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HEADER UNKNOWN FUNCTION 01-AUG-13 4M0M
TITLE THE CRYSTAL STRUCTURE OF A FUNCTIONALLY UNKNOWN PROTEIN LPG2422 FROM
TITLE 2 LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR. PHILADELPHIA 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA;
SOURCE 3 ORGANISM_TAXID: 272624;
SOURCE 4 STRAIN: PHILADELPHIA 1;
SOURCE 5 GENE: LPG2422;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,H.LI,S.CLANCY,H.SHUMAN,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 21-AUG-13 4M0M 0
JRNL AUTH K.TAN,H.LI,S.CLANCY,H.SHUMAN,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF A FUNCTIONALLY UNKNOWN PROTEIN
JRNL TITL 2 LPG2422 FROM LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR.
JRNL TITL 3 PHILADELPHIA 1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 43522
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2196
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 33.9792 - 5.5156 0.98 2769 157 0.1716 0.2302
REMARK 3 2 5.5156 - 4.3809 1.00 2671 144 0.1502 0.1828
REMARK 3 3 4.3809 - 3.8280 1.00 2651 127 0.1479 0.1947
REMARK 3 4 3.8280 - 3.4784 1.00 2651 126 0.1782 0.2461
REMARK 3 5 3.4784 - 3.2293 1.00 2614 155 0.1951 0.2356
REMARK 3 6 3.2293 - 3.0390 1.00 2613 138 0.2114 0.2728
REMARK 3 7 3.0390 - 2.8869 1.00 2578 146 0.2033 0.2706
REMARK 3 8 2.8869 - 2.7613 1.00 2617 132 0.2107 0.2612
REMARK 3 9 2.7613 - 2.6550 1.00 2604 124 0.2016 0.2531
REMARK 3 10 2.6550 - 2.5634 1.00 2575 133 0.2100 0.2786
REMARK 3 11 2.5634 - 2.4833 1.00 2619 137 0.2173 0.3235
REMARK 3 12 2.4833 - 2.4123 1.00 2582 147 0.2260 0.3165
REMARK 3 13 2.4123 - 2.3488 1.00 2559 143 0.2388 0.2918
REMARK 3 14 2.3488 - 2.2915 0.99 2555 125 0.2479 0.2864
REMARK 3 15 2.2915 - 2.2395 0.95 2423 143 0.2642 0.2927
REMARK 3 16 2.2395 - 2.1918 0.87 2245 119 0.2873 0.3452
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.550
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 : 0.007 5929
REMARK 3 ANGLE : 0.979 8001
REMARK 3 CHIRALITY : 0.066 867
REMARK 3 PLANARITY : 0.004 1051
REMARK 3 DIHEDRAL : 14.483 2263
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 10 through 323 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5168 23.6221 156.3675
REMARK 3 T TENSOR
REMARK 3 T11: 0.2606 T22: 0.4035
REMARK 3 T33: 0.2796 T12: 0.0084
REMARK 3 T13: -0.0274 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 1.5296 L22: 0.9440
REMARK 3 L33: 2.5952 L12: 0.0137
REMARK 3 L13: -0.4391 L23: -0.0983
REMARK 3 S TENSOR
REMARK 3 S11: 0.0184 S12: 0.1392 S13: 0.0379
REMARK 3 S21: -0.0482 S22: -0.0086 S23: 0.0324
REMARK 3 S31: -0.1126 S32: -0.1415 S33: -0.0084
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 324 through 396 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8242 10.2415 186.2404
REMARK 3 T TENSOR
REMARK 3 T11: 0.3600 T22: 0.5090
REMARK 3 T33: 0.3428 T12: -0.0025
REMARK 3 T13: 0.0295 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 2.1531 L22: 1.8732
REMARK 3 L33: 4.8610 L12: -0.4111
REMARK 3 L13: 1.0093 L23: -1.5583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0678 S12: -0.0822 S13: 0.0209
REMARK 3 S21: -0.1467 S22: -0.0709 S23: 0.0106
REMARK 3 S31: 0.2903 S32: 0.1162 S33: 0.0336
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 397 through 628 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9917 -7.4625 163.1511
REMARK 3 T TENSOR
REMARK 3 T11: 0.4432 T22: 0.4557
REMARK 3 T33: 0.4172 T12: 0.0366
REMARK 3 T13: -0.0287 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 2.2924 L22: 0.3553
REMARK 3 L33: 1.5155 L12: -0.5219
REMARK 3 L13: -1.1390 L23: 0.0294
REMARK 3 S TENSOR
REMARK 3 S11: -0.0744 S12: -0.0036 S13: -0.3390
REMARK 3 S21: -0.0432 S22: 0.0690 S23: 0.0467
REMARK 3 S31: 0.3099 S32: 0.3684 S33: 0.0229
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 629 through 737 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2995 11.7839 137.8721
REMARK 3 T TENSOR
REMARK 3 T11: 0.5087 T22: 0.8927
REMARK 3 T33: 0.5073 T12: 0.0510
REMARK 3 T13: 0.0875 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 2.0196 L22: 4.2845
REMARK 3 L33: 1.4781 L12: -2.7871
REMARK 3 L13: 0.8972 L23: -1.9489
REMARK 3 S TENSOR
REMARK 3 S11: 0.3058 S12: 0.5617 S13: 0.3184
REMARK 3 S21: -0.7121 S22: -0.4320 S23: -0.6279
REMARK 3 S31: 0.3670 S32: 0.3910 S33: 0.1962
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 4M0M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-13.
REMARK 100 THE RCSB ID CODE IS RCSB081315.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97937
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43629
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 34.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.64400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/ARP/WARP/HKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CALCIUM ACETATE, 0.1M SODIUM
REMARK 280 CACODYLATE:HCL, 40% PEG300, PH 6.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 34.26400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.62700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.61700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.62700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.26400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.61700
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 SER A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 GLU A 5
REMARK 465 LYS A 6
REMARK 465 ASP A 7
REMARK 465 VAL A 8
REMARK 465 ARG A 9
REMARK 465 LEU A 599
REMARK 465 SER A 600
REMARK 465 SER A 714
REMARK 465 LYS A 715
REMARK 465 LEU A 716
REMARK 465 GLU A 717
REMARK 465 MSE A 718
REMARK 465 VAL A 738
REMARK 465 THR A 739
REMARK 465 LYS A 740
REMARK 465 ASP A 741
REMARK 465 LEU A 742
REMARK 465 VAL A 743
REMARK 465 HIS A 744
REMARK 465 GLU A 745
REMARK 465 GLU A 746
REMARK 465 VAL A 747
REMARK 465 SER A 748
REMARK 465 GLN A 749
REMARK 465 VAL A 750
REMARK 465 LYS A 751
REMARK 465 LEU A 752
REMARK 465 ASN A 753
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 LYS A 64 CE NZ
REMARK 470 LYS A 69 CD CE NZ
REMARK 470 LYS A 81 CD CE NZ
REMARK 470 LYS A 129 CE NZ
REMARK 470 LYS A 133 NZ
REMARK 470 GLU A 193 CG CD OE1 OE2
REMARK 470 LYS A 225 NZ
REMARK 470 GLU A 264 CD OE1 OE2
REMARK 470 LYS A 284 CG CD CE NZ
REMARK 470 GLU A 286 OE1 OE2
REMARK 470 ARG A 289 CD NE CZ NH1 NH2
REMARK 470 LYS A 328 CD CE NZ
REMARK 470 LYS A 395 CD CE NZ
REMARK 470 LYS A 419 CE NZ
REMARK 470 LYS A 452 CG CD CE NZ
REMARK 470 LYS A 480 CD CE NZ
REMARK 470 LYS A 544 CE NZ
REMARK 470 ARG A 569 CD NE CZ NH1 NH2
REMARK 470 LYS A 577 CD CE NZ
REMARK 470 GLN A 671 CG CD OE1 NE2
REMARK 470 LYS A 675 CG CD CE NZ
REMARK 470 ARG A 679 CZ NH1 NH2
REMARK 470 ARG A 703 NE CZ NH1 NH2
REMARK 470 TYR A 710 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 712 CE NZ
REMARK 470 ARG A 736 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 737 CG CD CE NZ
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 144 -128.68 61.07
REMARK 500 ASP A 172 69.47 36.47
REMARK 500 HIS A 235 -50.06 -29.45
REMARK 500 THR A 242 -161.63 -121.71
REMARK 500 LYS A 328 43.07 -146.30
REMARK 500 ASN A 403 68.24 -152.32
REMARK 500 ASP A 429 -174.30 -174.96
REMARK 500 GLU A 451 56.88 -100.91
REMARK 500 ASN A 497 18.74 53.67
REMARK 500 ASN A 608 -158.81 -136.61
REMARK 500 VAL A 734 -6.77 -59.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 802
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 805
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC108377 RELATED DB: TARGETTRACK
DBREF 4M0M A 1 753 UNP Q5ZSU4 Q5ZSU4_LEGPH 1 753
SEQADV 4M0M SER A -2 UNP Q5ZSU4 EXPRESSION TAG
SEQADV 4M0M ASN A -1 UNP Q5ZSU4 EXPRESSION TAG
SEQADV 4M0M ALA A 0 UNP Q5ZSU4 EXPRESSION TAG
SEQRES 1 A 756 SER ASN ALA MSE SER THR SER GLU LYS ASP VAL ARG GLU
SEQRES 2 A 756 GLN LYS VAL LYS THR VAL THR LEU SER PHE LEU GLY THR
SEQRES 3 A 756 GLY GLN HIS ARG GLU LYS VAL HIS HIS ILE LEU THR SER
SEQRES 4 A 756 PHE HIS ASN THR ILE SER GLU VAL ASN LYS ASP ASN PRO
SEQRES 5 A 756 THR VAL ALA MSE ARG MSE PHE ASP GLY PRO GLY SER GLU
SEQRES 6 A 756 PRO LYS SER GLY ASP SER LYS ASP PRO ILE PRO GLY THR
SEQRES 7 A 756 TYR ILE TYR ASN PRO LYS ASP ASN SER LYS ILE LEU ILE
SEQRES 8 A 756 SER PRO VAL ILE SER GLN THR ILE THR ASN ALA ILE GLN
SEQRES 9 A 756 LYS LEU THR GLY ASN LEU ALA GLY GLU GLY ILE GLU HIS
SEQRES 10 A 756 LEU LEU PHE GLU ALA VAL LEU TYR LEU ASN ASP ILE ILE
SEQRES 11 A 756 GLU LYS ASN GLY GLY LYS LEU PRO GLU THR VAL ASN LEU
SEQRES 12 A 756 HIS GLY PHE SER ARG GLY ALA ASP THR CYS MSE ARG MSE
SEQRES 13 A 756 ALA ASN LEU LEU TYR GLN LEU TYR PRO ASP ILE LYS VAL
SEQRES 14 A 756 ASN LEU PHE LEU ILE ASP GLN VAL PRO GLY PRO GLY LYS
SEQRES 15 A 756 ARG ASP ASP PRO HIS SER TYR THR VAL PRO PRO ASN VAL
SEQRES 16 A 756 GLU HIS PHE GLU SER THR LEU MSE LEU HIS GLU TYR ARG
SEQRES 17 A 756 PRO GLY PHE ASP PRO GLN HIS SER GLY ARG TYR VAL ILE
SEQRES 18 A 756 ALA ASP PRO GLU LYS THR LYS VAL VAL VAL LYS PRO TYR
SEQRES 19 A 756 TYR GLY GLU HIS ASN THR GLY ASN ARG VAL THR GLU ASP
SEQRES 20 A 756 PRO ASN THR ASN HIS THR ALA ILE LEU LEU ASN ASP ASP
SEQRES 21 A 756 MSE ASN ARG PHE CYS ARG GLU THR GLY SER LEU PRO SER
SEQRES 22 A 756 VAL GLY ILE SER PRO PRO ILE ILE ALA ARG VAL GLY ASP
SEQRES 23 A 756 LYS LYS GLU GLU VAL ARG THR HIS SER GLU LEU SER PRO
SEQRES 24 A 756 GLU LYS ARG PHE GLU LEU LEU CYS GLY MSE LYS GLU ASN
SEQRES 25 A 756 GLU TRP GLY TYR ALA LYS LEU THR LYS LYS TYR HIS GLU
SEQRES 26 A 756 ARG SER ILE LEU SER LYS ARG GLU ASP TYR VAL GLN ASP
SEQRES 27 A 756 SER ARG LEU PHE VAL ASN GLN GLU HIS ARG GLU LEU PHE
SEQRES 28 A 756 LYS GLN LEU TYR PRO LYS SER PHE ASN TRP PHE PHE GLU
SEQRES 29 A 756 LYS ASN HIS GLY GLY GLN THR LYS LYS GLU GLU VAL ILE
SEQRES 30 A 756 VAL GLU LEU LYS SER LEU SER GLU ASP PRO ARG TYR GLU
SEQRES 31 A 756 HIS PHE PHE SER SER LEU ALA LYS HIS PHE GLN ILE ASN
SEQRES 32 A 756 GLU ASN ASN ILE ALA GLY THR LEU PRO GLU PRO SER GLY
SEQRES 33 A 756 ILE ASP ARG ASP GLU LYS SER SER PHE GLY GLN PRO PRO
SEQRES 34 A 756 VAL ARG ASP ARG LEU SER TYR LEU GLN HIS SER LEU THR
SEQRES 35 A 756 SER ILE ALA ASN TYR TYR HIS TYR HIS CYS ASP GLU LYS
SEQRES 36 A 756 SER SER THR ASN GLU SER VAL LYS ASN LEU LEU LEU GLU
SEQRES 37 A 756 ARG VAL LYS GLU SER ARG THR LYS PRO ASP SER GLU ALA
SEQRES 38 A 756 ILE LYS HIS LEU GLU GLN THR MSE ASP GLU VAL ARG GLN
SEQRES 39 A 756 ILE LEU GLU SER LYS ASN GLU LYS GLY PHE LEU TRP GLN
SEQRES 40 A 756 GLN ILE ASN HIS ILE SER PRO ASN ALA ARG GLN TYR CYS
SEQRES 41 A 756 GLU GLN VAL LYS ALA ALA LEU ARG GLU HIS LEU GLU HIS
SEQRES 42 A 756 ASN GLN VAL LEU SER ASP THR GLN LYS GLU GLU ILE ARG
SEQRES 43 A 756 LYS ALA MSE ASP ARG MSE ASP ASN ILE VAL ASN ASP SER
SEQRES 44 A 756 SER LYS ASP SER GLN GLN LYS TYR ARG GLU ILE ARG ARG
SEQRES 45 A 756 GLU VAL ILE GLU LEU ASN ALA LYS ALA THR THR PRO GLU
SEQRES 46 A 756 ASP ASP ASN GLN LEU THR ARG SER HIS PHE GLN LYS ALA
SEQRES 47 A 756 TYR PHE GLU LEU SER GLY ASP THR GLN LYS THR LEU ASN
SEQRES 48 A 756 LEU GLU SER LEU SER GLN THR LEU ASN GLN LEU SER LYS
SEQRES 49 A 756 ALA HIS TYR GLY GLU THR SER MSE THR ASP LYS ILE THR
SEQRES 50 A 756 GLN ARG LEU ASP GLY TYR LYS ASN ARG ASN TRP PHE TRP
SEQRES 51 A 756 ASN SER VAL LYS GLU VAL LEU ASN PHE PHE ASN ILE PRO
SEQRES 52 A 756 LEU PRO LYS LEU HIS SER GLU VAL LYS GLU GLN ILE ALA
SEQRES 53 A 756 ASP LYS LEU LYS GLU ARG LEU VAL ASP LEU LYS GLU LYS
SEQRES 54 A 756 GLY MSE GLY ASN ASP VAL ASN ALA ILE THR ARG GLU LEU
SEQRES 55 A 756 GLY LYS ALA ARG GLU ASP LEU ILE GLU HIS TYR LYS LYS
SEQRES 56 A 756 THR SER LYS LEU GLU MSE GLY GLU LEU ASP LYS ILE ILE
SEQRES 57 A 756 ASN LYS SER MSE GLU GLU LEU LEU VAL ALA ARG LYS VAL
SEQRES 58 A 756 THR LYS ASP LEU VAL HIS GLU GLU VAL SER GLN VAL LYS
SEQRES 59 A 756 LEU ASN
MODRES 4M0M MSE A 53 MET SELENOMETHIONINE
MODRES 4M0M MSE A 55 MET SELENOMETHIONINE
MODRES 4M0M MSE A 151 MET SELENOMETHIONINE
MODRES 4M0M MSE A 153 MET SELENOMETHIONINE
MODRES 4M0M MSE A 200 MET SELENOMETHIONINE
MODRES 4M0M MSE A 258 MET SELENOMETHIONINE
MODRES 4M0M MSE A 306 MET SELENOMETHIONINE
MODRES 4M0M MSE A 486 MET SELENOMETHIONINE
MODRES 4M0M MSE A 546 MET SELENOMETHIONINE
MODRES 4M0M MSE A 549 MET SELENOMETHIONINE
MODRES 4M0M MSE A 629 MET SELENOMETHIONINE
MODRES 4M0M MSE A 688 MET SELENOMETHIONINE
MODRES 4M0M MSE A 729 MET SELENOMETHIONINE
HET MSE A 53 8
HET MSE A 55 8
HET MSE A 151 8
HET MSE A 153 8
HET MSE A 200 8
HET MSE A 258 8
HET MSE A 306 8
HET MSE A 486 8
HET MSE A 546 8
HET MSE A 549 8
HET MSE A 629 8
HET MSE A 688 8
HET MSE A 729 8
HET PG4 A 801 13
HET PG4 A 802 10
HET PG4 A 803 13
HET PO4 A 804 5
HET PO4 A 805 5
HETNAM MSE SELENOMETHIONINE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PO4 PHOSPHATE ION
FORMUL 1 MSE 13(C5 H11 N O2 SE)
FORMUL 2 PG4 3(C8 H18 O5)
FORMUL 5 PO4 2(O4 P 3-)
FORMUL 7 HOH *82(H2 O)
HELIX 1 1 HIS A 32 ASN A 45 1 14
HELIX 2 2 SER A 89 GLY A 105 1 17
HELIX 3 3 GLY A 111 ASN A 130 1 20
HELIX 4 4 SER A 144 TYR A 161 1 18
HELIX 5 5 ASP A 182 TYR A 186 1 5
HELIX 6 6 ASN A 236 ARG A 240 5 5
HELIX 7 7 ASP A 244 THR A 247 5 4
HELIX 8 8 ASN A 248 THR A 265 1 18
HELIX 9 9 SER A 295 ASN A 309 1 15
HELIX 10 10 ASN A 309 LYS A 315 1 7
HELIX 11 11 LYS A 328 TYR A 332 5 5
HELIX 12 12 ASN A 341 TYR A 352 1 12
HELIX 13 13 TYR A 352 GLU A 361 1 10
HELIX 14 14 LYS A 369 ASP A 383 1 15
HELIX 15 15 TYR A 386 PHE A 397 1 12
HELIX 16 16 ASN A 403 LEU A 408 1 6
HELIX 17 17 ASP A 429 CYS A 449 1 21
HELIX 18 18 SER A 453 ARG A 471 1 19
HELIX 19 19 PRO A 474 LYS A 496 1 23
HELIX 20 20 GLY A 500 ASN A 507 1 8
HELIX 21 21 ASN A 512 ASN A 531 1 20
HELIX 22 22 SER A 535 ASN A 554 1 20
HELIX 23 23 ASP A 559 THR A 579 1 21
HELIX 24 24 ASP A 583 PHE A 597 1 15
HELIX 25 25 ASN A 608 SER A 620 1 13
HELIX 26 26 SER A 628 PHE A 657 1 30
HELIX 27 27 SER A 666 LYS A 686 1 21
HELIX 28 28 ASP A 691 HIS A 709 1 19
HELIX 29 29 GLU A 720 VAL A 734 1 15
SHEET 1 A 6 VAL A 51 PHE A 56 0
SHEET 2 A 6 THR A 15 PHE A 20 1 N THR A 15 O ALA A 52
SHEET 3 A 6 THR A 137 PHE A 143 1 O ASN A 139 N VAL A 16
SHEET 4 A 6 LYS A 165 ILE A 171 1 O ASN A 167 N LEU A 140
SHEET 5 A 6 VAL A 192 MSE A 200 1 O GLU A 196 N LEU A 170
SHEET 6 A 6 LYS A 225 TYR A 231 1 O LYS A 225 N GLU A 193
SHEET 1 B 2 TYR A 76 ASN A 79 0
SHEET 2 B 2 SER A 84 LEU A 87 -1 O SER A 84 N ASN A 79
SHEET 1 C 2 THR A 187 VAL A 188 0
SHEET 2 C 2 VAL A 217 ILE A 218 1 O VAL A 217 N VAL A 188
SHEET 1 D 2 ILE A 277 VAL A 281 0
SHEET 2 D 2 LYS A 284 VAL A 288 -1 O GLU A 286 N ALA A 279
LINK C ALA A 52 N MSE A 53 1555 1555 1.33
LINK C MSE A 53 N ARG A 54 1555 1555 1.33
LINK C ARG A 54 N MSE A 55 1555 1555 1.33
LINK C MSE A 55 N PHE A 56 1555 1555 1.33
LINK C CYS A 150 N MSE A 151 1555 1555 1.33
LINK C MSE A 151 N ARG A 152 1555 1555 1.33
LINK C ARG A 152 N MSE A 153 1555 1555 1.33
LINK C MSE A 153 N ALA A 154 1555 1555 1.33
LINK C LEU A 199 N MSE A 200 1555 1555 1.33
LINK C MSE A 200 N LEU A 201 1555 1555 1.33
LINK C ASP A 257 N MSE A 258 1555 1555 1.33
LINK C MSE A 258 N ASN A 259 1555 1555 1.34
LINK C GLY A 305 N MSE A 306 1555 1555 1.33
LINK C MSE A 306 N LYS A 307 1555 1555 1.33
LINK C THR A 485 N MSE A 486 1555 1555 1.33
LINK C MSE A 486 N ASP A 487 1555 1555 1.33
LINK C ALA A 545 N MSE A 546 1555 1555 1.33
LINK C MSE A 546 N ASP A 547 1555 1555 1.33
LINK C ARG A 548 N MSE A 549 1555 1555 1.33
LINK C MSE A 549 N ASP A 550 1555 1555 1.33
LINK C SER A 628 N MSE A 629 1555 1555 1.33
LINK C MSE A 629 N THR A 630 1555 1555 1.33
LINK C GLY A 687 N MSE A 688 1555 1555 1.33
LINK C MSE A 688 N GLY A 689 1555 1555 1.33
LINK C SER A 728 N MSE A 729 1555 1555 1.33
LINK C MSE A 729 N GLU A 730 1555 1555 1.33
SITE 1 AC1 5 THR A 242 ARG A 514 SER A 556 LYS A 558
SITE 2 AC1 5 LYS A 563
SITE 1 AC2 5 GLY A 132 ASP A 163 ASN A 402 GLU A 720
SITE 2 AC2 5 LYS A 727
SITE 1 AC3 4 ALA A 219 HIS A 508 TYR A 624 GLY A 625
SITE 1 AC4 4 ARG A 180 HIS A 212 ARG A 215 SER A 324
SITE 1 AC5 5 ASN A 236 ARG A 240 ARG A 280 GLN A 367
SITE 2 AC5 5 HOH A 977
CRYST1 68.528 69.234 177.254 90.00 90.00 90.00 P 21 21 21 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 0.014593 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014444 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005642 0.00000
TER 5770 LYS A 737
MASTER 400 0 18 29 12 0 8 6 5897 1 176 59
END |