HEADER TRANSPORT PROTEIN 02-SEP-16 5T77
TITLE CRYSTAL STRUCTURE OF THE MOP FLIPPASE MURJ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE LIPID II FLIPPASE MURJ;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSIPHO AFRICANUS (STRAIN TCF52B);
SOURCE 3 ORGANISM_TAXID: 484019;
SOURCE 4 STRAIN: TCF52B;
SOURCE 5 GENE: MVIN, THA_1814;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSPORTER, FLIPPASE, PEPTIDOGLYCAN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.Y.KUK,S.-Y.LEE
REVDAT 4 06-MAR-24 5T77 1 LINK
REVDAT 3 15-FEB-17 5T77 1 JRNL
REVDAT 2 04-JAN-17 5T77 1 JRNL
REVDAT 1 28-DEC-16 5T77 0
JRNL AUTH A.C.KUK,E.H.MASHALIDIS,S.Y.LEE
JRNL TITL CRYSTAL STRUCTURE OF THE MOP FLIPPASE MURJ IN AN
JRNL TITL 2 INWARD-FACING CONFORMATION.
JRNL REF NAT. STRUCT. MOL. BIOL. V. 24 171 2017
JRNL REFN ESSN 1545-9985
JRNL PMID 28024149
JRNL DOI 10.1038/NSMB.3346
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 41953
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2092
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 34.1965 - 4.9279 0.97 2697 137 0.1955 0.2167
REMARK 3 2 4.9279 - 3.9132 0.96 2625 138 0.1810 0.2100
REMARK 3 3 3.9132 - 3.4191 0.99 2683 147 0.1746 0.2033
REMARK 3 4 3.4191 - 3.1067 0.99 2682 143 0.1745 0.1979
REMARK 3 5 3.1067 - 2.8841 0.99 2709 130 0.1786 0.2139
REMARK 3 6 2.8841 - 2.7142 0.99 2672 150 0.1696 0.1906
REMARK 3 7 2.7142 - 2.5783 0.99 2708 135 0.1614 0.1883
REMARK 3 8 2.5783 - 2.4661 0.99 2679 142 0.1673 0.1912
REMARK 3 9 2.4661 - 2.3712 0.99 2675 143 0.1758 0.1851
REMARK 3 10 2.3712 - 2.2894 0.99 2688 142 0.1853 0.2055
REMARK 3 11 2.2894 - 2.2178 0.98 2660 138 0.2236 0.2744
REMARK 3 12 2.2178 - 2.1544 0.99 2653 141 0.2203 0.2221
REMARK 3 13 2.1544 - 2.0977 0.97 2659 139 0.2370 0.2684
REMARK 3 14 2.0977 - 2.0465 0.95 2572 136 0.2743 0.3144
REMARK 3 15 2.0465 - 2.0000 0.93 2499 131 0.3003 0.3223
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.980
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 : 0.009 4348
REMARK 3 ANGLE : 0.546 5691
REMARK 3 CHIRALITY : 0.039 634
REMARK 3 PLANARITY : 0.003 655
REMARK 3 DIHEDRAL : 11.878 2473
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): 149.2486 38.2960 143.0684
REMARK 3 T TENSOR
REMARK 3 T11: 0.2190 T22: 0.2565
REMARK 3 T33: 0.2493 T12: 0.0021
REMARK 3 T13: 0.0111 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 0.5234 L22: 3.1519
REMARK 3 L33: 2.2643 L12: -0.2136
REMARK 3 L13: -0.5335 L23: 2.0140
REMARK 3 S TENSOR
REMARK 3 S11: 0.0266 S12: 0.0079 S13: -0.1158
REMARK 3 S21: 0.0593 S22: -0.0416 S23: -0.0670
REMARK 3 S31: 0.0792 S32: 0.0140 S33: 0.0150
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 246 THROUGH 433 )
REMARK 3 ORIGIN FOR THE GROUP (A): 137.1820 37.1064 167.0961
REMARK 3 T TENSOR
REMARK 3 T11: 0.2039 T22: 0.2445
REMARK 3 T33: 0.1837 T12: 0.0242
REMARK 3 T13: 0.0170 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 1.3525 L22: 3.2417
REMARK 3 L33: 1.6419 L12: 0.9906
REMARK 3 L13: -0.4437 L23: -1.0409
REMARK 3 S TENSOR
REMARK 3 S11: -0.0058 S12: -0.1288 S13: -0.1558
REMARK 3 S21: 0.1475 S22: -0.0138 S23: -0.0484
REMARK 3 S31: 0.1562 S32: -0.0231 S33: 0.0196
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 434 THROUGH 470 )
REMARK 3 ORIGIN FOR THE GROUP (A): 148.8867 39.6504 183.7386
REMARK 3 T TENSOR
REMARK 3 T11: 0.4460 T22: 0.5223
REMARK 3 T33: 0.3117 T12: -0.0213
REMARK 3 T13: -0.1632 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 5.7076 L22: 8.2103
REMARK 3 L33: 6.9084 L12: 3.4694
REMARK 3 L13: -1.2267 L23: -4.3847
REMARK 3 S TENSOR
REMARK 3 S11: 0.3445 S12: -0.4235 S13: -0.3122
REMARK 3 S21: 1.3833 S22: -0.4179 S23: -0.7536
REMARK 3 S31: -0.2781 S32: 0.5777 S33: 0.0734
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 5T77 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000223647.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41992
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, CALCIUM CHLORIDE, LIPIDIC
REMARK 280 CUBIC PHASE, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 47.08150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.78650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 47.08150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.78650
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 TOTAL BURIED SURFACE AREA: 2780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -139.0 KCAL/MOL
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 MET A 1
REMARK 465 SER A 2
REMARK 465 ILE A 3
REMARK 465 TYR A 471
REMARK 465 ALA A 472
REMARK 465 ARG A 473
REMARK 465 LYS A 474
REMARK 465 LYS A 475
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 ILE A 8 CG1 CG2 CD1
REMARK 470 LEU A 9 CG CD1 CD2
REMARK 470 LYS A 197 CD CE NZ
REMARK 470 LYS A 216 CD CE NZ
REMARK 470 LYS A 275 CE NZ
REMARK 470 LYS A 415 CD CE NZ
REMARK 470 ARG A 463 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 465 CG CD1 CD2
REMARK 470 ARG A 467 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 468 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 470 CG CD1 CD2
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 A 672 O HOH A 729 1.95
REMARK 500 O HOH A 604 O HOH A 616 2.07
REMARK 500 O HOH A 741 O HOH A 747 2.13
REMARK 500 O HOH A 740 O HOH A 744 2.18
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 A 703 O HOH A 737 49410 2.10
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 VAL A 266 -58.61 -127.19
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 OLB A 515
REMARK 610 OLB A 517
REMARK 610 OLB A 518
REMARK 610 OLB A 519
REMARK 610 OLB A 520
REMARK 610 OLB A 521
REMARK 610 OLC A 523
REMARK 610 OLC A 524
REMARK 610 OLC A 525
REMARK 610 OLC A 526
REMARK 610 OLC A 527
REMARK 610 OLC A 529
REMARK 610 OLC A 530
REMARK 610 OLC A 531
REMARK 610 OLC A 532
REMARK 610 OLC A 533
REMARK 610 OLC A 534
REMARK 610 OLC A 535
REMARK 610 OLC A 536
REMARK 610 OLC A 537
REMARK 610 OLC A 538
REMARK 610 OLC A 539
REMARK 610 OLC A 540
REMARK 610 OLC A 541
REMARK 610 OLC A 542
REMARK 610 OLC A 543
REMARK 610 OLC A 544
REMARK 610 OLC A 545
REMARK 610 OLC A 546
REMARK 610 OLC A 547
REMARK 610 OLC A 548
REMARK 610 OLC A 549
REMARK 610 OLC A 550
REMARK 610 OLC A 551
REMARK 610 OLC A 552
REMARK 610 OLC A 553
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 34 O
REMARK 620 2 HOH A 642 O 89.6
REMARK 620 3 HOH A 678 O 95.3 81.0
REMARK 620 4 HOH A 699 O 81.7 64.3 145.2
REMARK 620 5 HOH A 724 O 87.4 128.7 150.2 64.6
REMARK 620 6 HOH A 725 O 91.7 146.5 65.5 148.8 84.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 74 OE2
REMARK 620 2 ASP A 77 OD1 93.8
REMARK 620 3 ASP A 77 OD2 94.7 53.5
REMARK 620 4 HOH A 673 O 143.9 117.2 90.1
REMARK 620 5 HOH A 682 O 71.8 129.4 78.9 74.1
REMARK 620 6 HOH A 689 O 89.7 75.9 129.3 114.3 148.4
REMARK 620 7 HOH A 712 O 92.0 155.4 149.6 67.8 75.1 80.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 511 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 74 OE1
REMARK 620 2 GLU A 74 OE2 49.3
REMARK 620 3 1PE A 514 OH7 49.0 62.3
REMARK 620 4 HOH A 606 O 47.7 62.5 1.6
REMARK 620 5 HOH A 634 O 48.3 63.3 1.7 0.8
REMARK 620 6 HOH A 699 O 46.0 61.8 3.3 1.8 2.4
REMARK 620 7 HOH A 719 O 49.5 65.2 3.0 2.7 1.9 4.0
REMARK 620 8 HOH A 724 O 46.7 64.2 4.3 2.8 2.7 2.5 2.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 506 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 210 ND1
REMARK 620 2 HIS A 213 ND1 110.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 510 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 241 O
REMARK 620 2 HOH A 629 O 70.6
REMARK 620 3 HOH A 670 O 67.0 93.0
REMARK 620 4 HOH A 686 O 68.3 136.8 82.8
REMARK 620 5 HOH A 739 O 127.9 106.1 158.7 89.3
REMARK 620 6 HOH A 749 O 146.9 111.9 79.9 109.6 84.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 318 O
REMARK 620 2 OLC A 533 O25 134.4
REMARK 620 3 HOH A 625 O 100.8 86.3
REMARK 620 4 HOH A 655 O 67.1 69.4 82.5
REMARK 620 5 HOH A 702 O 77.3 148.3 88.7 140.8
REMARK 620 6 HOH A 730 O 141.2 84.4 76.7 147.4 64.0
REMARK 620 7 HOH A 732 O 91.9 92.4 163.6 112.3 83.9 86.9
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 529
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 541
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 542
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 553
DBREF 5T77 A 1 475 UNP B7IE18 B7IE18_THEAB 1 475
SEQRES 1 A 475 MET SER ILE LEU PHE SER SER ILE LEU PHE SER ILE ALA
SEQRES 2 A 475 THR PHE PHE SER ARG ILE LEU GLY LEU PHE ARG ASP VAL
SEQRES 3 A 475 LEU PHE ALA LYS TYR PHE GLY VAL SER TYR GLU LEU ASP
SEQRES 4 A 475 ALA TYR PHE ILE ALA ILE MET PHE PRO PHE PHE LEU ARG
SEQRES 5 A 475 LYS VAL PHE GLY GLU GLY ALA MET SER SER ALA PHE VAL
SEQRES 6 A 475 PRO LEU TYR SER GLU LYS SER GLY GLU GLU LYS ASP LYS
SEQRES 7 A 475 PHE LEU SER SER VAL ILE ASN GLY PHE SER LEU ILE ILE
SEQRES 8 A 475 LEU ALA LEU VAL ILE LEU SER TYR PHE PHE PRO GLU LEU
SEQRES 9 A 475 ILE ILE ASN LEU PHE GLY ALA GLY SER SER HIS GLU THR
SEQRES 10 A 475 LYS ILE LEU ALA LYS LYS LEU LEU LEU ILE THR SER PRO
SEQRES 11 A 475 SER ILE TYR PHE ILE PHE LEU TRP ALA ILE SER TYR SER
SEQRES 12 A 475 ILE LEU ASN THR ASN ASN LYS PHE PHE TRP PRO ALA LEU
SEQRES 13 A 475 THR PRO SER ILE SER ASN ILE THR ILE ILE ILE GLY THR
SEQRES 14 A 475 PHE LEU SER THR LYS TYR GLY ILE ILE SER PRO THR ILE
SEQRES 15 A 475 GLY PHE LEU ILE GLY SER ILE LEU MET PHE PHE SER ILE
SEQRES 16 A 475 ILE LYS SER ILE ILE LYS HIS LYS TYR TYR PHE THR ILE
SEQRES 17 A 475 LYS HIS PHE PRO HIS PHE LEU LYS LEU PHE PHE PRO THR
SEQRES 18 A 475 PHE MET THR MET VAL VAL SER GLN ILE ASN THR VAL VAL
SEQRES 19 A 475 ASP MET ASN VAL VAL SER PHE TYR ASP LYS GLY SER ILE
SEQRES 20 A 475 SER TYR LEU GLN TYR ALA SER ARG PHE TYR LEU LEU PRO
SEQRES 21 A 475 TYR GLY LEU PHE ALA VAL SER VAL SER THR VAL VAL LEU
SEQRES 22 A 475 SER LYS ILE SER ASN ASP ARG LYS ASN PHE ASN TYR HIS
SEQRES 23 A 475 LEU ASN ASP ALA LEU LYS THR THR LEU PHE PHE THR ILE
SEQRES 24 A 475 PRO SER MET VAL GLY LEU ILE PHE LEU SER THR PRO ILE
SEQRES 25 A 475 ILE ARG PHE PHE TYR GLU HIS GLY ALA PHE THR SER LYS
SEQRES 26 A 475 ASP THR LEU ILE THR SER LYS ILE LEU ILE ALA TYR THR
SEQRES 27 A 475 LEU GLY LEU PRO PHE TYR GLY ILE TYR SER THR ILE SER
SEQRES 28 A 475 ARG SER TYR HIS ALA ILE LYS ASN THR LYS THR PRO PHE
SEQRES 29 A 475 ILE ALA ALA THR ILE VAL SER LEU SER ASN ILE ILE LEU
SEQRES 30 A 475 ASP ILE ILE PHE GLY LEU LYS TYR GLY PRO ILE GLY VAL
SEQRES 31 A 475 ALA LEU ALA THR SER ILE ALA GLY ILE ILE GLY VAL LEU
SEQRES 32 A 475 TYR LEU LEU PHE SER VAL LYS THR PHE PRO ILE LYS ASP
SEQRES 33 A 475 PHE LEU LYS ILE SER LEU ASN SER LEU ILE MET LEU PHE
SEQRES 34 A 475 VAL ILE TYR LEU THR ASP PHE THR ASP ASN GLU PHE TRP
SEQRES 35 A 475 PHE LEU ILE GLN ILE LEU ILE GLY ILE LEU VAL TYR LEU
SEQRES 36 A 475 ILE PHE SER SER ILE PHE TYR ARG ASP LEU ILE ARG ARG
SEQRES 37 A 475 PHE LEU TYR ALA ARG LYS LYS
HET CL A 501 1
HET CL A 502 1
HET CL A 503 1
HET CL A 504 1
HET CL A 505 1
HET ZN A 506 1
HET CA A 507 1
HET CA A 508 1
HET CA A 509 1
HET NA A 510 1
HET NA A 511 1
HET 1PE A 512 38
HET 1PE A 513 38
HET 1PE A 514 37
HET OLB A 515 28
HET OLB A 516 65
HET OLB A 517 53
HET OLB A 518 28
HET OLB A 519 29
HET OLB A 520 37
HET OLB A 521 30
HET OLC A 522 65
HET OLC A 523 31
HET OLC A 524 16
HET OLC A 525 37
HET OLC A 526 11
HET OLC A 527 34
HET OLC A 528 65
HET OLC A 529 53
HET OLC A 530 38
HET OLC A 531 17
HET OLC A 532 27
HET OLC A 533 55
HET OLC A 534 11
HET OLC A 535 17
HET OLC A 536 22
HET OLC A 537 10
HET OLC A 538 13
HET OLC A 539 13
HET OLC A 540 13
HET OLC A 541 13
HET OLC A 542 13
HET OLC A 543 8
HET OLC A 544 8
HET OLC A 545 41
HET OLC A 546 11
HET OLC A 547 11
HET OLC A 548 22
HET OLC A 549 37
HET OLC A 550 31
HET OLC A 551 14
HET OLC A 552 15
HET OLC A 553 25
HETNAM CL CHLORIDE ION
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN 1PE PEG400
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 CL 5(CL 1-)
FORMUL 7 ZN ZN 2+
FORMUL 8 CA 3(CA 2+)
FORMUL 11 NA 2(NA 1+)
FORMUL 13 1PE 3(C10 H22 O6)
FORMUL 16 OLB 7(C21 H40 O4)
FORMUL 23 OLC 32(C21 H40 O4)
FORMUL 55 HOH *149(H2 O)
HELIX 1 AA1 LEU A 4 PHE A 32 1 29
HELIX 2 AA2 SER A 35 GLU A 57 1 23
HELIX 3 AA3 MET A 60 GLU A 70 1 11
HELIX 4 AA4 SER A 72 PHE A 101 1 30
HELIX 5 AA5 PRO A 102 ALA A 111 1 10
HELIX 6 AA6 SER A 114 SER A 129 1 16
HELIX 7 AA7 PRO A 130 ASN A 148 1 19
HELIX 8 AA8 PHE A 151 THR A 157 1 7
HELIX 9 AA9 THR A 157 LEU A 171 1 15
HELIX 10 AB1 LEU A 171 GLY A 176 1 6
HELIX 11 AB2 ILE A 177 SER A 194 1 18
HELIX 12 AB3 ILE A 196 LYS A 201 1 6
HELIX 13 AB4 HIS A 210 GLN A 229 1 20
HELIX 14 AB5 ILE A 230 PHE A 241 1 12
HELIX 15 AB6 GLY A 245 ALA A 265 1 21
HELIX 16 AB7 VAL A 266 VAL A 268 5 3
HELIX 17 AB8 SER A 269 ASP A 279 1 11
HELIX 18 AB9 ASN A 282 LEU A 308 1 27
HELIX 19 AC1 LEU A 308 GLU A 318 1 11
HELIX 20 AC2 THR A 323 LEU A 339 1 17
HELIX 21 AC3 GLY A 340 ILE A 357 1 18
HELIX 22 AC4 THR A 360 GLY A 386 1 27
HELIX 23 AC5 GLY A 386 LYS A 410 1 25
HELIX 24 AC6 PRO A 413 THR A 434 1 22
HELIX 25 AC7 PHE A 441 TYR A 462 1 22
HELIX 26 AC8 TYR A 462 LEU A 470 1 9
LINK O VAL A 34 CA CA A 508 1555 1555 2.23
LINK OE2AGLU A 74 CA CA A 507 1555 1555 2.45
LINK OE1BGLU A 74 NA NA A 511 1555 4949 2.75
LINK OE2BGLU A 74 NA NA A 511 1555 4949 2.48
LINK OD1 ASP A 77 CA CA A 507 1555 1555 2.48
LINK OD2 ASP A 77 CA CA A 507 1555 1555 2.39
LINK ND1 HIS A 210 ZN ZN A 506 1555 1555 2.03
LINK ND1 HIS A 213 ZN ZN A 506 1555 1555 2.04
LINK O PHE A 241 NA NA A 510 1555 1555 2.69
LINK O GLU A 318 CA CA A 509 1555 1555 2.42
LINK CA CA A 507 O HOH A 673 1555 1555 2.48
LINK CA CA A 507 O HOH A 682 1555 1555 2.41
LINK CA CA A 507 O HOH A 689 1555 1555 2.44
LINK CA CA A 507 O HOH A 712 1555 4949 2.47
LINK CA CA A 508 O HOH A 642 1555 1555 2.47
LINK CA CA A 508 O HOH A 678 1555 1555 2.51
LINK CA CA A 508 O HOH A 699 1555 1555 2.58
LINK CA CA A 508 O HOH A 724 1555 1555 2.53
LINK CA CA A 508 O HOH A 725 1555 1555 2.38
LINK CA CA A 509 O25 OLC A 533 1555 1555 2.46
LINK CA CA A 509 O HOH A 625 1555 1555 2.43
LINK CA CA A 509 O HOH A 655 1555 1555 2.50
LINK CA CA A 509 O HOH A 702 1555 1555 2.33
LINK CA CA A 509 O HOH A 730 1555 1555 2.52
LINK CA CA A 509 O HOH A 732 1555 1555 2.43
LINK NA NA A 510 O HOH A 629 1555 1555 2.39
LINK NA NA A 510 O HOH A 670 1555 1555 2.33
LINK NA NA A 510 O HOH A 686 1555 1555 2.38
LINK NA NA A 510 O HOH A 739 1555 1555 2.39
LINK NA NA A 510 O HOH A 749 1555 1555 2.43
LINK NA NA A 511 OH7 1PE A 514 1555 1555 2.33
LINK NA NA A 511 O HOH A 606 1555 1555 2.36
LINK NA NA A 511 O HOH A 634 1555 1555 2.55
LINK NA NA A 511 O HOH A 699 1555 1555 2.64
LINK NA NA A 511 O HOH A 719 1555 4959 2.50
LINK NA NA A 511 O HOH A 724 1555 1555 2.48
SITE 1 AC1 2 TYR A 41 ARG A 255
SITE 1 AC2 5 LYS A 71 PHE A 79 HIS A 210 HIS A 213
SITE 2 AC2 5 ZN A 506
SITE 1 AC3 3 HIS A 210 HIS A 213 ZN A 506
SITE 1 AC4 2 SER A 72 GLY A 73
SITE 1 AC5 3 SER A 35 TYR A 36 LYS A 244
SITE 1 AC6 4 HIS A 210 HIS A 213 CL A 502 CL A 503
SITE 1 AC7 5 GLU A 74 ASP A 77 HOH A 673 HOH A 682
SITE 2 AC7 5 HOH A 689
SITE 1 AC8 6 VAL A 34 HOH A 642 HOH A 678 HOH A 699
SITE 2 AC8 6 HOH A 724 HOH A 725
SITE 1 AC9 7 GLU A 318 OLC A 533 HOH A 625 HOH A 655
SITE 2 AC9 7 HOH A 702 HOH A 730 HOH A 732
SITE 1 AD1 7 PHE A 241 TYR A 242 HOH A 629 HOH A 670
SITE 2 AD1 7 HOH A 686 HOH A 739 HOH A 749
SITE 1 AD2 5 1PE A 514 HOH A 606 HOH A 634 HOH A 699
SITE 2 AD2 5 HOH A 724
SITE 1 AD3 6 TYR A 285 ASN A 288 ASP A 289 LYS A 292
SITE 2 AD3 6 ASP A 416 HOH A 728
SITE 1 AD4 7 LYS A 30 TYR A 31 PHE A 170 HIS A 319
SITE 2 AD4 7 GLY A 320 1PE A 514 HOH A 732
SITE 1 AD5 6 LYS A 30 ALA A 321 NA A 511 1PE A 513
SITE 2 AD5 6 HOH A 606 HOH A 656
SITE 1 AD6 5 ASN A 107 ALA A 111 VAL A 233 ASN A 237
SITE 2 AD6 5 OLB A 518
SITE 1 AD7 2 ILE A 199 HOH A 671
SITE 1 AD8 6 PHE A 343 ILE A 346 THR A 411 PHE A 412
SITE 2 AD8 6 PHE A 417 OLC A 545
SITE 1 AD9 4 ASN A 237 PHE A 241 OLB A 515 HOH A 611
SITE 1 AE1 2 LEU A 126 OLC A 532
SITE 1 AE2 6 ASP A 289 LYS A 292 THR A 293 PHE A 296
SITE 2 AE2 6 TYR A 462 OLC A 551
SITE 1 AE3 3 SER A 301 OLC A 547 OLC A 551
SITE 1 AE4 3 LEU A 94 PHE A 218 PHE A 219
SITE 1 AE5 3 PHE A 206 THR A 207 ILE A 208
SITE 1 AE6 5 TYR A 99 PHE A 100 PHE A 101 GLU A 103
SITE 2 AE6 5 LYS A 122
SITE 1 AE7 5 ILE A 167 TYR A 175 SER A 179 ILE A 182
SITE 2 AE7 5 HOH A 604
SITE 1 AE8 6 TRP A 153 PRO A 154 THR A 157 SER A 194
SITE 2 AE8 6 ILE A 195 HOH A 706
SITE 1 AE9 5 THR A 437 ASN A 439 TRP A 442 ILE A 445
SITE 2 AE9 5 LEU A 448
SITE 1 AF1 2 THR A 360 OLC A 541
SITE 1 AF2 7 THR A 224 PHE A 364 ALA A 367 THR A 368
SITE 2 AF2 7 SER A 371 LEU A 372 HOH A 617
SITE 1 AF3 2 TYR A 385 LEU A 392
SITE 1 AF4 2 OLB A 519 HOH A 604
SITE 1 AF5 7 ILE A 19 PHE A 315 PHE A 316 HIS A 319
SITE 2 AF5 7 GLU A 440 CA A 509 HOH A 655
SITE 1 AF6 1 ILE A 186
SITE 1 AF7 2 LYS A 332 LEU A 392
SITE 1 AF8 1 PHE A 23
SITE 1 AF9 2 TYR A 204 HOH A 711
SITE 1 AG1 1 THR A 224
SITE 1 AG2 1 OLC A 529
SITE 1 AG3 1 OLC A 552
SITE 1 AG4 1 TYR A 99
SITE 1 AG5 4 ILE A 306 ILE A 335 PHE A 343 OLB A 517
SITE 1 AG6 1 OLB A 521
SITE 1 AG7 1 PHE A 206
SITE 1 AG8 2 SER A 408 OLC A 552
SITE 1 AG9 3 OLB A 520 OLB A 521 OLC A 553
SITE 1 AH1 4 ILE A 369 TYR A 404 OLC A 542 OLC A 550
SITE 1 AH2 3 VAL A 268 VAL A 271 OLC A 551
CRYST1 94.163 99.573 74.660 90.00 112.91 90.00 C 1 2 1 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 0.010620 0.000000 0.004488 0.00000
SCALE2 0.000000 0.010043 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014541 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
