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2qmt.pdb
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HEADER IMMUNE SYSTEM 16-JUL-07 2QMT
TITLE CRYSTAL POLYMORPHISM OF PROTEIN GB1 EXAMINED BY SOLID-STATE
TITLE 2 NMR AND X-RAY DIFFRACTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN G-BINDING PROTEIN G;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IMMUNOGLOBULIN BETA 1 BINDING DOMAIN (RESIDUES
COMPND 5 303-357);
COMPND 6 SYNONYM: IGG-BINDING PROTEIN G;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: SPG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 OTHER_DETAILS: SYNTHESIZED PLASMID, PREPARED ACCORDING TO
SOURCE 10 SMITH, C., WITHKA, J., AND REGAN, L. BIOCHEMISTRY 1994, 33,
SOURCE 11 5510-5517, EXPRESSING PROTEIN IDENTICAL IN SEQUENCE AND
SOURCE 12 STRUCTURE TO THE IGG BETA 1 BINDING DOMAIN OF PROTEIN G OF
SOURCE 13 STREPTOCOCCUS AREUS
KEYWDS IMMUNGLOBULIN BINDING DOMAIN, THERMOSTABLE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR H.L.FRERICKS SCHMIDT,L.J.SPERLING,Y.G.GAO,B.J.WYLIE,
AUTHOR 2 J.M.BOETTCHER,S.R.WILSON,C.M.RIENSTRA
REVDAT 3 24-FEB-09 2QMT 1 VERSN
REVDAT 2 15-JAN-08 2QMT 1 AUTHOR JRNL
REVDAT 1 25-DEC-07 2QMT 0
JRNL AUTH H.L.FRERICKS SCHMIDT,L.J.SPERLING,Y.G.GAO,
JRNL AUTH 2 B.J.WYLIE,J.M.BOETTCHER,S.R.WILSON,C.M.RIENSTRA
JRNL TITL CRYSTAL POLYMORPHISM OF PROTEIN GB1 EXAMINED BY
JRNL TITL 2 SOLID-STATE NMR SPECTROSCOPY AND X-RAY DIFFRACTION.
JRNL REF J.PHYS.CHEM.B V. 111 14362 2007
JRNL REFN ISSN 1089-5647
JRNL PMID 18052145
JRNL DOI 10.1021/JP075531P
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.185
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.185
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1159
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 23753
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 438
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 ANGLE DISTANCES (A) : 2.396
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QMT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-07.
REMARK 100 THE RCSB ID CODE IS RCSB043795.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25051
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.050
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 (%) : 94.5
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.23800
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1PGA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM NACL, 50% MPD, 6% IPA, 25 MM
REMARK 280 ACETATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.40000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.20000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 25.20000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 50.40000
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1080 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1090 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLN A 2 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 GLU A 19 OE1 - CD - OE2 ANGL. DEV. = 9.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 101
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 102
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 203
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GI9 RELATED DB: PDB
REMARK 900 ORTHORHOMBIC SINGLE CRYSTAL STRUCTURE OF GB1 - 1.14
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 15156 RELATED DB: BMRB
REMARK 900 SOLID-STATE NMR CHEMICAL SHIFT ASSIGNMENTS OF GB1
REMARK 900 RELATED ID: 2JSV RELATED DB: PDB
REMARK 900 ENSEMBLE OF SOLID-STATE NMR STRUCTURES OF GB1
REMARK 900 RELATED ID: 1PGA RELATED DB: PDB
REMARK 900 ALTERNATIVE ORTHORHOMBIC SINGLE CRYSTAL STRUCTURE OF GB1
REMARK 900 RELATED ID: 1PGB RELATED DB: PDB
REMARK 900 ALTERNATIVE TRIGONAL SINGLE CRYSTAL STRUCTURE OF GB1
REMARK 900 RELATED ID: 2GB1 RELATED DB: PDB
REMARK 900 AVERAGE SOLUTION NMR STRUCTURE OF GB1
DBREF 2QMT A 2 56 UNP P19909 SPG2_STRSG 303 357
SEQADV 2QMT MET A 1 UNP P19909 INITIATING METHIONINE
SEQADV 2QMT GLN A 2 UNP P19909 THR 303 ENGINEERED
SEQRES 1 A 56 MET GLN TYR LYS LEU ILE LEU ASN GLY LYS THR LEU LYS
SEQRES 2 A 56 GLY GLU THR THR THR GLU ALA VAL ASP ALA ALA THR ALA
SEQRES 3 A 56 GLU LYS VAL PHE LYS GLN TYR ALA ASN ASP ASN GLY VAL
SEQRES 4 A 56 ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS THR PHE
SEQRES 5 A 56 THR VAL THR GLU
HET PO4 A 101 5
HET MRD A 102 8
HET IPA A 203 4
HET IPA A 204 4
HETNAM PO4 PHOSPHATE ION
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 2 PO4 O4 P 3-
FORMUL 3 MRD C6 H14 O2
FORMUL 4 IPA 2(C3 H8 O)
FORMUL 6 HOH *135(H2 O)
HELIX 1 1 ASP A 22 ASN A 37 1 16
SHEET 1 A 4 LYS A 13 GLU A 19 0
SHEET 2 A 4 GLN A 2 ASN A 8 -1 N LEU A 5 O THR A 16
SHEET 3 A 4 THR A 51 THR A 55 1 O PHE A 52 N LYS A 4
SHEET 4 A 4 GLU A 42 ASP A 46 -1 N GLU A 42 O THR A 55
SITE 1 AC1 8 TYR A 3 ASP A 22 ALA A 23 ASP A 47
SITE 2 AC1 8 LYS A 50 HOH A1058 HOH A1073 HOH A1077
SITE 1 AC2 7 ALA A 20 VAL A 21 GLU A 27 LYS A 31
SITE 2 AC2 7 TRP A 43 HOH A1021 HOH A1089
SITE 1 AC3 5 ALA A 24 GLU A 27 TYR A 45 PHE A 52
SITE 2 AC3 5 HOH A1030
SITE 1 AC4 4 ASN A 8 THR A 55 HOH A1094 HOH A1147
CRYST1 35.730 35.730 75.600 90.00 90.00 120.00 P 32 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.027988 0.016159 0.000000 0.00000
SCALE2 0.000000 0.032317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013228 0.00000
ATOM 1 N MET A 1 -0.289 27.922 25.680 1.00 10.61 N
ATOM 2 CA MET A 1 0.136 28.162 24.322 1.00 10.12 C
ATOM 3 C MET A 1 -0.375 27.076 23.367 1.00 8.57 C
ATOM 4 O MET A 1 -0.458 25.943 23.800 1.00 9.29 O
ATOM 5 CB MET A 1 1.648 28.265 24.266 1.00 11.78 C
ATOM 6 CG MET A 1 2.082 28.903 22.922 1.00 14.19 C
ATOM 7 SD MET A 1 3.858 29.332 22.996 1.00 15.49 S
ATOM 8 CE MET A 1 3.740 30.671 24.161 1.00 13.45 C
ATOM 9 N GLN A 2 -0.638 27.472 22.156 1.00 9.84 N
ATOM 10 CA GLN A 2 -1.050 26.463 21.142 1.00 9.06 C
ATOM 11 C GLN A 2 0.204 25.807 20.563 1.00 8.63 C
ATOM 12 O GLN A 2 1.139 26.453 20.198 1.00 10.75 O
ATOM 13 CB GLN A 2 -1.822 27.060 20.035 1.00 10.21 C
ATOM 14 CG GLN A 2 -3.119 27.748 20.090 1.00 18.67 C
ATOM 15 CD GLN A 2 -3.792 27.664 18.717 1.00 29.22 C
ATOM 16 OE1 GLN A 2 -3.157 27.837 17.673 1.00 58.36 O
ATOM 17 NE2 GLN A 2 -5.071 27.345 18.734 1.00 33.90 N
ATOM 18 N TYR A 3 0.190 24.479 20.503 1.00 8.48 N
ATOM 19 CA TYR A 3 1.163 23.650 19.850 1.00 7.99 C
ATOM 20 C TYR A 3 0.455 22.830 18.776 1.00 8.26 C
ATOM 21 O TYR A 3 -0.695 22.426 18.960 1.00 9.29 O
ATOM 22 CB TYR A 3 1.863 22.689 20.833 1.00 8.67 C
ATOM 23 CG TYR A 3 2.705 23.479 21.836 1.00 8.21 C
ATOM 24 CD1 TYR A 3 4.036 23.761 21.653 1.00 8.04 C
ATOM 25 CD2 TYR A 3 2.074 23.976 22.999 1.00 8.39 C
ATOM 26 CE1 TYR A 3 4.788 24.489 22.574 1.00 9.04 C
ATOM 27 CE2 TYR A 3 2.795 24.729 23.930 1.00 10.03 C
ATOM 28 CZ TYR A 3 4.126 24.965 23.699 1.00 8.52 C
ATOM 29 OH TYR A 3 4.840 25.729 24.629 1.00 9.84 O
ATOM 30 N LYS A 4 1.131 22.569 17.703 1.00 7.91 N
ATOM 31 CA LYS A 4 0.570 21.841 16.579 1.00 8.50 C
ATOM 32 C LYS A 4 1.314 20.545 16.318 1.00 7.07 C
ATOM 33 O LYS A 4 2.553 20.496 16.508 1.00 9.00 O
ATOM 34 CB LYS A 4 0.673 22.688 15.340 1.00 10.34 C
ATOM 35 CG LYS A 4 -0.026 22.105 14.107 1.00 13.50 C
ATOM 36 CD LYS A 4 0.070 23.183 13.026 1.00 19.61 C
ATOM 37 CE LYS A 4 -0.623 22.735 11.769 1.00 27.51 C
ATOM 38 NZ LYS A 4 -0.698 23.808 10.722 1.00 28.10 N
ATOM 39 N LEU A 5 0.594 19.513 15.914 1.00 8.02 N
ATOM 40 CA LEU A 5 1.145 18.240 15.473 1.00 8.08 C
ATOM 41 C LEU A 5 0.770 17.998 14.041 1.00 8.20 C
ATOM 42 O LEU A 5 -0.423 18.004 13.693 1.00 8.86 O
ATOM 43 CB LEU A 5 0.631 17.102 16.363 1.00 8.81 C
ATOM 44 CG LEU A 5 1.048 15.695 15.925 1.00 8.73 C
ATOM 45 CD1 LEU A 5 2.520 15.444 16.110 1.00 9.45 C
ATOM 46 CD2 LEU A 5 0.271 14.663 16.737 1.00 11.26 C
ATOM 47 N ILE A 6 1.773 17.751 13.219 1.00 7.90 N
ATOM 48 CA ILE A 6 1.583 17.293 11.835 1.00 8.38 C
ATOM 49 C ILE A 6 1.758 15.784 11.827 1.00 8.27 C
ATOM 50 O ILE A 6 2.818 15.245 12.217 1.00 9.05 O
ATOM 51 CB ILE A 6 2.577 17.940 10.872 1.00 10.06 C
ATOM 52 CG1 ILE A 6 2.605 19.451 10.945 1.00 15.40 C
ATOM 53 CG2 ILE A 6 2.310 17.481 9.446 1.00 11.81 C
ATOM 54 CD1 ILE A 6 3.526 20.273 10.140 1.00 22.44 C
ATOM 55 N LEU A 7 0.712 15.097 11.383 1.00 9.47 N
ATOM 56 CA LEU A 7 0.641 13.649 11.297 1.00 9.93 C
ATOM 57 C LEU A 7 0.950 13.162 9.887 1.00 8.37 C
ATOM 58 O LEU A 7 0.232 13.522 8.966 1.00 9.38 O
ATOM 59 CB LEU A 7 -0.764 13.183 11.699 1.00 12.24 C
ATOM 60 CG LEU A 7 -1.154 13.406 13.170 1.00 13.45 C
ATOM 61 CD1 LEU A 7 -2.683 13.566 13.317 1.00 15.32 C
ATOM 62 CD2 LEU A 7 -0.733 12.241 14.021 1.00 14.68 C
ATOM 63 N ASN A 8 1.959 12.347 9.773 1.00 9.58 N
ATOM 64 CA ASN A 8 2.270 11.691 8.501 1.00 10.18 C
ATOM 65 C ASN A 8 2.483 10.216 8.793 1.00 10.58 C
ATOM 66 O ASN A 8 3.539 9.620 8.552 1.00 11.56 O
ATOM 67 CB ASN A 8 3.425 12.342 7.812 1.00 12.04 C
ATOM 68 CG ASN A 8 3.605 11.891 6.385 1.00 16.50 C
ATOM 69 OD1 ASN A 8 2.714 11.267 5.803 1.00 17.85 O
ATOM 70 ND2 ASN A 8 4.750 12.237 5.796 1.00 17.23 N
ATOM 71 N GLY A 9 1.489 9.590 9.345 1.00 11.35 N
ATOM 72 CA GLY A 9 1.491 8.159 9.547 1.00 12.49 C
ATOM 73 C GLY A 9 1.187 7.420 8.258 1.00 11.24 C
ATOM 74 O GLY A 9 0.793 7.981 7.268 1.00 13.40 O
ATOM 75 N LYS A 10 1.352 6.076 8.344 1.00 13.09 N
ATOM 76 CA LYS A 10 0.999 5.235 7.211 1.00 14.12 C
ATOM 77 C LYS A 10 -0.453 5.393 6.816 1.00 12.88 C
ATOM 78 O LYS A 10 -0.721 5.484 5.611 1.00 14.06 O
ATOM 79 CB LYS A 10 1.344 3.779 7.566 1.00 18.77 C
ATOM 80 CG LYS A 10 2.844 3.467 7.493 1.00 22.82 C
ATOM 81 CD LYS A 10 3.102 1.982 7.713 1.00 32.27 C
ATOM 82 CE LYS A 10 4.445 1.728 8.382 1.00 48.44 C
ATOM 83 NZ LYS A 10 4.332 1.406 9.840 1.00 40.39 N
ATOM 84 N THR A 11 -1.317 5.449 7.847 1.00 10.62 N
ATOM 85 CA THR A 11 -2.725 5.685 7.473 1.00 11.54 C
ATOM 86 C THR A 11 -3.311 6.905 8.125 1.00 10.95 C
ATOM 87 O THR A 11 -4.329 7.388 7.568 1.00 11.88 O
ATOM 88 CB THR A 11 -3.309 4.313 7.835 1.00 17.95 C
ATOM 89 OG1 THR A 11 -4.419 4.029 7.011 1.00 55.03 O
ATOM 90 CG2 THR A 11 -3.557 4.293 9.311 1.00 12.41 C
ATOM 91 N LEU A 12 -2.768 7.424 9.235 1.00 9.70 N
ATOM 92 CA LEU A 12 -3.308 8.605 9.907 1.00 10.14 C
ATOM 93 C LEU A 12 -2.514 9.808 9.480 1.00 9.11 C
ATOM 94 O LEU A 12 -1.277 9.897 9.729 1.00 9.90 O
ATOM 95 CB LEU A 12 -3.318 8.403 11.421 1.00 10.36 C
ATOM 96 CG LEU A 12 -4.355 8.957 12.392 1.00 37.35 C
ATOM 97 CD1 LEU A 12 -3.740 9.324 13.769 1.00 11.71 C
ATOM 98 CD2 LEU A 12 -5.176 10.147 11.886 1.00 10.26 C
ATOM 99 N LYS A 13 -3.160 10.771 8.829 1.00 8.48 N
ATOM 100 CA LYS A 13 -2.524 11.968 8.335 1.00 8.93 C
ATOM 101 C LYS A 13 -3.359 13.197 8.713 1.00 8.01 C
ATOM 102 O LYS A 13 -4.557 13.126 8.872 1.00 8.96 O
ATOM 103 CB LYS A 13 -2.342 11.894 6.806 1.00 11.50 C
ATOM 104 CG LYS A 13 -1.388 10.715 6.398 1.00 11.64 C
ATOM 105 CD LYS A 13 -1.247 10.705 4.874 1.00 15.75 C
ATOM 106 CE LYS A 13 -0.479 9.499 4.377 1.00 17.84 C
ATOM 107 NZ LYS A 13 0.874 9.263 4.855 1.00 22.26 N
ATOM 108 N GLY A 14 -2.708 14.353 8.755 1.00 8.96 N
ATOM 109 CA GLY A 14 -3.380 15.633 8.958 1.00 9.02 C
ATOM 110 C GLY A 14 -2.712 16.433 10.040 1.00 8.43 C
ATOM 111 O GLY A 14 -1.453 16.398 10.202 1.00 10.14 O
ATOM 112 N GLU A 15 -3.505 17.202 10.800 1.00 7.81 N
ATOM 113 CA GLU A 15 -2.984 18.079 11.801 1.00 9.09 C
ATOM 114 C GLU A 15 -3.885 18.174 12.982 1.00 8.81 C
ATOM 115 O GLU A 15 -5.128 18.097 12.823 1.00 9.85 O
ATOM 116 CB GLU A 15 -2.940 19.514 11.261 1.00 13.63 C
ATOM 117 CG GLU A 15 -2.142 19.701 10.019 1.00 14.22 C
ATOM 118 CD GLU A 15 -2.242 21.078 9.447 1.00 15.75 C
ATOM 119 OE1 GLU A 15 -3.223 21.791 9.747 1.00 16.96 O
ATOM 120 OE2 GLU A 15 -1.275 21.408 8.738 1.00 18.94 O
ATOM 121 N THR A 16 -3.296 18.381 14.141 1.00 8.84 N
ATOM 122 CA THR A 16 -4.107 18.650 15.327 1.00 10.66 C
ATOM 123 C THR A 16 -3.364 19.659 16.172 1.00 9.91 C
ATOM 124 O THR A 16 -2.157 19.807 16.065 1.00 12.31 O
ATOM 125 CB THR A 16 -4.318 17.344 16.069 1.00 11.88 C
ATOM 126 OG1 THR A 16 -4.824 16.281 15.259 1.00 33.58 O
ATOM 127 CG2 THR A 16 -5.384 17.587 17.109 1.00 11.50 C
ATOM 128 N THR A 17 -4.087 20.370 17.031 1.00 10.91 N
ATOM 129 CA THR A 17 -3.470 21.312 17.944 1.00 9.78 C
ATOM 130 C THR A 17 -3.873 21.027 19.373 1.00 10.55 C
ATOM 131 O THR A 17 -4.930 20.425 19.652 1.00 13.33 O
ATOM 132 CB THR A 17 -3.879 22.762 17.605 1.00 11.43 C
ATOM 133 OG1 THR A 17 -5.274 22.839 17.857 1.00 19.36 O
ATOM 134 CG2 THR A 17 -3.480 23.064 16.194 1.00 13.74 C
ATOM 135 N THR A 18 -3.047 21.477 20.307 1.00 8.97 N
ATOM 136 CA THR A 18 -3.378 21.360 21.736 1.00 9.80 C
ATOM 137 C THR A 18 -2.916 22.609 22.442 1.00 9.60 C
ATOM 138 O THR A 18 -1.973 23.255 22.049 1.00 10.41 O
ATOM 139 CB THR A 18 -2.786 20.086 22.354 1.00 11.04 C
ATOM 140 OG1 THR A 18 -3.513 19.733 23.539 1.00 13.32 O
ATOM 141 CG2 THR A 18 -1.318 20.269 22.743 1.00 11.14 C
ATOM 142 N GLU A 19 -3.629 22.957 23.497 1.00 9.41 N
ATOM 143 CA GLU A 19 -3.282 24.057 24.382 1.00 10.97 C
ATOM 144 C GLU A 19 -2.507 23.502 25.561 1.00 10.47 C
ATOM 145 O GLU A 19 -3.004 22.668 26.309 1.00 13.18 O
ATOM 146 CB GLU A 19 -4.524 24.792 24.845 1.00 11.22 C
ATOM 147 CG GLU A 19 -5.390 25.367 23.749 1.00 32.80 C
ATOM 148 CD GLU A 19 -4.579 26.325 22.878 1.00 45.01 C
ATOM 149 OE1 GLU A 19 -3.938 27.187 23.522 1.00 34.82 O
ATOM 150 OE2 GLU A 19 -4.685 26.080 21.654 1.00 31.86 O
ATOM 151 N ALA A 20 -1.268 23.960 25.761 1.00 9.29 N
ATOM 152 CA ALA A 20 -0.431 23.409 26.822 1.00 9.68 C
ATOM 153 C ALA A 20 0.412 24.511 27.464 1.00 9.12 C
ATOM 154 O ALA A 20 0.712 25.525 26.894 1.00 9.62 O
ATOM 155 CB ALA A 20 0.443 22.283 26.295 1.00 10.49 C
ATOM 156 N VAL A 21 0.810 24.202 28.706 1.00 9.32 N
ATOM 157 CA VAL A 21 1.614 25.198 29.434 1.00 9.56 C
ATOM 158 C VAL A 21 3.004 25.291 28.877 1.00 9.85 C
ATOM 159 O VAL A 21 3.657 26.341 29.071 1.00 10.68 O
ATOM 160 CB VAL A 21 1.731 24.861 30.928 1.00 9.62 C
ATOM 161 CG1 VAL A 21 0.375 25.055 31.629 1.00 12.25 C
ATOM 162 CG2 VAL A 21 2.204 23.446 31.190 1.00 11.24 C
ATOM 163 N ASP A 22 3.538 24.252 28.236 1.00 9.28 N
ATOM 164 CA ASP A 22 4.905 24.230 27.704 1.00 9.55 C
ATOM 165 C ASP A 22 5.018 23.099 26.698 1.00 8.59 C
ATOM 166 O ASP A 22 4.126 22.282 26.548 1.00 8.95 O
ATOM 167 CB ASP A 22 5.944 24.124 28.816 1.00 11.48 C
ATOM 168 CG ASP A 22 5.751 22.967 29.751 1.00 10.76 C
ATOM 169 OD1 ASP A 22 5.291 21.910 29.301 1.00 11.08 O
ATOM 170 OD2 ASP A 22 5.968 23.109 31.010 1.00 14.12 O
ATOM 171 N ALA A 23 6.148 23.132 25.999 1.00 8.75 N
ATOM 172 CA ALA A 23 6.354 22.187 24.881 1.00 9.81 C
ATOM 173 C ALA A 23 6.508 20.774 25.420 1.00 8.28 C
ATOM 174 O ALA A 23 6.048 19.787 24.815 1.00 8.91 O
ATOM 175 CB ALA A 23 7.547 22.553 24.049 1.00 10.93 C
ATOM 176 N ALA A 24 7.088 20.606 26.611 1.00 9.40 N
ATOM 177 CA ALA A 24 7.250 19.284 27.182 1.00 9.09 C
ATOM 178 C ALA A 24 5.908 18.639 27.466 1.00 9.72 C
ATOM 179 O ALA A 24 5.748 17.437 27.295 1.00 10.11 O
ATOM 180 CB ALA A 24 8.065 19.346 28.465 1.00 11.87 C
ATOM 181 N THR A 25 4.963 19.474 27.904 1.00 9.42 N
ATOM 182 CA THR A 25 3.643 18.953 28.170 1.00 10.78 C
ATOM 183 C THR A 25 2.899 18.608 26.869 1.00 9.10 C
ATOM 184 O THR A 25 2.260 17.546 26.780 1.00 10.20 O
ATOM 185 CB THR A 25 2.877 19.958 29.050 1.00 10.16 C
ATOM 186 OG1 THR A 25 3.619 20.129 30.269 1.00 11.80 O
ATOM 187 CG2 THR A 25 1.520 19.428 29.389 1.00 14.12 C
ATOM 188 N ALA A 26 3.020 19.508 25.897 1.00 9.20 N
ATOM 189 CA ALA A 26 2.417 19.199 24.588 1.00 8.86 C
ATOM 190 C ALA A 26 3.011 17.931 23.996 1.00 8.72 C
ATOM 191 O ALA A 26 2.281 17.133 23.382 1.00 8.95 O
ATOM 192 CB ALA A 26 2.620 20.392 23.660 1.00 9.69 C
ATOM 193 N GLU A 27 4.288 17.725 24.145 1.00 8.02 N
ATOM 194 CA GLU A 27 4.940 16.521 23.637 1.00 7.91 C
ATOM 195 C GLU A 27 4.301 15.273 24.221 1.00 8.21 C
ATOM 196 O GLU A 27 4.056 14.296 23.476 1.00 8.94 O
ATOM 197 CB GLU A 27 6.414 16.546 23.954 1.00 8.49 C
ATOM 198 CG GLU A 27 7.146 15.331 23.388 1.00 9.51 C
ATOM 199 CD GLU A 27 8.562 15.168 23.896 1.00 8.98 C
ATOM 200 OE1 GLU A 27 8.995 15.867 24.845 1.00 11.78 O
ATOM 201 OE2 GLU A 27 9.291 14.319 23.325 1.00 10.51 O
ATOM 202 N LYS A 28 4.045 15.261 25.480 1.00 9.00 N
ATOM 203 CA LYS A 28 3.415 14.121 26.146 1.00 9.54 C
ATOM 204 C LYS A 28 2.019 13.913 25.588 1.00 9.26 C
ATOM 205 O LYS A 28 1.598 12.778 25.324 1.00 10.48 O
ATOM 206 CB LYS A 28 3.378 14.287 27.658 1.00 11.87 C
ATOM 207 CG LYS A 28 4.762 14.210 28.271 1.00 13.89 C
ATOM 208 CD LYS A 28 4.788 14.696 29.721 1.00 19.80 C
ATOM 209 CE LYS A 28 6.057 14.285 30.451 1.00 26.33 C
ATOM 210 NZ LYS A 28 6.328 15.294 31.512 1.00 29.45 N
ATOM 211 N VAL A 29 1.237 14.967 25.426 1.00 9.41 N
ATOM 212 CA VAL A 29 -0.103 14.848 24.864 1.00 9.43 C
ATOM 213 C VAL A 29 -0.031 14.239 23.472 1.00 8.70 C
ATOM 214 O VAL A 29 -0.774 13.324 23.114 1.00 9.40 O
ATOM 215 CB VAL A 29 -0.784 16.224 24.831 1.00 10.49 C
ATOM 216 CG1 VAL A 29 -2.054 16.215 23.980 1.00 12.30 C
ATOM 217 CG2 VAL A 29 -1.115 16.713 26.242 1.00 11.96 C
ATOM 218 N PHE A 30 0.837 14.780 22.605 1.00 7.75 N
ATOM 219 CA PHE A 30 0.906 14.303 21.230 1.00 7.99 C
ATOM 220 C PHE A 30 1.435 12.894 21.130 1.00 8.00 C
ATOM 221 O PHE A 30 0.967 12.132 20.282 1.00 8.31 O
ATOM 222 CB PHE A 30 1.717 15.306 20.403 1.00 7.93 C
ATOM 223 CG PHE A 30 1.040 16.616 20.135 1.00 7.84 C
ATOM 224 CD1 PHE A 30 -0.327 16.742 19.931 1.00 8.02 C
ATOM 225 CD2 PHE A 30 1.775 17.785 20.058 1.00 8.45 C
ATOM 226 CE1 PHE A 30 -0.913 17.938 19.625 1.00 9.60 C
ATOM 227 CE2 PHE A 30 1.199 18.992 19.739 1.00 8.42 C
ATOM 228 CZ PHE A 30 -0.172 19.089 19.541 1.00 8.68 C
ATOM 229 N LYS A 31 2.438 12.552 21.911 1.00 8.51 N
ATOM 230 CA LYS A 31 2.985 11.186 21.837 1.00 8.92 C
ATOM 231 C LYS A 31 1.941 10.221 22.365 1.00 8.73 C
ATOM 232 O LYS A 31 1.810 9.138 21.817 1.00 9.59 O
ATOM 233 CB LYS A 31 4.312 11.061 22.564 1.00 10.21 C
ATOM 234 CG LYS A 31 5.400 11.668 21.703 1.00 10.56 C
ATOM 235 CD LYS A 31 6.764 11.593 22.313 1.00 12.07 C
ATOM 236 CE LYS A 31 7.831 11.834 21.243 1.00 13.98 C
ATOM 237 NZ LYS A 31 9.097 11.895 22.019 1.00 12.46 N
ATOM 238 N GLN A 32 1.172 10.586 23.377 1.00 8.53 N
ATOM 239 CA GLN A 32 0.097 9.686 23.810 1.00 9.75 C
ATOM 240 C GLN A 32 -0.943 9.525 22.738 1.00 9.82 C
ATOM 241 O GLN A 32 -1.414 8.406 22.460 1.00 10.62 O
ATOM 242 CB GLN A 32 -0.484 10.211 25.116 1.00 10.79 C
ATOM 243 CG GLN A 32 0.604 10.328 26.177 1.00 41.44 C
ATOM 244 CD GLN A 32 0.397 9.640 27.500 1.00 55.76 C
ATOM 245 OE1 GLN A 32 0.562 10.189 28.593 1.00 52.88 O
ATOM 246 NE2 GLN A 32 0.028 8.372 27.408 1.00 18.07 N
ATOM 247 N TYR A 33 -1.346 10.598 22.094 1.00 8.95 N
ATOM 248 CA TYR A 33 -2.324 10.581 21.019 1.00 10.03 C
ATOM 249 C TYR A 33 -1.813 9.700 19.877 1.00 8.94 C
ATOM 250 O TYR A 33 -2.563 8.818 19.328 1.00 9.78 O
ATOM 251 CB TYR A 33 -2.578 11.998 20.518 1.00 10.88 C
ATOM 252 CG TYR A 33 -3.345 12.042 19.218 1.00 12.02 C
ATOM 253 CD1 TYR A 33 -4.742 11.937 19.179 1.00 14.36 C
ATOM 254 CD2 TYR A 33 -2.682 12.211 17.995 1.00 13.51 C
ATOM 255 CE1 TYR A 33 -5.411 11.994 17.959 1.00 17.27 C
ATOM 256 CE2 TYR A 33 -3.338 12.253 16.814 1.00 15.81 C
ATOM 257 CZ TYR A 33 -4.705 12.144 16.793 1.00 14.45 C
ATOM 258 OH TYR A 33 -5.240 12.216 15.516 1.00 21.31 O
ATOM 259 N ALA A 34 -0.561 9.873 19.455 1.00 9.21 N
ATOM 260 CA ALA A 34 -0.022 9.057 18.368 1.00 9.87 C
ATOM 261 C ALA A 34 -0.028 7.594 18.794 1.00 9.37 C
ATOM 262 O ALA A 34 -0.462 6.729 17.993 1.00 12.12 O
ATOM 263 CB ALA A 34 1.378 9.529 18.011 1.00 11.37 C
ATOM 264 N ASN A 35 0.467 7.305 19.951 1.00 10.43 N
ATOM 265 CA ASN A 35 0.507 5.899 20.409 1.00 12.05 C
ATOM 266 C ASN A 35 -0.907 5.309 20.392 1.00 11.18 C
ATOM 267 O ASN A 35 -1.111 4.155 19.926 1.00 13.99 O
ATOM 268 CB ASN A 35 1.077 5.840 21.803 1.00 13.52 C
ATOM 269 CG ASN A 35 1.037 4.436 22.383 1.00 18.91 C
ATOM 270 OD1 ASN A 35 1.872 3.594 22.128 1.00 25.84 O
ATOM 271 ND2 ASN A 35 0.014 4.186 23.189 1.00 20.69 N
ATOM 272 N ASP A 36 -1.871 6.010 20.870 1.00 10.31 N
ATOM 273 CA ASP A 36 -3.230 5.482 21.007 1.00 11.92 C
ATOM 274 C ASP A 36 -3.854 5.244 19.646 1.00 11.25 C
ATOM 275 O ASP A 36 -4.830 4.462 19.495 1.00 13.70 O
ATOM 276 CB ASP A 36 -4.073 6.440 21.823 1.00 12.83 C
ATOM 277 CG ASP A 36 -3.649 6.507 23.275 1.00 11.14 C
ATOM 278 OD1 ASP A 36 -2.706 5.842 23.674 1.00 13.37 O
ATOM 279 OD2 ASP A 36 -4.329 7.289 23.937 1.00 12.73 O
ATOM 280 N ASN A 37 -3.394 5.927 18.613 1.00 10.77 N
ATOM 281 CA ASN A 37 -3.865 5.764 17.234 1.00 11.84 C
ATOM 282 C ASN A 37 -2.899 4.887 16.468 1.00 11.82 C
ATOM 283 O ASN A 37 -3.048 4.901 15.209 1.00 14.72 O
ATOM 284 CB ASN A 37 -4.031 7.130 16.564 1.00 14.75 C
ATOM 285 CG ASN A 37 -5.248 7.832 17.104 1.00 13.37 C
ATOM 286 OD1 ASN A 37 -6.349 7.592 16.551 1.00 20.38 O
ATOM 287 ND2 ASN A 37 -5.199 8.609 18.149 1.00 15.10 N
ATOM 288 N GLY A 38 -2.013 4.198 17.027 1.00 12.73 N
ATOM 289 CA GLY A 38 -1.181 3.219 16.365 1.00 16.83 C
ATOM 290 C GLY A 38 -0.094 3.809 15.512 1.00 14.99 C
ATOM 291 O GLY A 38 0.421 3.104 14.614 1.00 18.68 O
ATOM 292 N VAL A 39 0.273 5.060 15.743 1.00 12.44 N
ATOM 293 CA VAL A 39 1.350 5.659 14.992 1.00 11.49 C
ATOM 294 C VAL A 39 2.641 5.479 15.737 1.00 14.34 C
ATOM 295 O VAL A 39 2.711 6.000 16.883 1.00 20.70 O
ATOM 296 CB VAL A 39 1.081 7.162 14.774 1.00 12.68 C
ATOM 297 CG1 VAL A 39 2.188 7.826 13.982 1.00 13.81 C
ATOM 298 CG2 VAL A 39 -0.276 7.301 14.104 1.00 14.38 C
ATOM 299 N ASP A 40 3.612 4.858 15.149 1.00 13.94 N
ATOM 300 CA ASP A 40 4.924 4.584 15.677 1.00 12.82 C
ATOM 301 C ASP A 40 5.956 5.088 14.710 1.00 12.81 C
ATOM 302 O ASP A 40 6.308 4.446 13.730 1.00 15.64 O
ATOM 303 CB ASP A 40 5.078 3.048 15.831 1.00 18.47 C
ATOM 304 CG ASP A 40 6.377 2.610 16.468 1.00 25.87 C
ATOM 305 OD1 ASP A 40 7.168 3.451 16.939 1.00 25.26 O
ATOM 306 OD2 ASP A 40 6.589 1.376 16.532 1.00 35.95 O
ATOM 307 N GLY A 41 6.417 6.320 14.885 1.00 13.39 N
ATOM 308 CA GLY A 41 7.188 7.020 13.918 1.00 14.49 C
ATOM 309 C GLY A 41 8.360 7.853 14.450 1.00 11.67 C
ATOM 310 O GLY A 41 8.753 7.772 15.615 1.00 14.20 O
ATOM 311 N GLU A 42 8.929 8.590 13.581 1.00 9.76 N
ATOM 312 CA GLU A 42 10.036 9.521 13.915 1.00 9.51 C
ATOM 313 C GLU A 42 9.472 10.895 14.136 1.00 8.71 C
ATOM 314 O GLU A 42 8.535 11.338 13.445 1.00 9.76 O
ATOM 315 CB GLU A 42 11.055 9.533 12.799 1.00 11.95 C
ATOM 316 CG GLU A 42 11.911 8.277 12.752 1.00 16.87 C
ATOM 317 CD GLU A 42 12.142 7.537 14.036 1.00 44.20 C
ATOM 318 OE1 GLU A 42 12.648 8.120 15.017 1.00 44.56 O
ATOM 319 OE2 GLU A 42 11.822 6.323 14.108 1.00 73.11 O
ATOM 320 N TRP A 43 10.041 11.625 15.085 1.00 8.15 N
ATOM 321 CA TRP A 43 9.501 12.877 15.562 1.00 8.11 C
ATOM 322 C TRP A 43 10.476 14.031 15.337 1.00 6.86 C
ATOM 323 O TRP A 43 11.702 13.902 15.479 1.00 7.85 O
ATOM 324 CB TRP A 43 9.298 12.821 17.083 1.00 8.23 C
ATOM 325 CG TRP A 43 8.124 11.946 17.412 1.00 8.55 C
ATOM 326 CD1 TRP A 43 8.080 10.585 17.460 1.00 9.48 C
ATOM 327 CD2 TRP A 43 6.800 12.380 17.727 1.00 8.28 C
ATOM 328 NE1 TRP A 43 6.809 10.156 17.783 1.00 9.66 N
ATOM 329 CE2 TRP A 43 6.000 11.245 17.955 1.00 9.61 C
ATOM 330 CE3 TRP A 43 6.219 13.636 17.836 1.00 8.24 C
ATOM 331 CZ2 TRP A 43 4.648 11.310 18.276 1.00 9.38 C
ATOM 332 CZ3 TRP A 43 4.873 13.700 18.166 1.00 9.86 C
ATOM 333 CH2 TRP A 43 4.103 12.571 18.388 1.00 9.79 C
ATOM 334 N THR A 44 9.932 15.191 15.001 1.00 7.62 N
ATOM 335 CA THR A 44 10.632 16.462 15.102 1.00 7.91 C
ATOM 336 C THR A 44 9.809 17.445 15.958 1.00 8.00 C
ATOM 337 O THR A 44 8.580 17.300 16.123 1.00 8.42 O
ATOM 338 CB THR A 44 10.927 17.113 13.737 1.00 8.42 C
ATOM 339 OG1 THR A 44 9.713 17.594 13.124 1.00 10.51 O
ATOM 340 CG2 THR A 44 11.583 16.144 12.774 1.00 9.81 C
ATOM 341 N TYR A 45 10.496 18.477 16.424 1.00 8.11 N
ATOM 342 CA TYR A 45 9.864 19.584 17.121 1.00 8.47 C
ATOM 343 C TYR A 45 10.633 20.858 16.780 1.00 7.99 C
ATOM 344 O TYR A 45 11.873 20.879 16.849 1.00 8.92 O
ATOM 345 CB TYR A 45 9.821 19.412 18.653 1.00 7.74 C
ATOM 346 CG TYR A 45 9.300 20.662 19.313 1.00 8.25 C
ATOM 347 CD1 TYR A 45 8.034 21.097 19.120 1.00 8.78 C
ATOM 348 CD2 TYR A 45 10.128 21.393 20.162 1.00 8.86 C
ATOM 349 CE1 TYR A 45 7.532 22.228 19.719 1.00 8.76 C
ATOM 350 CE2 TYR A 45 9.646 22.554 20.744 1.00 9.88 C
ATOM 351 CZ TYR A 45 8.341 22.970 20.542 1.00 8.73 C
ATOM 352 OH TYR A 45 7.857 24.145 21.088 1.00 10.28 O
ATOM 353 N ASP A 46 9.924 21.907 16.387 1.00 8.43 N
ATOM 354 CA ASP A 46 10.550 23.179 16.164 1.00 9.28 C
ATOM 355 C ASP A 46 9.994 24.187 17.176 1.00 8.14 C
ATOM 356 O ASP A 46 8.837 24.535 17.165 1.00 9.90 O
ATOM 357 CB ASP A 46 10.322 23.700 14.746 1.00 12.53 C
ATOM 358 CG ASP A 46 11.330 24.788 14.418 1.00 15.36 C
ATOM 359 OD1 ASP A 46 11.848 25.471 15.326 1.00 18.76 O
ATOM 360 OD2 ASP A 46 11.676 24.917 13.210 1.00 19.11 O
ATOM 361 N ASP A 47 10.898 24.627 18.061 1.00 10.10 N
ATOM 362 CA ASP A 47 10.491 25.512 19.156 1.00 10.55 C
ATOM 363 C ASP A 47 10.139 26.905 18.660 1.00 12.08 C
ATOM 364 O ASP A 47 9.500 27.703 19.406 1.00 13.05 O
ATOM 365 CB ASP A 47 11.579 25.560 20.246 1.00 10.49 C
ATOM 366 CG ASP A 47 11.042 26.060 21.558 1.00 12.54 C
ATOM 367 OD1 ASP A 47 9.928 25.692 22.008 1.00 12.02 O
ATOM 368 OD2 ASP A 47 11.783 26.784 22.283 1.00 16.64 O
ATOM 369 N ALA A 48 10.524 27.276 17.481 1.00 11.68 N
ATOM 370 CA ALA A 48 10.222 28.606 16.961 1.00 14.06 C
ATOM 371 C ALA A 48 8.792 28.605 16.453 1.00 13.57 C
ATOM 372 O ALA A 48 8.115 29.656 16.558 1.00 16.40 O
ATOM 373 CB ALA A 48 11.194 29.016 15.851 1.00 15.91 C
ATOM 374 N THR A 49 8.303 27.512 15.865 1.00 11.98 N
ATOM 375 CA THR A 49 6.966 27.441 15.291 1.00 12.59 C
ATOM 376 C THR A 49 5.987 26.613 16.117 1.00 10.86 C
ATOM 377 O THR A 49 4.814 26.458 15.749 1.00 12.91 O
ATOM 378 CB THR A 49 7.024 26.849 13.866 1.00 14.30 C
ATOM 379 OG1 THR A 49 7.404 25.487 14.004 1.00 12.43 O
ATOM 380 CG2 THR A 49 8.063 27.555 13.030 1.00 15.92 C
ATOM 381 N LYS A 50 6.411 26.106 17.246 1.00 9.58 N
ATOM 382 CA LYS A 50 5.608 25.362 18.178 1.00 9.20 C
ATOM 383 C LYS A 50 4.963 24.182 17.491 1.00 8.62 C
ATOM 384 O LYS A 50 3.858 23.759 17.823 1.00 10.79 O
ATOM 385 CB LYS A 50 4.597 26.250 18.908 1.00 9.59 C
ATOM 386 CG LYS A 50 5.193 27.511 19.520 1.00 11.00 C
ATOM 387 CD LYS A 50 6.235 27.231 20.567 1.00 10.18 C
ATOM 388 CE LYS A 50 6.932 28.503 21.049 1.00 12.34 C
ATOM 389 NZ LYS A 50 8.019 28.098 21.971 1.00 12.61 N
ATOM 390 N THR A 51 5.690 23.549 16.562 1.00 8.74 N
ATOM 391 CA THR A 51 5.138 22.463 15.743 1.00 8.49 C
ATOM 392 C THR A 51 5.947 21.189 15.881 1.00 7.97 C
ATOM 393 O THR A 51 7.180 21.216 15.716 1.00 9.28 O
ATOM 394 CB THR A 51 5.127 22.930 14.273 1.00 9.29 C
ATOM 395 OG1 THR A 51 4.259 24.059 14.160 1.00 11.62 O
ATOM 396 CG2 THR A 51 4.532 21.861 13.371 1.00 11.45 C
ATOM 397 N PHE A 52 5.264 20.117 16.150 1.00 7.62 N
ATOM 398 CA PHE A 52 5.759 18.766 16.210 1.00 7.76 C
ATOM 399 C PHE A 52 5.376 18.050 14.901 1.00 7.80 C
ATOM 400 O PHE A 52 4.325 18.370 14.306 1.00 8.45 O
ATOM 401 CB PHE A 52 5.111 17.947 17.331 1.00 7.62 C
ATOM 402 CG PHE A 52 5.410 18.440 18.707 1.00 7.52 C
ATOM 403 CD1 PHE A 52 4.764 19.486 19.289 1.00 8.92 C
ATOM 404 CD2 PHE A 52 6.404 17.818 19.429 1.00 8.37 C
ATOM 405 CE1 PHE A 52 5.031 19.897 20.582 1.00 8.76 C
ATOM 406 CE2 PHE A 52 6.686 18.174 20.743 1.00 8.32 C
ATOM 407 CZ PHE A 52 6.000 19.254 21.324 1.00 7.98 C
ATOM 408 N THR A 53 6.176 17.096 14.478 1.00 7.68 N
ATOM 409 CA THR A 53 5.765 16.218 13.377 1.00 7.62 C
ATOM 410 C THR A 53 6.019 14.789 13.790 1.00 8.25 C
ATOM 411 O THR A 53 6.995 14.510 14.512 1.00 8.83 O
ATOM 412 CB THR A 53 6.486 16.500 12.035 1.00 8.62 C
ATOM 413 OG1 THR A 53 7.842 16.056 12.091 1.00 11.33 O
ATOM 414 CG2 THR A 53 6.448 17.954 11.730 1.00 9.39 C
ATOM 415 N VAL A 54 5.162 13.878 13.326 1.00 8.11 N
ATOM 416 CA VAL A 54 5.447 12.450 13.460 1.00 8.01 C
ATOM 417 C VAL A 54 5.220 11.770 12.117 1.00 8.16 C
ATOM 418 O VAL A 54 4.204 11.983 11.426 1.00 9.59 O
ATOM 419 CB VAL A 54 4.607 11.773 14.557 1.00 9.05 C
ATOM 420 CG1 VAL A 54 3.097 11.883 14.341 1.00 8.95 C
ATOM 421 CG2 VAL A 54 5.021 10.309 14.726 1.00 9.48 C
ATOM 422 N THR A 55 6.192 10.959 11.696 1.00 9.04 N
ATOM 423 CA THR A 55 6.221 10.355 10.371 1.00 9.74 C
ATOM 424 C THR A 55 6.552 8.886 10.482 1.00 9.58 C
ATOM 425 O THR A 55 7.550 8.495 11.114 1.00 12.09 O
ATOM 426 CB THR A 55 7.273 11.032 9.485 1.00 9.85 C
ATOM 427 OG1 THR A 55 6.968 12.434 9.487 1.00 11.62 O
ATOM 428 CG2 THR A 55 7.243 10.487 8.078 1.00 12.87 C
ATOM 429 N GLU A 56 5.746 8.050 9.841 1.00 10.29 N
ATOM 430 CA GLU A 56 6.035 6.627 9.727 1.00 12.75 C
ATOM 431 C GLU A 56 6.697 6.273 8.386 1.00 19.58 C
ATOM 432 O GLU A 56 6.586 7.040 7.456 1.00 18.77 O
ATOM 433 CB GLU A 56 4.755 5.824 9.860 1.00 14.63 C
ATOM 434 CG GLU A 56 4.209 5.857 11.264 1.00 13.33 C
ATOM 435 CD GLU A 56 3.031 4.952 11.472 1.00 15.16 C
ATOM 436 OE1 GLU A 56 2.013 4.954 10.710 1.00 18.50 O
ATOM 437 OE2 GLU A 56 3.019 4.149 12.406 1.00 16.91 O
ATOM 438 OXT GLU A 56 7.279 5.095 8.401 1.00 23.62 O
TER 439 GLU A 56
HETATM 440 P PO4 A 101 8.403 26.122 25.115 1.00 12.21 P
HETATM 441 O1 PO4 A 101 9.643 25.374 24.575 1.00 13.97 O
HETATM 442 O2 PO4 A 101 7.358 26.332 24.068 1.00 12.83 O
HETATM 443 O3 PO4 A 101 7.939 25.361 26.317 1.00 12.18 O
HETATM 444 O4 PO4 A 101 8.983 27.487 25.549 1.00 14.61 O
HETATM 445 C1 MRD A 102 9.423 15.356 20.042 1.00 13.61 C
HETATM 446 C2 MRD A 102 10.932 15.272 20.060 1.00 13.76 C
HETATM 447 O2 MRD A 102 11.192 14.006 20.727 1.00 13.86 O
HETATM 448 CM MRD A 102 11.533 15.448 18.734 1.00 17.10 C
HETATM 449 C3 MRD A 102 11.540 16.370 20.931 1.00 15.32 C
HETATM 450 C4 MRD A 102 13.084 16.341 20.837 1.00 15.11 C
HETATM 451 O4 MRD A 102 13.576 15.200 21.621 1.00 16.99 O
HETATM 452 C5 MRD A 102 13.613 17.602 21.545 1.00 17.40 C
HETATM 453 C1 IPA A 203 10.020 18.444 25.116 1.00 13.72 C
HETATM 454 C2 IPA A 203 10.626 19.153 23.848 1.00 16.09 C
HETATM 455 C3 IPA A 203 9.569 19.215 22.738 1.00 17.02 C
HETATM 456 O2 IPA A 203 10.831 20.528 24.141 1.00 17.64 O
HETATM 457 C1 IPA A 204 6.946 13.811 7.074 1.00 15.38 C
HETATM 458 C2 IPA A 204 7.049 15.294 7.493 1.00 22.63 C
HETATM 459 C3 IPA A 204 5.912 15.924 8.239 1.00 20.38 C
HETATM 460 O2 IPA A 204 7.337 16.158 6.408 1.00 63.21 O
HETATM 461 O HOH A1001 7.930 15.755 27.286 1.00 12.43 O
HETATM 462 O HOH A1003 8.266 13.440 11.720 1.00 10.28 O
HETATM 463 O HOH A1004 8.746 20.070 13.649 1.00 12.38 O
HETATM 464 O HOH A1005 -0.837 5.678 10.746 1.00 13.00 O
HETATM 465 O HOH A1006 11.993 9.970 16.486 1.00 12.10 O
HETATM 466 O HOH A1007 -0.958 22.030 29.796 1.00 12.97 O
HETATM 467 O HOH A1008 -7.298 18.216 14.569 1.00 13.96 O
HETATM 468 O HOH A1009 -1.183 30.195 21.565 1.00 15.00 O
HETATM 469 O HOH A1010 4.593 28.013 26.315 1.00 13.06 O
HETATM 470 O HOH A1011 -6.993 20.436 16.119 1.00 16.43 O
HETATM 471 O HOH A1012 0.164 19.641 7.130 1.00 15.95 O
HETATM 472 O HOH A1013 1.618 29.110 19.405 1.00 16.84 O
HETATM 473 O HOH A1014 5.561 25.567 32.313 1.00 18.03 O
HETATM 474 O HOH A1016 8.987 22.660 27.604 1.00 18.87 O
HETATM 475 O HOH A1017 -4.820 17.578 20.029 1.00 19.19 O
HETATM 476 O HOH A1018 4.121 8.216 20.533 1.00 17.88 O
HETATM 477 O HOH A1019 -1.496 19.807 28.183 1.00 21.23 O
HETATM 478 O HOH A1021 -2.763 27.521 26.163 1.00 21.81 O
HETATM 479 O HOH A1022 6.102 7.384 17.555 1.00 20.89 O
HETATM 480 O HOH A1023 -4.121 8.406 4.831 1.00 24.98 O
HETATM 481 O HOH A1024 -5.854 18.880 22.241 1.00 23.41 O
HETATM 482 O HOH A1027 4.046 5.894 19.134 1.00 22.85 O
HETATM 483 O HOH A1028 3.866 25.185 11.710 1.00 20.56 O
HETATM 484 O HOH A1029 -3.519 12.581 24.116 1.00 26.10 O
HETATM 485 O HOH A1030 -3.442 29.746 23.134 1.00 25.82 O
HETATM 486 O HOH A1031 -6.300 21.780 24.222 1.00 24.86 O
HETATM 487 O HOH A1032 -7.316 7.411 14.024 1.00 21.58 O
HETATM 488 O HOH A1033 -0.550 23.549 7.582 1.00 26.33 O
HETATM 489 O HOH A1034 -7.421 20.153 18.889 1.00 26.09 O
HETATM 490 O HOH A1035 -1.444 17.403 29.500 1.00 22.82 O
HETATM 491 O HOH A1036 -8.867 24.177 22.669 1.00 55.26 O
HETATM 492 O HOH A1037 5.394 2.373 12.039 1.00 28.24 O
HETATM 493 O HOH A1038 12.329 29.459 19.605 1.00 34.30 O
HETATM 494 O HOH A1039 -1.244 13.446 27.729 1.00 46.94 O
HETATM 495 O HOH A1040 0.934 17.421 33.009 1.00 24.69 O
HETATM 496 O HOH A1041 2.658 28.147 16.045 1.00 28.93 O
HETATM 497 O HOH A1042 -2.594 4.780 12.612 1.00 24.42 O
HETATM 498 O HOH A1043 3.187 1.187 13.287 1.00 40.51 O
HETATM 499 O HOH A1045 9.988 8.406 9.001 1.00 28.23 O
HETATM 500 O HOH A1046 0.631 6.471 29.197 1.00 22.86 O
HETATM 501 O HOH A1047 -5.582 9.479 22.827 1.00 30.42 O
HETATM 502 O HOH A1048 -7.684 12.113 14.266 1.00 44.10 O
HETATM 503 O HOH A1049 14.102 25.904 25.232 1.00 43.22 O
HETATM 504 O HOH A1050 3.992 8.613 31.737 1.00 35.94 O
HETATM 505 O HOH A1051 7.862 31.340 14.375 1.00 29.18 O
HETATM 506 O HOH A1052 6.420 9.588 4.208 1.00 29.97 O
HETATM 507 O HOH A1053 -2.608 0.022 19.160 1.00 41.85 O
HETATM 508 O HOH A1054 -2.230 30.765 19.147 1.00 25.73 O
HETATM 509 O HOH A1055 10.147 4.201 13.616 1.00 60.80 O
HETATM 510 O HOH A1056 1.477 2.472 18.179 1.00 54.45 O
HETATM 511 O HOH A1057 4.992 21.799 33.107 1.00 26.05 O
HETATM 512 O HOH A1058 6.930 29.457 25.828 1.00 21.86 O
HETATM 513 O HOH A1059 -0.599 16.881 7.425 1.00 22.03 O
HETATM 514 O HOH A1061 -3.530 19.958 26.133 1.00 28.46 O
HETATM 515 O HOH A1062 2.799 20.405 6.897 1.00 19.83 O
HETATM 516 O HOH A1063 -0.877 6.760 25.776 1.00 18.20 O
HETATM 517 O HOH A1064 7.981 21.630 11.329 1.00 26.46 O
HETATM 518 O HOH A1065 -4.630 14.896 21.284 1.00 52.53 O
HETATM 519 O HOH A1066 -2.278 25.545 15.723 1.00 48.67 O
HETATM 520 O HOH A1067 7.784 29.599 28.909 1.00 31.59 O
HETATM 521 O HOH A1069 8.006 24.363 11.592 1.00 21.10 O
HETATM 522 O HOH A1070 -5.174 22.719 30.973 1.00 56.70 O
HETATM 523 O HOH A1071 -11.128 17.773 22.631 1.00 49.59 O
HETATM 524 O HOH A1072 -3.878 8.340 2.284 1.00 52.98 O
HETATM 525 O HOH A1073 8.507 26.771 28.545 1.00 25.10 O
HETATM 526 O HOH A1076 2.364 3.227 25.807 1.00 63.72 O
HETATM 527 O HOH A1077 10.749 28.459 24.080 1.00 33.70 O
HETATM 528 O HOH A1078 -5.227 2.016 17.162 1.00 43.01 O
HETATM 529 O HOH A1079 10.768 30.299 28.969 1.00 53.18 O
HETATM 530 O HOH A1080 -5.196 8.999 25.200 0.50 73.67 O
HETATM 531 O HOH A1081 -0.040 15.598 29.429 1.00 55.82 O
HETATM 532 O HOH A1083 13.655 3.832 13.239 1.00 37.11 O
HETATM 533 O HOH A1084 -2.872 11.415 27.031 1.00 38.17 O
HETATM 534 O HOH A1085 -7.400 24.307 27.242 1.00 62.52 O
HETATM 535 O HOH A1086 4.427 8.425 6.158 1.00 22.37 O
HETATM 536 O HOH A1087 -6.438 23.932 21.292 1.00 39.95 O
HETATM 537 O HOH A1088 2.105 15.814 31.516 1.00 26.89 O
HETATM 538 O HOH A1089 -2.783 24.132 29.763 1.00 29.19 O
HETATM 539 O HOH A1090 10.620 30.943 12.600 0.50 47.70 O
HETATM 540 O HOH A1091 -2.745 10.180 1.301 1.00 32.80 O
HETATM 541 O HOH A1093 0.538 2.676 11.484 1.00 29.80 O
HETATM 542 O HOH A1094 -9.077 18.083 20.006 1.00 35.26 O
HETATM 543 O HOH A1095 9.755 5.062 11.528 1.00 33.89 O
HETATM 544 O HOH A1096 9.566 8.582 6.298 1.00 46.63 O
HETATM 545 O HOH A1097 0.636 4.216 26.932 1.00 31.90 O
HETATM 546 O HOH A1098 -1.062 -0.442 16.854 1.00 41.20 O
HETATM 547 O HOH A1099 7.887 31.002 24.437 1.00 38.41 O
HETATM 548 O HOH A1100 1.148 26.429 16.100 1.00 33.55 O
HETATM 549 O HOH A1101 -3.490 0.420 15.445 1.00 39.92 O
HETATM 550 O HOH A1102 5.587 19.320 34.157 1.00 24.81 O
HETATM 551 O HOH A1103 -7.738 19.838 26.107 1.00 36.47 O
HETATM 552 O HOH A1104 -6.457 15.770 20.200 1.00 33.73 O
HETATM 553 O HOH A1105 9.908 30.482 23.390 1.00 34.04 O
HETATM 554 O HOH A1107 5.612 3.809 4.634 1.00 39.02 O
HETATM 555 O HOH A1108 10.064 28.120 29.567 1.00 42.69 O
HETATM 556 O HOH A1109 -6.022 21.453 27.227 1.00 42.34 O
HETATM 557 O HOH A1110 10.054 21.423 9.652 1.00 31.50 O
HETATM 558 O HOH A1111 6.988 14.511 33.782 1.00 46.35 O
HETATM 559 O HOH A1112 1.300 13.687 32.321 1.00 48.79 O
HETATM 560 O HOH A1113 5.813 19.624 8.049 1.00 37.31 O
HETATM 561 O HOH A1114 10.934 22.851 26.399 1.00 46.75 O
HETATM 562 O HOH A1115 -7.653 3.563 15.826 1.00 40.68 O
HETATM 563 O HOH A1116 -3.703 15.969 29.108 1.00 33.50 O
HETATM 564 O HOH A1117 -5.581 32.457 19.388 1.00 43.76 O
HETATM 565 O HOH A1119 12.850 27.082 12.713 1.00 41.63 O
HETATM 566 O HOH A1120 8.042 23.874 32.274 1.00 41.23 O
HETATM 567 O HOH A1121 6.135 27.415 30.366 1.00 25.03 O
HETATM 568 O HOH A1122 5.866 18.193 30.982 1.00 35.40 O
HETATM 569 O HOH A1123 7.068 20.328 31.775 1.00 41.89 O
HETATM 570 O HOH A1125 -5.618 23.392 28.834 1.00 49.30 O
HETATM 571 O HOH A1126 1.155 6.650 2.977 1.00 35.64 O
HETATM 572 O HOH A1128 1.141 4.415 3.582 1.00 44.13 O
HETATM 573 O HOH A1130 -5.103 30.480 21.534 1.00 38.80 O
HETATM 574 O HOH A1131 0.137 0.555 13.605 1.00 36.54 O
HETATM 575 O HOH A1133 0.932 9.863 30.837 1.00 49.09 O
HETATM 576 O HOH A1134 14.314 27.280 21.681 1.00 59.25 O
HETATM 577 O HOH A1135 -4.838 18.332 27.091 1.00 53.01 O
HETATM 578 O HOH A1136 8.735 22.663 7.801 1.00 40.28 O
HETATM 579 O HOH A1140 -5.088 30.294 16.586 1.00 44.07 O
HETATM 580 O HOH A1141 5.191 24.713 9.893 1.00 48.26 O
HETATM 581 O HOH A1142 -4.287 1.973 11.398 1.00 59.91 O
HETATM 582 O HOH A1143 4.128 10.492 2.917 1.00 66.67 O
HETATM 583 O HOH A1144 8.030 -1.278 17.088 1.00 43.15 O
HETATM 584 O HOH A1145 -2.770 6.957 3.733 1.00 69.08 O
HETATM 585 O HOH A1146 4.365 10.709 30.882 1.00101.21 O
HETATM 586 O HOH A1147 -8.208 15.664 16.699 1.00 50.93 O
HETATM 587 O HOH A1148 -2.030 25.908 12.669 1.00 88.21 O
HETATM 588 O HOH A1149 -3.511 15.836 19.003 1.00 41.79 O
HETATM 589 O HOH A1151 3.231 7.008 4.466 1.00 48.40 O
HETATM 590 O HOH A1152 12.186 26.052 26.493 1.00 48.69 O
HETATM 591 O HOH A1153 -9.899 4.025 15.737 1.00111.37 O
HETATM 592 O HOH A1154 12.025 3.796 10.239 1.00 72.77 O
HETATM 593 O HOH A1155 0.009 0.974 20.645 1.00 68.15 O
HETATM 594 O HOH A1156 1.834 1.323 4.274 1.00 82.83 O
HETATM 595 O HOH A1157 -8.300 26.321 20.071 1.00 45.57 O
CONECT 440 441 442 443 444
CONECT 441 440
CONECT 442 440
CONECT 443 440
CONECT 444 440
CONECT 445 446
CONECT 446 445 447 448 449
CONECT 447 446
CONECT 448 446
CONECT 449 446 450
CONECT 450 449 451 452
CONECT 451 450
CONECT 452 450
CONECT 453 454
CONECT 454 453 455 456
CONECT 455 454
CONECT 456 454
CONECT 457 458
CONECT 458 457 459 460
CONECT 459 458
CONECT 460 458
MASTER 243 0 4 1 4 0 7 6 594 1 21 5
END