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HEADER HYDROLASE 19-DEC-13 4O5P
TITLE CRYSTAL STRUCTURE OF AN UNCHARACTERIZED PROTEIN FROM PSEUDOMONAS
TITLE 2 AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHOLIPASE EFFECTOR;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: PA3290;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS PHOSPHOLIPASE EFFECTOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.D.HU,Z.Q.GAO,H.ZHANG,Y.H.DONG
REVDAT 1 13-AUG-14 4O5P 0
JRNL AUTH H.D.HU,H.ZHANG,Z.Q.GAO,D.WANG,G.LIU,J.XU,K.LAN,Y.H.DONG
JRNL TITL STRUCTURE OF THE TYPE VI SECRETION PHOSPHOLIPASE EFFECTOR
JRNL TITL 2 TLE1 PROVIDES INSIGHT INTO ITS HYDROLYSIS AND MEMBRANE
JRNL TITL 3 TARGETING.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 2175 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 25084336
JRNL DOI 10.1107/S1399004714012899
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 105980
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 5266
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 28.3010 - 6.1968 0.97 7292 366 0.2059 0.2046
REMARK 3 2 6.1968 - 4.9270 0.99 7532 399 0.1917 0.2300
REMARK 3 3 4.9270 - 4.3067 0.99 7414 407 0.1692 0.1951
REMARK 3 4 4.3067 - 3.9140 0.94 7113 359 0.1779 0.2118
REMARK 3 5 3.9140 - 3.6341 0.92 6973 352 0.1977 0.2383
REMARK 3 6 3.6341 - 3.4202 0.89 6684 358 0.1988 0.2287
REMARK 3 7 3.4202 - 3.2492 0.89 6655 395 0.2050 0.2565
REMARK 3 8 3.2492 - 3.1079 0.87 6664 305 0.2203 0.2499
REMARK 3 9 3.1079 - 2.9884 0.86 6343 414 0.2224 0.2805
REMARK 3 10 2.9884 - 2.8854 0.87 6567 394 0.2316 0.2530
REMARK 3 11 2.8854 - 2.7953 0.87 6544 316 0.2163 0.3152
REMARK 3 12 2.7953 - 2.7154 0.86 6530 350 0.2324 0.2884
REMARK 3 13 2.7154 - 2.6440 0.88 6688 319 0.2219 0.2778
REMARK 3 14 2.6440 - 2.5795 0.89 6644 340 0.2290 0.2622
REMARK 3 15 2.5795 - 2.5209 0.89 6714 387 0.2276 0.2962
REMARK 3 16 2.5209 - 2.4673 0.90 6769 321 0.2195 0.2828
REMARK 3 17 2.4673 - 2.4180 0.89 6737 353 0.2261 0.3029
REMARK 3 18 2.4180 - 2.3724 0.90 6723 350 0.2346 0.2729
REMARK 3 19 2.3724 - 2.3300 0.88 6752 352 0.2406 0.3312
REMARK 3 20 2.3300 - 2.2905 0.81 6043 361 0.3945 0.4546
REMARK 3 21 2.2905 - 2.2536 0.85 6439 339 0.3553 0.4000
REMARK 3 22 2.2536 - 2.2190 0.90 6739 356 0.4181 0.4581
REMARK 3 23 2.2190 - 2.1863 0.81 6155 279 0.4579 0.5674
REMARK 3 24 2.1863 - 2.1555 0.88 6720 322 0.3354 0.3624
REMARK 3 25 2.1555 - 2.1264 0.92 6767 342 0.2407 0.3283
REMARK 3 26 2.1264 - 2.0988 0.89 6922 310 0.2410 0.3139
REMARK 3 27 2.0988 - 2.0726 0.90 6789 316 0.2245 0.2914
REMARK 3 28 2.0726 - 2.0476 0.91 6744 369 0.2262 0.2907
REMARK 3 29 2.0476 - 2.0238 0.89 6721 378 0.2298 0.2909
REMARK 3 30 2.0238 - 2.0011 0.81 6051 323 0.2354 0.2950
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.008 11761
REMARK 3 ANGLE : 1.199 15910
REMARK 3 CHIRALITY : 0.078 1714
REMARK 3 PLANARITY : 0.005 2110
REMARK 3 DIHEDRAL : 15.115 4337
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 4O5P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JAN-14.
REMARK 100 THE RCSB ID CODE IS RCSB084074.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BSRF
REMARK 200 BEAMLINE : 3W1A
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 : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109609
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.21200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04M CITRIC ACID, 0.1M BIS-TRIS
REMARK 280 PROPANE, 17% PEG 3350 , PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MSE A 1
REMARK 465 PRO A 2
REMARK 465 GLU A 44
REMARK 465 GLN A 45
REMARK 465 LYS A 46
REMARK 465 ARG A 47
REMARK 465 LEU A 48
REMARK 465 SER A 49
REMARK 465 GLU A 50
REMARK 465 GLY A 51
REMARK 465 ASP A 52
REMARK 465 VAL A 53
REMARK 465 VAL A 54
REMARK 465 GLY A 55
REMARK 465 GLY A 56
REMARK 465 ALA A 57
REMARK 465 PRO A 58
REMARK 465 ALA A 287
REMARK 465 ASP A 288
REMARK 465 SER A 289
REMARK 465 ALA A 290
REMARK 465 SER A 312
REMARK 465 GLN A 313
REMARK 465 CYS A 314
REMARK 465 LEU A 315
REMARK 465 PRO A 316
REMARK 465 THR A 317
REMARK 465 ILE A 318
REMARK 465 LEU A 319
REMARK 465 ASP A 353
REMARK 465 ALA A 354
REMARK 465 ALA A 423
REMARK 465 PRO A 424
REMARK 465 ALA A 425
REMARK 465 VAL A 426
REMARK 465 HIS A 427
REMARK 465 PRO A 428
REMARK 465 ASP A 429
REMARK 465 PHE A 430
REMARK 465 HIS A 431
REMARK 465 GLU A 432
REMARK 465 GLY A 528
REMARK 465 GLU A 529
REMARK 465 PRO A 530
REMARK 465 TRP A 663
REMARK 465 PHE A 664
REMARK 465 MSE A 665
REMARK 465 ASN A 666
REMARK 465 THR A 667
REMARK 465 SER A 668
REMARK 465 ALA A 669
REMARK 465 ILE A 670
REMARK 465 GLY A 671
REMARK 465 PRO A 672
REMARK 465 ARG A 673
REMARK 465 GLU A 674
REMARK 465 LEU A 729
REMARK 465 PHE A 730
REMARK 465 LEU A 731
REMARK 465 PRO A 732
REMARK 465 SER A 733
REMARK 465 LEU A 734
REMARK 465 ALA A 735
REMARK 465 ARG A 736
REMARK 465 PRO A 737
REMARK 465 LEU A 738
REMARK 465 LEU A 739
REMARK 465 SER A 740
REMARK 465 GLY A 741
REMARK 465 LYS A 742
REMARK 465 VAL A 743
REMARK 465 GLU A 814
REMARK 465 ALA A 815
REMARK 465 LEU A 816
REMARK 465 LYS A 817
REMARK 465 ALA A 818
REMARK 465 ARG A 819
REMARK 465 ASP A 820
REMARK 465 LEU A 821
REMARK 465 GLY A 822
REMARK 465 SER A 823
REMARK 465 LEU A 824
REMARK 465 ALA A 825
REMARK 465 GLY A 826
REMARK 465 LEU A 827
REMARK 465 VAL A 828
REMARK 465 ALA A 829
REMARK 465 LYS A 830
REMARK 465 ALA A 831
REMARK 465 GLU A 832
REMARK 465 LEU A 833
REMARK 465 THR A 834
REMARK 465 GLN A 835
REMARK 465 ALA A 836
REMARK 465 PRO A 837
REMARK 465 ALA A 838
REMARK 465 ALA A 839
REMARK 465 ALA A 840
REMARK 465 THR A 841
REMARK 465 PRO A 842
REMARK 465 ALA A 843
REMARK 465 TRP A 844
REMARK 465 LEU A 845
REMARK 465 ALA A 846
REMARK 465 GLU A 847
REMARK 465 ALA A 848
REMARK 465 LYS A 849
REMARK 465 GLN A 850
REMARK 465 ALA A 851
REMARK 465 LEU A 852
REMARK 465 GLN A 853
REMARK 465 ASP A 854
REMARK 465 MSE A 855
REMARK 465 GLY A 856
REMARK 465 THR A 857
REMARK 465 GLU A 858
REMARK 465 GLN A 859
REMARK 465 ALA A 860
REMARK 465 GLN A 861
REMARK 465 PRO A 862
REMARK 465 PRO A 863
REMARK 465 GLY A 864
REMARK 465 PRO A 865
REMARK 465 GLY A 866
REMARK 465 SER A 867
REMARK 465 ALA A 868
REMARK 465 PRO A 869
REMARK 465 GLY A 870
REMARK 465 TRP A 871
REMARK 465 LEU A 872
REMARK 465 LYS A 873
REMARK 465 ARG A 874
REMARK 465 GLY A 875
REMARK 465 LYS A 876
REMARK 465 ASP A 877
REMARK 465 LEU A 878
REMARK 465 MSE A 879
REMARK 465 GLU A 880
REMARK 465 SER A 881
REMARK 465 LEU A 882
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MSE B 1
REMARK 465 PRO B 2
REMARK 465 GLN B 43
REMARK 465 GLU B 44
REMARK 465 GLN B 45
REMARK 465 LYS B 46
REMARK 465 ARG B 47
REMARK 465 LEU B 48
REMARK 465 SER B 49
REMARK 465 GLU B 50
REMARK 465 GLY B 51
REMARK 465 ASP B 52
REMARK 465 VAL B 53
REMARK 465 VAL B 54
REMARK 465 GLY B 55
REMARK 465 GLY B 56
REMARK 465 ALA B 57
REMARK 465 PRO B 58
REMARK 465 CYS B 59
REMARK 465 ALA B 287
REMARK 465 ASP B 288
REMARK 465 SER B 289
REMARK 465 ALA B 290
REMARK 465 PRO B 316
REMARK 465 THR B 317
REMARK 465 ILE B 318
REMARK 465 LEU B 319
REMARK 465 PRO B 320
REMARK 465 ASP B 353
REMARK 465 ALA B 354
REMARK 465 ASN B 355
REMARK 465 GLY B 356
REMARK 465 ALA B 423
REMARK 465 PRO B 424
REMARK 465 ALA B 425
REMARK 465 VAL B 426
REMARK 465 HIS B 427
REMARK 465 PRO B 428
REMARK 465 ASP B 429
REMARK 465 PHE B 430
REMARK 465 HIS B 431
REMARK 465 GLU B 432
REMARK 465 GLU B 433
REMARK 465 GLY B 528
REMARK 465 GLU B 529
REMARK 465 PRO B 530
REMARK 465 LEU B 531
REMARK 465 PHE B 664
REMARK 465 MSE B 665
REMARK 465 ASN B 666
REMARK 465 THR B 667
REMARK 465 SER B 668
REMARK 465 ALA B 669
REMARK 465 ILE B 670
REMARK 465 GLY B 671
REMARK 465 PRO B 672
REMARK 465 ARG B 673
REMARK 465 LEU B 729
REMARK 465 PHE B 730
REMARK 465 LEU B 731
REMARK 465 PRO B 732
REMARK 465 SER B 733
REMARK 465 LEU B 734
REMARK 465 ALA B 735
REMARK 465 ARG B 736
REMARK 465 PRO B 737
REMARK 465 LEU B 738
REMARK 465 LEU B 739
REMARK 465 SER B 740
REMARK 465 GLY B 741
REMARK 465 LYS B 742
REMARK 465 VAL B 813
REMARK 465 GLU B 814
REMARK 465 ALA B 815
REMARK 465 LEU B 816
REMARK 465 LYS B 817
REMARK 465 ALA B 818
REMARK 465 ARG B 819
REMARK 465 ASP B 820
REMARK 465 LEU B 821
REMARK 465 GLY B 822
REMARK 465 SER B 823
REMARK 465 LEU B 824
REMARK 465 ALA B 825
REMARK 465 GLY B 826
REMARK 465 LEU B 827
REMARK 465 VAL B 828
REMARK 465 ALA B 829
REMARK 465 LYS B 830
REMARK 465 ALA B 831
REMARK 465 GLU B 832
REMARK 465 LEU B 833
REMARK 465 THR B 834
REMARK 465 GLN B 835
REMARK 465 ALA B 836
REMARK 465 PRO B 837
REMARK 465 ALA B 838
REMARK 465 ALA B 839
REMARK 465 ALA B 840
REMARK 465 THR B 841
REMARK 465 PRO B 842
REMARK 465 ALA B 843
REMARK 465 TRP B 844
REMARK 465 LEU B 845
REMARK 465 ALA B 846
REMARK 465 GLU B 847
REMARK 465 ALA B 848
REMARK 465 LYS B 849
REMARK 465 GLN B 850
REMARK 465 ALA B 851
REMARK 465 LEU B 852
REMARK 465 GLN B 853
REMARK 465 ASP B 854
REMARK 465 MSE B 855
REMARK 465 GLY B 856
REMARK 465 THR B 857
REMARK 465 GLU B 858
REMARK 465 GLN B 859
REMARK 465 ALA B 860
REMARK 465 GLN B 861
REMARK 465 PRO B 862
REMARK 465 PRO B 863
REMARK 465 GLY B 864
REMARK 465 PRO B 865
REMARK 465 GLY B 866
REMARK 465 SER B 867
REMARK 465 ALA B 868
REMARK 465 PRO B 869
REMARK 465 GLY B 870
REMARK 465 TRP B 871
REMARK 465 LEU B 872
REMARK 465 LYS B 873
REMARK 465 ARG B 874
REMARK 465 GLY B 875
REMARK 465 LYS B 876
REMARK 465 ASP B 877
REMARK 465 LEU B 878
REMARK 465 MSE B 879
REMARK 465 GLU B 880
REMARK 465 SER B 881
REMARK 465 LEU B 882
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 VAL A 14 CG1 CG2
REMARK 470 ARG A 260 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 491 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 559 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 41 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 163 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 491 CG CD NE CZ NH1 NH2
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 O HOH B 1168 O HOH B 1294 2.10
REMARK 500 NH2 ARG A 721 O GLY A 744 2.16
REMARK 500 O HOH A 1256 O HOH A 1367 2.18
REMARK 500 NH2 ARG B 197 O HOH B 1111 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH B 1264 O HOH B 1387 1455 2.17
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 SER A 84 71.27 -109.83
REMARK 500 SER A 86 42.42 -140.68
REMARK 500 SER A 235 -127.85 66.87
REMARK 500 VAL A 254 -68.94 -102.45
REMARK 500 ALA A 257 113.31 53.08
REMARK 500 ASP A 258 -11.70 68.64
REMARK 500 ASP A 302 14.61 56.91
REMARK 500 ASP A 322 12.54 -144.50
REMARK 500 ARG A 328 126.64 -170.98
REMARK 500 GLN A 338 -2.90 -141.92
REMARK 500 ASP A 640 15.04 56.60
REMARK 500 ASP A 688 -114.24 58.45
REMARK 500 SER B 86 45.10 -143.95
REMARK 500 ASN B 131 -71.21 -58.31
REMARK 500 MSE B 132 86.19 -160.92
REMARK 500 SER B 235 -129.32 68.24
REMARK 500 SER B 255 108.30 153.70
REMARK 500 ASP B 256 116.78 67.89
REMARK 500 ASP B 258 7.81 58.22
REMARK 500 ASP B 302 17.04 59.37
REMARK 500 SER B 312 -162.90 -163.01
REMARK 500 ASP B 322 14.06 -140.24
REMARK 500 PRO B 533 154.60 -45.66
REMARK 500 ASP B 640 24.44 45.92
REMARK 500 ASP B 688 -113.15 58.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1114 DISTANCE = 5.60 ANGSTROMS
REMARK 525 HOH A1237 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH A1264 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH A1265 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A1278 DISTANCE = 5.44 ANGSTROMS
REMARK 525 HOH A1288 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A1290 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH A1298 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH A1357 DISTANCE = 9.37 ANGSTROMS
REMARK 525 HOH A1405 DISTANCE = 8.36 ANGSTROMS
REMARK 525 HOH B 974 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH B1018 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH B1104 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH B1157 DISTANCE = 7.75 ANGSTROMS
REMARK 525 HOH B1161 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH B1178 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH B1222 DISTANCE = 5.70 ANGSTROMS
REMARK 525 HOH B1248 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B1255 DISTANCE = 8.50 ANGSTROMS
REMARK 525 HOH B1256 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH B1260 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH B1261 DISTANCE = 8.82 ANGSTROMS
REMARK 525 HOH B1266 DISTANCE = 7.09 ANGSTROMS
REMARK 525 HOH B1269 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH B1303 DISTANCE = 8.41 ANGSTROMS
REMARK 525 HOH B1317 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH B1344 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH B1383 DISTANCE = 5.76 ANGSTROMS
DBREF 4O5P A 1 882 UNP Q9HYV3 Q9HYV3_PSEAE 1 882
DBREF 4O5P B 1 882 UNP Q9HYV3 Q9HYV3_PSEAE 1 882
SEQADV 4O5P GLY A -1 UNP Q9HYV3 EXPRESSION TAG
SEQADV 4O5P SER A 0 UNP Q9HYV3 EXPRESSION TAG
SEQADV 4O5P GLY B -1 UNP Q9HYV3 EXPRESSION TAG
SEQADV 4O5P SER B 0 UNP Q9HYV3 EXPRESSION TAG
SEQRES 1 A 884 GLY SER MSE PRO ASN PHE GLY PHE HIS ILE ALA PRO THR
SEQRES 2 A 884 HIS PRO VAL ALA GLY ARG LEU THR TYR ASP SER LYS LYS
SEQRES 3 A 884 LEU SER GLU ASN ILE LEU LYS GLN GLN SER ASP GLU ARG
SEQRES 4 A 884 VAL PHE SER ARG ALA GLN GLU GLN LYS ARG LEU SER GLU
SEQRES 5 A 884 GLY ASP VAL VAL GLY GLY ALA PRO CYS CYS LYS ALA ILE
SEQRES 6 A 884 HIS ILE THR LEU GLY PHE ASP GLY THR ASN ASN ASN ASP
SEQRES 7 A 884 LYS ALA ASP GLY SER SER VAL SER PRO SER CYS SER ASN
SEQRES 8 A 884 VAL ALA ARG LEU ILE HIS ALA SER ILE GLY SER GLY ASP
SEQRES 9 A 884 ASP ILE ASN SER ARG GLY ILE PHE LYS TYR TYR CYS PRO
SEQRES 10 A 884 GLY VAL GLY THR VAL PHE PRO ASP ILE LYS GLU PHE THR
SEQRES 11 A 884 PRO SER ASN MSE GLY LEU ILE GLY ALA GLU GLY GLY GLU
SEQRES 12 A 884 ASN ARG ILE ASN TRP GLY LEU VAL GLN LEU VAL ASP ALA
SEQRES 13 A 884 LEU PHE TYR THR LEU LEU LYS SER ARG LEU LYS LEU ASN
SEQRES 14 A 884 ASP VAL GLN GLY LEU VAL GLU GLU MSE SER THR ASN TRP
SEQRES 15 A 884 THR VAL SER THR LEU THR GLY GLY LEU LEU GLU ASN GLY
SEQRES 16 A 884 GLU LYS LYS ARG ARG ALA ALA LEU GLU PRO LYS LEU LYS
SEQRES 17 A 884 GLU LEU GLU GLU LYS LEU ARG GLN ARG GLN ASN SER GLY
SEQRES 18 A 884 GLN LYS PRO HIS ILE LEU ALA MSE ARG LEU TYR ILE TYR
SEQRES 19 A 884 GLY PHE SER ARG GLY ALA ALA GLU ALA ARG ALA PHE ALA
SEQRES 20 A 884 ASN TRP LEU GLN GLU LEU THR ARG VAL SER ASP ALA ASP
SEQRES 21 A 884 GLY ARG VAL GLU TYR ARG PHE ALA GLY LEU PRO ILE SER
SEQRES 22 A 884 ILE GLU PHE LEU GLY LEU PHE ASP THR VAL ALA ALA VAL
SEQRES 23 A 884 GLY LEU ALA ASP SER ALA PRO PHE ALA ALA GLY HIS MSE
SEQRES 24 A 884 ASP TRP ALA ASP ASP THR MSE ARG LEU PRO ASP GLU ALA
SEQRES 25 A 884 LEU SER GLN CYS LEU PRO THR ILE LEU PRO GLU ASP CYS
SEQRES 26 A 884 SER PHE LEU LYS ARG CYS VAL HIS LEU VAL SER CYS HIS
SEQRES 27 A 884 GLU GLN ARG ALA SER PHE PRO LEU ASP SER ILE ARG ARG
SEQRES 28 A 884 ARG ASP MSE ASP ALA ASN GLY ARG ARG THR GLY PRO SER
SEQRES 29 A 884 CYS TYR ARG LYS TRP THR VAL GLU TYR ALA TYR PRO GLY
SEQRES 30 A 884 VAL HIS SER ASP VAL GLY GLY GLY TYR GLY VAL GLY ASN
SEQRES 31 A 884 GLN GLY LYS ALA VAL GLY GLY SER GLU PHE LEU LEU SER
SEQRES 32 A 884 GLN ILE ALA LEU GLN HIS MSE TYR ALA GLU ALA PHE GLU
SEQRES 33 A 884 ALA GLY ALA PRO LEU GLN VAL PRO ALA PRO ALA VAL HIS
SEQRES 34 A 884 PRO ASP PHE HIS GLU GLU TRP ARG VAL MSE VAL PRO LYS
SEQRES 35 A 884 ILE GLU ALA GLU PHE SER VAL SER GLU GLU LEU ALA THR
SEQRES 36 A 884 ARG PHE ASN ALA TRP GLN ALA GLN ALA LYS ALA GLY PRO
SEQRES 37 A 884 LEU GLU GLU VAL ILE ARG ARG GLU THR ALA LEU ILE THR
SEQRES 38 A 884 ALA TRP ARG ILE ASP ARG TYR ALA GLY GLY LEU ARG ASN
SEQRES 39 A 884 LYS ALA PHE PHE ALA ASN VAL PRO PRO ASP MSE PRO GLU
SEQRES 40 A 884 ALA GLN GLN LYS ALA TRP GLU ALA LEU HIS LYS ARG ARG
SEQRES 41 A 884 SER ARG GLU TYR ALA ALA ALA GLN GLN GLY GLU PRO LEU
SEQRES 42 A 884 PRO PRO MSE SER ALA ALA GLU GLN ALA GLU TRP ASP ARG
SEQRES 43 A 884 ASN VAL ALA LEU ILE GLY GLY GLU ASP GLN LEU ARG ASP
SEQRES 44 A 884 LEU ARG VAL GLU LYS GLN PHE ASP PRO PRO LEU ASP GLN
SEQRES 45 A 884 ARG GLN LEU LEU GLY ALA ALA ALA GLU PHE ALA HIS ASP
SEQRES 46 A 884 TYR LYS GLY ASP TRP GLY VAL LEU ASP ASP GLY MSE THR
SEQRES 47 A 884 VAL GLY GLY VAL ILE ASP LEU LEU LEU GLY GLY THR VAL
SEQRES 48 A 884 PHE LEU ILE ASN GLU GLU ASP GLU ALA GLU GLU TYR SER
SEQRES 49 A 884 GLN ILE HIS ARG ASP GLY SER ALA ARG TYR HIS GLN LEU
SEQRES 50 A 884 PHE SER ALA PRO ASP ARG VAL ALA PRO GLY GLN GLU LYS
SEQRES 51 A 884 LEU VAL ALA LEU PHE ASP GLU GLN VAL HIS ASP SER ARG
SEQRES 52 A 884 ALA TRP PHE MSE ASN THR SER ALA ILE GLY PRO ARG GLU
SEQRES 53 A 884 PRO PHE THR ASP TYR PHE ARG TYR ARG LEU VAL HIS PHE
SEQRES 54 A 884 ASP ASN GLU SER ASN LYS ARG LEU SER VAL LEU ALA THR
SEQRES 55 A 884 ALA GLY ARG VAL VAL GLY VAL GLY VAL MSE LEU ALA SER
SEQRES 56 A 884 VAL GLY LEU SER VAL LYS ARG ARG ASP PRO ARG MSE LEU
SEQRES 57 A 884 LEU GLY LEU PHE LEU PRO SER LEU ALA ARG PRO LEU LEU
SEQRES 58 A 884 SER GLY LYS VAL GLY LEU PRO GLU ILE SER ALA PHE ASP
SEQRES 59 A 884 PRO LEU THR GLY ILE ALA LEU PRO MSE VAL GLY GLY ALA
SEQRES 60 A 884 ALA LEU ASP ASN LEU ARG ALA PHE THR ARG GLU PRO GLY
SEQRES 61 A 884 ASP LYS VAL GLU GLN ILE GLY GLN LEU PRO PRO PRO PRO
SEQRES 62 A 884 PRO LEU ALA VAL ALA ALA VAL GLN SER PRO ALA LEU GLN
SEQRES 63 A 884 GLN VAL LEU LEU ALA GLN GLN THR VAL GLU ALA LEU LYS
SEQRES 64 A 884 ALA ARG ASP LEU GLY SER LEU ALA GLY LEU VAL ALA LYS
SEQRES 65 A 884 ALA GLU LEU THR GLN ALA PRO ALA ALA ALA THR PRO ALA
SEQRES 66 A 884 TRP LEU ALA GLU ALA LYS GLN ALA LEU GLN ASP MSE GLY
SEQRES 67 A 884 THR GLU GLN ALA GLN PRO PRO GLY PRO GLY SER ALA PRO
SEQRES 68 A 884 GLY TRP LEU LYS ARG GLY LYS ASP LEU MSE GLU SER LEU
SEQRES 1 B 884 GLY SER MSE PRO ASN PHE GLY PHE HIS ILE ALA PRO THR
SEQRES 2 B 884 HIS PRO VAL ALA GLY ARG LEU THR TYR ASP SER LYS LYS
SEQRES 3 B 884 LEU SER GLU ASN ILE LEU LYS GLN GLN SER ASP GLU ARG
SEQRES 4 B 884 VAL PHE SER ARG ALA GLN GLU GLN LYS ARG LEU SER GLU
SEQRES 5 B 884 GLY ASP VAL VAL GLY GLY ALA PRO CYS CYS LYS ALA ILE
SEQRES 6 B 884 HIS ILE THR LEU GLY PHE ASP GLY THR ASN ASN ASN ASP
SEQRES 7 B 884 LYS ALA ASP GLY SER SER VAL SER PRO SER CYS SER ASN
SEQRES 8 B 884 VAL ALA ARG LEU ILE HIS ALA SER ILE GLY SER GLY ASP
SEQRES 9 B 884 ASP ILE ASN SER ARG GLY ILE PHE LYS TYR TYR CYS PRO
SEQRES 10 B 884 GLY VAL GLY THR VAL PHE PRO ASP ILE LYS GLU PHE THR
SEQRES 11 B 884 PRO SER ASN MSE GLY LEU ILE GLY ALA GLU GLY GLY GLU
SEQRES 12 B 884 ASN ARG ILE ASN TRP GLY LEU VAL GLN LEU VAL ASP ALA
SEQRES 13 B 884 LEU PHE TYR THR LEU LEU LYS SER ARG LEU LYS LEU ASN
SEQRES 14 B 884 ASP VAL GLN GLY LEU VAL GLU GLU MSE SER THR ASN TRP
SEQRES 15 B 884 THR VAL SER THR LEU THR GLY GLY LEU LEU GLU ASN GLY
SEQRES 16 B 884 GLU LYS LYS ARG ARG ALA ALA LEU GLU PRO LYS LEU LYS
SEQRES 17 B 884 GLU LEU GLU GLU LYS LEU ARG GLN ARG GLN ASN SER GLY
SEQRES 18 B 884 GLN LYS PRO HIS ILE LEU ALA MSE ARG LEU TYR ILE TYR
SEQRES 19 B 884 GLY PHE SER ARG GLY ALA ALA GLU ALA ARG ALA PHE ALA
SEQRES 20 B 884 ASN TRP LEU GLN GLU LEU THR ARG VAL SER ASP ALA ASP
SEQRES 21 B 884 GLY ARG VAL GLU TYR ARG PHE ALA GLY LEU PRO ILE SER
SEQRES 22 B 884 ILE GLU PHE LEU GLY LEU PHE ASP THR VAL ALA ALA VAL
SEQRES 23 B 884 GLY LEU ALA ASP SER ALA PRO PHE ALA ALA GLY HIS MSE
SEQRES 24 B 884 ASP TRP ALA ASP ASP THR MSE ARG LEU PRO ASP GLU ALA
SEQRES 25 B 884 LEU SER GLN CYS LEU PRO THR ILE LEU PRO GLU ASP CYS
SEQRES 26 B 884 SER PHE LEU LYS ARG CYS VAL HIS LEU VAL SER CYS HIS
SEQRES 27 B 884 GLU GLN ARG ALA SER PHE PRO LEU ASP SER ILE ARG ARG
SEQRES 28 B 884 ARG ASP MSE ASP ALA ASN GLY ARG ARG THR GLY PRO SER
SEQRES 29 B 884 CYS TYR ARG LYS TRP THR VAL GLU TYR ALA TYR PRO GLY
SEQRES 30 B 884 VAL HIS SER ASP VAL GLY GLY GLY TYR GLY VAL GLY ASN
SEQRES 31 B 884 GLN GLY LYS ALA VAL GLY GLY SER GLU PHE LEU LEU SER
SEQRES 32 B 884 GLN ILE ALA LEU GLN HIS MSE TYR ALA GLU ALA PHE GLU
SEQRES 33 B 884 ALA GLY ALA PRO LEU GLN VAL PRO ALA PRO ALA VAL HIS
SEQRES 34 B 884 PRO ASP PHE HIS GLU GLU TRP ARG VAL MSE VAL PRO LYS
SEQRES 35 B 884 ILE GLU ALA GLU PHE SER VAL SER GLU GLU LEU ALA THR
SEQRES 36 B 884 ARG PHE ASN ALA TRP GLN ALA GLN ALA LYS ALA GLY PRO
SEQRES 37 B 884 LEU GLU GLU VAL ILE ARG ARG GLU THR ALA LEU ILE THR
SEQRES 38 B 884 ALA TRP ARG ILE ASP ARG TYR ALA GLY GLY LEU ARG ASN
SEQRES 39 B 884 LYS ALA PHE PHE ALA ASN VAL PRO PRO ASP MSE PRO GLU
SEQRES 40 B 884 ALA GLN GLN LYS ALA TRP GLU ALA LEU HIS LYS ARG ARG
SEQRES 41 B 884 SER ARG GLU TYR ALA ALA ALA GLN GLN GLY GLU PRO LEU
SEQRES 42 B 884 PRO PRO MSE SER ALA ALA GLU GLN ALA GLU TRP ASP ARG
SEQRES 43 B 884 ASN VAL ALA LEU ILE GLY GLY GLU ASP GLN LEU ARG ASP
SEQRES 44 B 884 LEU ARG VAL GLU LYS GLN PHE ASP PRO PRO LEU ASP GLN
SEQRES 45 B 884 ARG GLN LEU LEU GLY ALA ALA ALA GLU PHE ALA HIS ASP
SEQRES 46 B 884 TYR LYS GLY ASP TRP GLY VAL LEU ASP ASP GLY MSE THR
SEQRES 47 B 884 VAL GLY GLY VAL ILE ASP LEU LEU LEU GLY GLY THR VAL
SEQRES 48 B 884 PHE LEU ILE ASN GLU GLU ASP GLU ALA GLU GLU TYR SER
SEQRES 49 B 884 GLN ILE HIS ARG ASP GLY SER ALA ARG TYR HIS GLN LEU
SEQRES 50 B 884 PHE SER ALA PRO ASP ARG VAL ALA PRO GLY GLN GLU LYS
SEQRES 51 B 884 LEU VAL ALA LEU PHE ASP GLU GLN VAL HIS ASP SER ARG
SEQRES 52 B 884 ALA TRP PHE MSE ASN THR SER ALA ILE GLY PRO ARG GLU
SEQRES 53 B 884 PRO PHE THR ASP TYR PHE ARG TYR ARG LEU VAL HIS PHE
SEQRES 54 B 884 ASP ASN GLU SER ASN LYS ARG LEU SER VAL LEU ALA THR
SEQRES 55 B 884 ALA GLY ARG VAL VAL GLY VAL GLY VAL MSE LEU ALA SER
SEQRES 56 B 884 VAL GLY LEU SER VAL LYS ARG ARG ASP PRO ARG MSE LEU
SEQRES 57 B 884 LEU GLY LEU PHE LEU PRO SER LEU ALA ARG PRO LEU LEU
SEQRES 58 B 884 SER GLY LYS VAL GLY LEU PRO GLU ILE SER ALA PHE ASP
SEQRES 59 B 884 PRO LEU THR GLY ILE ALA LEU PRO MSE VAL GLY GLY ALA
SEQRES 60 B 884 ALA LEU ASP ASN LEU ARG ALA PHE THR ARG GLU PRO GLY
SEQRES 61 B 884 ASP LYS VAL GLU GLN ILE GLY GLN LEU PRO PRO PRO PRO
SEQRES 62 B 884 PRO LEU ALA VAL ALA ALA VAL GLN SER PRO ALA LEU GLN
SEQRES 63 B 884 GLN VAL LEU LEU ALA GLN GLN THR VAL GLU ALA LEU LYS
SEQRES 64 B 884 ALA ARG ASP LEU GLY SER LEU ALA GLY LEU VAL ALA LYS
SEQRES 65 B 884 ALA GLU LEU THR GLN ALA PRO ALA ALA ALA THR PRO ALA
SEQRES 66 B 884 TRP LEU ALA GLU ALA LYS GLN ALA LEU GLN ASP MSE GLY
SEQRES 67 B 884 THR GLU GLN ALA GLN PRO PRO GLY PRO GLY SER ALA PRO
SEQRES 68 B 884 GLY TRP LEU LYS ARG GLY LYS ASP LEU MSE GLU SER LEU
MODRES 4O5P MSE A 132 MET SELENOMETHIONINE
MODRES 4O5P MSE A 176 MET SELENOMETHIONINE
MODRES 4O5P MSE A 227 MET SELENOMETHIONINE
MODRES 4O5P MSE A 297 MET SELENOMETHIONINE
MODRES 4O5P MSE A 304 MET SELENOMETHIONINE
MODRES 4O5P MSE A 352 MET SELENOMETHIONINE
MODRES 4O5P MSE A 408 MET SELENOMETHIONINE
MODRES 4O5P MSE A 437 MET SELENOMETHIONINE
MODRES 4O5P MSE A 503 MET SELENOMETHIONINE
MODRES 4O5P MSE A 534 MET SELENOMETHIONINE
MODRES 4O5P MSE A 595 MET SELENOMETHIONINE
MODRES 4O5P MSE A 710 MET SELENOMETHIONINE
MODRES 4O5P MSE A 725 MET SELENOMETHIONINE
MODRES 4O5P MSE A 761 MET SELENOMETHIONINE
MODRES 4O5P MSE B 132 MET SELENOMETHIONINE
MODRES 4O5P MSE B 176 MET SELENOMETHIONINE
MODRES 4O5P MSE B 227 MET SELENOMETHIONINE
MODRES 4O5P MSE B 297 MET SELENOMETHIONINE
MODRES 4O5P MSE B 304 MET SELENOMETHIONINE
MODRES 4O5P MSE B 352 MET SELENOMETHIONINE
MODRES 4O5P MSE B 408 MET SELENOMETHIONINE
MODRES 4O5P MSE B 437 MET SELENOMETHIONINE
MODRES 4O5P MSE B 503 MET SELENOMETHIONINE
MODRES 4O5P MSE B 534 MET SELENOMETHIONINE
MODRES 4O5P MSE B 595 MET SELENOMETHIONINE
MODRES 4O5P MSE B 710 MET SELENOMETHIONINE
MODRES 4O5P MSE B 725 MET SELENOMETHIONINE
MODRES 4O5P MSE B 761 MET SELENOMETHIONINE
HET MSE A 132 8
HET MSE A 176 8
HET MSE A 227 8
HET MSE A 297 8
HET MSE A 304 8
HET MSE A 352 8
HET MSE A 408 8
HET MSE A 437 8
HET MSE A 503 8
HET MSE A 534 8
HET MSE A 595 8
HET MSE A 710 8
HET MSE A 725 8
HET MSE A 761 8
HET MSE B 132 8
HET MSE B 176 8
HET MSE B 227 8
HET MSE B 297 8
HET MSE B 304 8
HET MSE B 352 8
HET MSE B 408 8
HET MSE B 437 8
HET MSE B 503 8
HET MSE B 534 8
HET MSE B 595 8
HET MSE B 710 8
HET MSE B 725 8
HET MSE B 761 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 28(C5 H11 N O2 SE)
FORMUL 3 HOH *1025(H2 O)
HELIX 1 1 ASP A 21 GLN A 33 1 13
HELIX 2 2 GLN A 33 ALA A 42 1 10
HELIX 3 3 ASN A 75 GLY A 80 1 6
HELIX 4 4 SER A 88 ALA A 96 1 9
HELIX 5 5 GLY A 101 ARG A 107 1 7
HELIX 6 6 PHE A 121 LYS A 125 5 5
HELIX 7 7 GLY A 136 LYS A 161 1 26
HELIX 8 8 LYS A 165 SER A 177 1 13
HELIX 9 9 ASN A 192 SER A 218 1 27
HELIX 10 10 SER A 235 ARG A 253 1 19
HELIX 11 11 TRP A 299 ASP A 301 5 3
HELIX 12 12 VAL A 376 GLY A 382 1 7
HELIX 13 13 GLY A 387 LYS A 391 5 5
HELIX 14 14 GLY A 395 LEU A 399 5 5
HELIX 15 15 LEU A 400 ALA A 415 1 16
HELIX 16 16 VAL A 438 GLU A 444 1 7
HELIX 17 17 SER A 448 ALA A 462 1 15
HELIX 18 18 PRO A 466 TYR A 486 1 21
HELIX 19 19 GLY A 489 LYS A 493 5 5
HELIX 20 20 ALA A 494 VAL A 499 5 6
HELIX 21 21 PRO A 504 GLN A 527 1 24
HELIX 22 22 SER A 535 ILE A 549 1 15
HELIX 23 23 GLY A 551 LEU A 558 5 8
HELIX 24 24 LEU A 568 GLY A 586 1 19
HELIX 25 25 ASN A 613 LEU A 635 1 23
HELIX 26 26 GLN A 646 GLN A 656 1 11
HELIX 27 27 THR A 677 ARG A 681 5 5
HELIX 28 28 PRO A 723 LEU A 727 5 5
HELIX 29 29 GLY A 764 ARG A 771 1 8
HELIX 30 30 GLU A 776 GLN A 786 1 11
HELIX 31 31 PRO A 792 ALA A 797 1 6
HELIX 32 32 SER A 800 VAL A 813 1 14
HELIX 33 33 ASP B 21 GLN B 33 1 13
HELIX 34 34 GLN B 33 ARG B 41 1 9
HELIX 35 35 SER B 88 ALA B 96 1 9
HELIX 36 36 GLY B 101 ARG B 107 1 7
HELIX 37 37 PHE B 121 LYS B 125 5 5
HELIX 38 38 GLY B 136 LYS B 161 1 26
HELIX 39 39 LYS B 165 SER B 177 1 13
HELIX 40 40 ASN B 192 SER B 218 1 27
HELIX 41 41 SER B 235 THR B 252 1 18
HELIX 42 42 TRP B 299 ASP B 301 5 3
HELIX 43 43 VAL B 376 GLY B 382 1 7
HELIX 44 44 GLY B 387 LYS B 391 5 5
HELIX 45 45 GLY B 395 LEU B 399 5 5
HELIX 46 46 LEU B 400 ALA B 415 1 16
HELIX 47 47 VAL B 438 GLU B 444 1 7
HELIX 48 48 SER B 448 ALA B 462 1 15
HELIX 49 49 PRO B 466 TYR B 486 1 21
HELIX 50 50 GLY B 489 LYS B 493 5 5
HELIX 51 51 ALA B 494 VAL B 499 5 6
HELIX 52 52 PRO B 504 GLN B 527 1 24
HELIX 53 53 SER B 535 GLY B 550 1 16
HELIX 54 54 GLU B 552 LEU B 558 5 7
HELIX 55 55 LEU B 568 GLY B 586 1 19
HELIX 56 56 ASN B 613 LEU B 635 1 23
HELIX 57 57 GLN B 646 GLN B 656 1 11
HELIX 58 58 THR B 677 ARG B 681 5 5
HELIX 59 59 PRO B 723 LEU B 727 5 5
HELIX 60 60 GLY B 764 ARG B 771 1 8
HELIX 61 61 GLU B 776 GLN B 786 1 11
HELIX 62 62 PRO B 792 VAL B 798 1 7
HELIX 63 63 SER B 800 THR B 812 1 13
SHEET 1 A 7 GLY A 5 ILE A 8 0
SHEET 2 A 7 THR A 368 TYR A 373 1 O GLU A 370 N HIS A 7
SHEET 3 A 7 CYS A 329 SER A 334 1 N VAL A 333 O TYR A 371
SHEET 4 A 7 LEU A 268 PHE A 278 1 N LEU A 277 O VAL A 330
SHEET 5 A 7 HIS A 223 PHE A 234 1 N ILE A 231 O GLY A 276
SHEET 6 A 7 CYS A 60 PHE A 69 1 N PHE A 69 O TYR A 232
SHEET 7 A 7 ILE A 109 CYS A 114 1 O CYS A 114 N GLY A 68
SHEET 1 B 5 GLY A 5 ILE A 8 0
SHEET 2 B 5 THR A 368 TYR A 373 1 O GLU A 370 N HIS A 7
SHEET 3 B 5 CYS A 329 SER A 334 1 N VAL A 333 O TYR A 371
SHEET 4 B 5 LEU A 268 PHE A 278 1 N LEU A 277 O VAL A 330
SHEET 5 B 5 ARG A 264 PHE A 265 -1 N PHE A 265 O LEU A 268
SHEET 1 C 2 VAL A 182 SER A 183 0
SHEET 2 C 2 GLY A 187 GLY A 188 -1 O GLY A 187 N SER A 183
SHEET 1 D 4 PHE A 292 MSE A 297 0
SHEET 2 D 4 GLY A 607 ILE A 612 -1 O PHE A 610 N ALA A 293
SHEET 3 D 4 LEU A 695 THR A 700 -1 O LEU A 698 N VAL A 609
SHEET 4 D 4 ARG A 703 VAL A 704 -1 O ARG A 703 N THR A 700
SHEET 1 E 3 LEU A 344 SER A 346 0
SHEET 2 E 3 VAL A 685 PHE A 687 1 O HIS A 686 N LEU A 344
SHEET 3 E 3 GLU A 690 SER A 691 -1 O GLU A 690 N PHE A 687
SHEET 1 F 2 ARG A 349 ASP A 351 0
SHEET 2 F 2 THR A 359 CYS A 363 -1 O CYS A 363 N ARG A 349
SHEET 1 G 3 GLY A 594 ASP A 602 0
SHEET 2 G 3 SER A 713 ARG A 721 -1 O VAL A 718 N VAL A 597
SHEET 3 G 3 GLU A 747 PHE A 751 -1 O GLU A 747 N LYS A 719
SHEET 1 H 2 PHE A 636 ALA A 638 0
SHEET 2 H 2 ARG A 641 VAL A 642 -1 O ARG A 641 N SER A 637
SHEET 1 I 7 GLY B 5 ILE B 8 0
SHEET 2 I 7 THR B 368 TYR B 373 1 O GLU B 370 N HIS B 7
SHEET 3 I 7 CYS B 329 SER B 334 1 N VAL B 333 O TYR B 373
SHEET 4 I 7 LEU B 268 PHE B 278 1 N LEU B 277 O VAL B 330
SHEET 5 I 7 ILE B 224 PHE B 234 1 N ILE B 231 O GLY B 276
SHEET 6 I 7 LYS B 61 PHE B 69 1 N ILE B 63 O ARG B 228
SHEET 7 I 7 ILE B 109 CYS B 114 1 O CYS B 114 N GLY B 68
SHEET 1 J 6 GLY B 5 ILE B 8 0
SHEET 2 J 6 THR B 368 TYR B 373 1 O GLU B 370 N HIS B 7
SHEET 3 J 6 CYS B 329 SER B 334 1 N VAL B 333 O TYR B 373
SHEET 4 J 6 LEU B 268 PHE B 278 1 N LEU B 277 O VAL B 330
SHEET 5 J 6 GLU B 262 PHE B 265 -1 N PHE B 265 O LEU B 268
SHEET 6 J 6 ARG B 253 VAL B 254 -1 N VAL B 254 O GLU B 262
SHEET 1 K 2 VAL B 182 SER B 183 0
SHEET 2 K 2 GLY B 187 GLY B 188 -1 O GLY B 187 N SER B 183
SHEET 1 L 4 ALA B 293 MSE B 297 0
SHEET 2 L 4 GLY B 607 ILE B 612 -1 O PHE B 610 N ALA B 293
SHEET 3 L 4 LEU B 695 THR B 700 -1 O LEU B 698 N VAL B 609
SHEET 4 L 4 ARG B 703 VAL B 704 -1 O ARG B 703 N THR B 700
SHEET 1 M 3 LEU B 344 SER B 346 0
SHEET 2 M 3 VAL B 685 PHE B 687 1 O HIS B 686 N LEU B 344
SHEET 3 M 3 GLU B 690 SER B 691 -1 O GLU B 690 N PHE B 687
SHEET 1 N 2 ARG B 349 ASP B 351 0
SHEET 2 N 2 THR B 359 CYS B 363 -1 O CYS B 363 N ARG B 349
SHEET 1 O 3 GLY B 594 ASP B 602 0
SHEET 2 O 3 SER B 713 ARG B 721 -1 O VAL B 718 N VAL B 597
SHEET 3 O 3 GLU B 747 PHE B 751 -1 O GLU B 747 N LYS B 719
SHEET 1 P 2 PHE B 636 ALA B 638 0
SHEET 2 P 2 ARG B 641 VAL B 642 -1 O ARG B 641 N SER B 637
SSBOND 1 CYS B 314 CYS B 323 1555 1555 2.04
LINK C ASN A 131 N MSE A 132 1555 1555 1.33
LINK C MSE A 132 N GLY A 133 1555 1555 1.33
LINK C GLU A 175 N MSE A 176 1555 1555 1.34
LINK C MSE A 176 N SER A 177 1555 1555 1.34
LINK C ALA A 226 N MSE A 227 1555 1555 1.33
LINK C MSE A 227 N ARG A 228 1555 1555 1.33
LINK C HIS A 296 N MSE A 297 1555 1555 1.33
LINK C MSE A 297 N ASP A 298 1555 1555 1.33
LINK C THR A 303 N MSE A 304 1555 1555 1.33
LINK C MSE A 304 N ARG A 305 1555 1555 1.33
LINK C ASP A 351 N MSE A 352 1555 1555 1.33
LINK C HIS A 407 N MSE A 408 1555 1555 1.34
LINK C MSE A 408 N TYR A 409 1555 1555 1.34
LINK C VAL A 436 N MSE A 437 1555 1555 1.33
LINK C MSE A 437 N VAL A 438 1555 1555 1.33
LINK C ASP A 502 N MSE A 503 1555 1555 1.33
LINK C MSE A 503 N PRO A 504 1555 1555 1.34
LINK C PRO A 533 N MSE A 534 1555 1555 1.33
LINK C MSE A 534 N SER A 535 1555 1555 1.33
LINK C GLY A 594 N MSE A 595 1555 1555 1.33
LINK C MSE A 595 N THR A 596 1555 1555 1.33
LINK C VAL A 709 N MSE A 710 1555 1555 1.33
LINK C MSE A 710 N LEU A 711 1555 1555 1.33
LINK C ARG A 724 N MSE A 725 1555 1555 1.34
LINK C MSE A 725 N LEU A 726 1555 1555 1.33
LINK C PRO A 760 N MSE A 761 1555 1555 1.33
LINK C MSE A 761 N VAL A 762 1555 1555 1.32
LINK C ASN B 131 N MSE B 132 1555 1555 1.33
LINK C MSE B 132 N GLY B 133 1555 1555 1.33
LINK C GLU B 175 N MSE B 176 1555 1555 1.34
LINK C MSE B 176 N SER B 177 1555 1555 1.33
LINK C ALA B 226 N MSE B 227 1555 1555 1.32
LINK C MSE B 227 N ARG B 228 1555 1555 1.33
LINK C HIS B 296 N MSE B 297 1555 1555 1.33
LINK C MSE B 297 N ASP B 298 1555 1555 1.33
LINK C THR B 303 N MSE B 304 1555 1555 1.33
LINK C MSE B 304 N ARG B 305 1555 1555 1.33
LINK C ASP B 351 N MSE B 352 1555 1555 1.33
LINK C HIS B 407 N MSE B 408 1555 1555 1.34
LINK C MSE B 408 N TYR B 409 1555 1555 1.34
LINK C VAL B 436 N MSE B 437 1555 1555 1.33
LINK C MSE B 437 N VAL B 438 1555 1555 1.33
LINK C ASP B 502 N MSE B 503 1555 1555 1.33
LINK C MSE B 503 N PRO B 504 1555 1555 1.34
LINK C PRO B 533 N MSE B 534 1555 1555 1.33
LINK C MSE B 534 N SER B 535 1555 1555 1.33
LINK C GLY B 594 N MSE B 595 1555 1555 1.33
LINK C MSE B 595 N THR B 596 1555 1555 1.33
LINK C VAL B 709 N MSE B 710 1555 1555 1.33
LINK C MSE B 710 N LEU B 711 1555 1555 1.33
LINK C ARG B 724 N MSE B 725 1555 1555 1.34
LINK C MSE B 725 N LEU B 726 1555 1555 1.33
LINK C PRO B 760 N MSE B 761 1555 1555 1.33
LINK C MSE B 761 N VAL B 762 1555 1555 1.33
CISPEP 1 LYS A 221 PRO A 222 0 6.51
CISPEP 2 LYS B 221 PRO B 222 0 -1.92
CISPEP 3 SER B 255 ASP B 256 0 -26.83
CISPEP 4 ASP B 256 ALA B 257 0 -24.86
CISPEP 5 PRO B 291 PHE B 292 0 -10.53
CISPEP 6 VAL B 762 GLY B 763 0 3.32
CRYST1 61.603 81.078 92.145 97.83 89.96 90.01 P 1 2
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 0.016233 0.000003 -0.000011 0.00000
SCALE2 0.000000 0.012334 0.001696 0.00000
SCALE3 0.000000 0.000000 0.010955 0.00000
TER 5754 VAL A 813
TER 11520 THR B 812
MASTER 636 0 28 63 57 0 0 612534 2 280 136
END |