LEU T 538
REMARK 465 GLU T 539
REMARK 465 ILE T 540
REMARK 465 CYS T 541
REMARK 465 LEU T 542
REMARK 465 GLN T 543
REMARK 465 ASP T 544
REMARK 465 LEU T 545
REMARK 465 GLU T 546
REMARK 465 HIS T 547
REMARK 465 ASP T 548
REMARK 465 HIS T 549
REMARK 465 ALA T 550
REMARK 465 GLY T 551
REMARK 465 VAL T 552
REMARK 465 PRO T 553
REMARK 465 LEU T 554
REMARK 465 LYS T 555
REMARK 465 ILE T 556
REMARK 465 SER T 557
REMARK 465 PRO T 558
REMARK 465 PRO T 559
REMARK 465 GLU T 596
REMARK 465 VAL T 597
REMARK 465 SER T 598
REMARK 465 LEU T 599
REMARK 465 ALA T 600
REMARK 465 ILE T 601
REMARK 465 GLU T 602
REMARK 465 ASN T 603
REMARK 465 GLY T 604
REMARK 465 ILE T 605
REMARK 465 ILE T 606
REMARK 465 ASN T 607
REMARK 465 PRO T 608
REMARK 465 ARG T 609
REMARK 465 ASP T 610
REMARK 465 ASP T 611
REMARK 465 PHE T 612
REMARK 465 LYS T 613
REMARK 465 ALA T 614
REMARK 465 ARG T 615
REMARK 465 ALA T 616
REMARK 465 ARG T 617
REMARK 465 ILE T 618
REMARK 465 MET T 619
REMARK 465 ALA T 620
REMARK 465 ASP T 621
REMARK 465 ASP T 622
REMARK 465 TYR T 623
REMARK 465 GLY T 624
REMARK 465 TRP T 625
REMARK 465 ASP T 626
REMARK 465 VAL T 627
REMARK 465 THR T 628
REMARK 465 ASP T 629
REMARK 465 ALA T 630
REMARK 465 ARG T 631
REMARK 465 LYS T 632
REMARK 465 ILE T 633
REMARK 465 TRP T 634
REMARK 465 CYS T 635
REMARK 465 PHE T 636
REMARK 465 GLY T 637
REMARK 465 PRO T 638
REMARK 465 ASP T 639
REMARK 465 ARG T 760
REMARK 465 PRO T 761
REMARK 465 GLY T 762
REMARK 465 TRP T 801
REMARK 465 SER T 802
REMARK 465 THR T 803
REMARK 465 LEU T 804
REMARK 465 GLY T 805
REMARK 465 SER T 806
REMARK 465 ASP T 807
REMARK 465 PRO T 808
REMARK 465 LEU T 809
REMARK 465 ASP T 810
REMARK 465 PRO T 811
REMARK 465 THR T 812
REMARK 465 SER T 813
REMARK 465 LYS T 814
REMARK 465 ALA T 815
REMARK 465 GLY T 816
REMARK 465 GLU T 817
REMARK 465 ILE T 818
REMARK 465 VAL T 819
REMARK 465 LEU T 820
REMARK 465 ALA T 821
REMARK 465 ALA T 822
REMARK 465 ARG T 823
REMARK 465 LYS T 824
REMARK 465 ARG T 825
REMARK 465 HIS T 826
REMARK 465 GLY T 827
REMARK 465 MET T 828
REMARK 465 LYS T 829
REMARK 465 GLU T 830
REMARK 465 GLU T 831
REMARK 465 VAL T 832
REMARK 465 PRO T 833
REMARK 465 GLY T 834
REMARK 465 TRP T 835
REMARK 465 GLN T 836
REMARK 465 GLU T 837
REMARK 465 TYR T 838
REMARK 465 TYR T 839
REMARK 465 ASP T 840
REMARK 465 LYS T 841
REMARK 465 LEU T 842
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1N0U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST ELONGATION FACTOR 2 IN COMPLEX WITH
REMARK 900 SORDARIN
REMARK 900 RELATED ID: EMD-5015 RELATED DB: EMDB
REMARK 900 CRYO-EM MAP FOR EEF2.80S.ALF4-.GDP COMPLEX
REMARK 900 RELATED ID: EMD-5017 RELATED DB: EMDB
REMARK 900 ISOLATED DENSITY OF THE EEF2, SEGMENTED OUT FROM CRYO-EM MAP FOR
REMARK 900 EEF2.80S.ALF4-.GDP COMPLEX (FROM EMD-5015)
DBREF 3DNY T 1 842 UNP P32324 EF2_YEAST 1 842
SEQRES 1 T 842 MET VAL ALA PHE THR VAL ASP GLN MET ARG SER LEU MET
SEQRES 2 T 842 ASP LYS VAL THR ASN VAL ARG ASN MET SER VAL ILE ALA
SEQRES 3 T 842 HIS VAL ASP HIS GLY LYS SER THR LEU THR ASP SER LEU
SEQRES 4 T 842 VAL GLN ARG ALA GLY ILE ILE SER ALA ALA LYS ALA GLY
SEQRES 5 T 842 GLU ALA ARG PHE THR ASP THR ARG LYS ASP GLU GLN GLU
SEQRES 6 T 842 ARG GLY ILE THR ILE LYS SER THR ALA ILE SER LEU TYR
SEQRES 7 T 842 SER GLU MET SER ASP GLU ASP VAL LYS GLU ILE LYS GLN
SEQRES 8 T 842 LYS THR ASP GLY ASN SER PHE LEU ILE ASN LEU ILE ASP
SEQRES 9 T 842 SER PRO GLY HIS VAL ASP PHE SER SER GLU VAL THR ALA
SEQRES 10 T 842 ALA LEU ARG VAL THR ASP GLY ALA LEU VAL VAL VAL ASP
SEQRES 11 T 842 THR ILE GLU GLY VAL CYS VAL GLN THR GLU THR VAL LEU
SEQRES 12 T 842 ARG GLN ALA LEU GLY GLU ARG ILE LYS PRO VAL VAL VAL
SEQRES 13 T 842 ILE ASN LYS VAL ASP ARG ALA LEU LEU GLU LEU GLN VAL
SEQRES 14 T 842 SER LYS GLU ASP LEU TYR GLN THR PHE ALA ARG THR VAL
SEQRES 15 T 842 GLU SER VAL ASN VAL ILE VAL SER THR TYR ALA ASP GLU
SEQRES 16 T 842 VAL LEU GLY ASP VAL GLN VAL TYR PRO ALA ARG GLY THR
SEQRES 17 T 842 VAL ALA PHE GLY SER GLY LEU HIS GLY TRP ALA PHE THR
SEQRES 18 T 842 ILE ARG GLN PHE ALA THR ARG TYR ALA LYS LYS PHE GLY
SEQRES 19 T 842 VAL ASP LYS ALA LYS MET MET ASP ARG LEU TRP GLY ASP
SEQRES 20 T 842 SER PHE PHE ASN PRO LYS THR LYS LYS TRP THR ASN LYS
SEQRES 21 T 842 ASP THR ASP ALA GLU GLY LYS PRO LEU GLU ARG ALA PHE
SEQRES 22 T 842 ASN MET PHE ILE LEU ASP PRO ILE PHE ARG LEU PHE THR
SEQRES 23 T 842 ALA ILE MET ASN PHE LYS LYS ASP GLU ILE PRO VAL LEU
SEQRES 24 T 842 LEU GLU LYS LEU GLU ILE VAL LEU LYS GLY ASP GLU LYS
SEQRES 25 T 842 ASP LEU GLU GLY LYS ALA LEU LEU LYS VAL VAL MET ARG
SEQRES 26 T 842 LYS PHE LEU PRO ALA ALA ASP ALA LEU LEU GLU MET ILE
SEQRES 27 T 842 VAL LEU HIS LEU PRO SER PRO VAL THR ALA GLN ALA TYR
SEQRES 28 T 842 ARG ALA GLU GLN LEU TYR GLU GLY PRO ALA ASP ASP ALA
SEQRES 29 T 842 ASN CYS ILE ALA ILE LYS ASN CYS ASP PRO LYS ALA ASP
SEQRES 30 T 842 LEU MET LEU TYR VAL SER LYS MET VAL PRO THR SER ASP
SEQRES 31 T 842 LYS GLY ARG PHE TYR ALA PHE GLY ARG VAL PHE ALA GLY
SEQRES 32 T 842 THR VAL LYS SER GLY GLN LYS VAL ARG ILE GLN GLY PRO
SEQRES 33 T 842 ASN TYR VAL PRO GLY LYS LYS ASP ASP LEU PHE ILE LYS
SEQRES 34 T 842 ALA ILE GLN ARG VAL VAL LEU MET MET GLY ARG PHE VAL
SEQRES 35 T 842 GLU PRO ILE ASP ASP CYS PRO ALA GLY ASN ILE ILE GLY
SEQRES 36 T 842 LEU VAL GLY ILE ASP GLN PHE LEU LEU LYS THR GLY THR
SEQRES 37 T 842 LEU THR THR SER GLU THR ALA HIS ASN MET LYS VAL MET
SEQRES 38 T 842 LYS PHE SER VAL SER PRO VAL VAL GLN VAL ALA VAL GLU
SEQRES 39 T 842 VAL LYS ASN ALA ASN ASP LEU PRO LYS LEU VAL GLU GLY
SEQRES 40 T 842 LEU LYS ARG LEU SER LYS SER ASP PRO CYS VAL LEU THR
SEQRES 41 T 842 TYR MET SER GLU SER GLY GLU HIS ILE VAL ALA GLY THR
SEQRES 42 T 842 GLY GLU LEU HIS LEU GLU ILE CYS LEU GLN ASP LEU GLU
SEQRES 43 T 842 HIS ASP HIS ALA GLY VAL PRO LEU LYS ILE SER PRO PRO
SEQRES 44 T 842 VAL VAL ALA TYR ARG GLU THR VAL GLU SER GLU SER SER
SEQRES 45 T 842 GLN THR ALA LEU SER LYS SER PRO ASN LYS HIS ASN ARG
SEQRES 46 T 842 ILE TYR LEU LYS ALA GLU PRO ILE ASP GLU GLU VAL SER
SEQRES 47 T 842 LEU ALA ILE GLU ASN GLY ILE ILE ASN PRO ARG ASP ASP
SEQRES 48 T 842 PHE LYS ALA ARG ALA ARG ILE MET ALA ASP ASP TYR GLY
SEQRES 49 T 842 TRP ASP VAL THR ASP ALA ARG LYS ILE TRP CYS PHE GLY
SEQRES 50 T 842 PRO ASP GLY ASN GLY PRO ASN LEU VAL ILE ASP GLN THR
SEQRES 51 T 842 LYS ALA VAL GLN TYR LEU HIS GLU ILE LYS ASP SER VAL
SEQRES 52 T 842 VAL ALA ALA PHE GLN TRP ALA THR LYS GLU GLY PRO ILE
SEQRES 53 T 842 PHE GLY GLU GLU MET ARG SER VAL ARG VAL ASN ILE LEU
SEQRES 54 T 842 ASP VAL THR LEU HIS ALA ASP ALA ILE HIS ARG GLY GLY
SEQRES 55 T 842 GLY GLN ILE ILE PRO THR MET ARG ARG ALA THR TYR ALA
SEQRES 56 T 842 GLY PHE LEU LEU ALA ASP PRO LYS ILE GLN GLU PRO VAL
SEQRES 57 T 842 PHE LEU VAL GLU ILE GLN CYS PRO GLU GLN ALA VAL GLY
SEQRES 58 T 842 GLY ILE TYR SER VAL LEU ASN LYS LYS ARG GLY GLN VAL
SEQRES 59 T 842 VAL SER GLU GLU GLN ARG PRO GLY THR PRO LEU PHE THR
SEQRES 60 T 842 VAL LYS ALA TYR LEU PRO VAL ASN GLU SER PHE GLY PHE
SEQRES 61 T 842 THR GLY GLU LEU ARG GLN ALA THR GLY GLY GLN ALA PHE
SEQRES 62 T 842 PRO GLN MET VAL PHE ASP HIS TRP SER THR LEU GLY SER
SEQRES 63 T 842 ASP PRO LEU ASP PRO THR SER LYS ALA GLY GLU ILE VAL
SEQRES 64 T 842 LEU ALA ALA ARG LYS ARG HIS GLY MET LYS GLU GLU VAL
SEQRES 65 T 842 PRO GLY TRP GLN GLU TYR TYR ASP LYS LEU
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
