Browse entries in the PDBbind-CN Database
HEADER RNA BINDING PROTEIN/RNA 24-SEP-10 2XS2 TITLE CRYSTAL STRUCTURE OF THE RRM DOMAIN OF MOUSE DELETED IN AZOOSPERMIA- TITLE 2 LIKE IN COMPLEX WITH RNA, UUGUUCUU COMPND MOL_ID: 1; COMPND 2 MOLECULE: DELETED IN AZOOSPERMIA-LIKE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 32-132; COMPND 5 SYNONYM: DAZ-LIKE AUTOSOMAL, DELETED IN AZOOSPERMIA-LIKE 1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: 5'-R(*UP*UP*GP*UP*UP*CP*UP*U)-3'; COMPND 10 CHAIN: B; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA-2 PLYSS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-SUMO-28A; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 14 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 15 ORGANISM_TAXID: 10090 KEYWDS RNA BINDING PROTEIN-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR H.T.JENKINS,T.A.EDWARDS REVDAT 4 13-JUN-18 2XS2 1 JRNL REMARK REVDAT 3 23-NOV-11 2XS2 1 JRNL REVDAT 2 02-NOV-11 2XS2 1 JRNL REVDAT 1 05-OCT-11 2XS2 0 JRNL AUTH H.T.JENKINS,B.MALKOVA,T.A.EDWARDS JRNL TITL KINKED BETA-STRANDS MEDIATE HIGH-AFFINITY RECOGNITION OF JRNL TITL 2 MRNA TARGETS BY THE GERM-CELL REGULATOR DAZL. JRNL REF PROC. NATL. ACAD. SCI. V. 108 18266 2011 JRNL REF 2 U.S.A. JRNL REFN ESSN 1091-6490 JRNL PMID 22021443 JRNL DOI 10.1073/PNAS.1105211108 REMARK 2 REMARK 2 RESOLUTION. 1.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0102 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.41 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 3 NUMBER OF REFLECTIONS : 24721 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.163 REMARK 3 R VALUE (WORKING SET) : 0.161 REMARK 3 FREE R VALUE : 0.193 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1313 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.35 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1445 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.22 REMARK 3 BIN R VALUE (WORKING SET) : 0.3250 REMARK 3 BIN FREE R VALUE SET COUNT : 67 REMARK 3 BIN FREE R VALUE : 0.3210 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 679 REMARK 3 NUCLEIC ACID ATOMS : 124 REMARK 3 HETEROGEN ATOMS : 1 REMARK 3 SOLVENT ATOMS : 129 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 16.33 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.38 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.08000 REMARK 3 B22 (A**2) : 0.23000 REMARK 3 B33 (A**2) : -0.16000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.055 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.053 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.031 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.679 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 870 ; 0.017 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1203 ; 1.642 ; 2.133 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 96 ; 6.297 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 35 ;33.729 ;22.857 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 134 ;10.858 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;26.313 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 137 ; 0.110 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 622 ; 0.010 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 306 ; 0.198 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 573 ; 0.313 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 73 ; 0.109 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.030 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 45 ; 0.171 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.118 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 2 ; 0.062 ; 0.200 REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 448 ; 1.830 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 728 ; 2.864 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 422 ; 3.807 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 470 ; 5.342 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 870 ; 1.971 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY REMARK 4 REMARK 4 2XS2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-SEP-10. REMARK 100 THE DEPOSITION ID IS D_1290045494. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-APR-10 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 : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : KIRKPATRICK BAEZ BIMORPH MIRROR REMARK 200 PAIR FOR HORIZONTAL AND VERTICAL REMARK 200 FOCUSSING REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26034 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350 REMARK 200 RESOLUTION RANGE LOW (A) : 27.410 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.06000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.3 REMARK 200 DATA REDUNDANCY IN SHELL : 5.10 REMARK 200 R MERGE FOR SHELL (I) : 0.65000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHELX REMARK 200 STARTING MODEL: NONE REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM MAGNESIUM FORMATE, 20 % (W/V) REMARK 280 PEG 3350, 0.1 MM ZINC ACETATE 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 19.05000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.24500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.03000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.24500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.05000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.03000 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1350 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 6640 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.9 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 400 REMARK 400 COMPOUND REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 120 TO SER 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 31 REMARK 465 ASN A 118 REMARK 465 LEU A 119 REMARK 465 SER A 120 REMARK 465 THR A 121 REMARK 465 TYR A 122 REMARK 465 GLN A 125 REMARK 465 PRO A 126 REMARK 465 ARG A 127 REMARK 465 PRO A 128 REMARK 465 LEU A 129 REMARK 465 ILE A 130 REMARK 465 PHE A 131 REMARK 465 ASN A 132 REMARK 465 U B 1 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 LEU A 32 CG CD1 CD2 REMARK 470 GLU A 34 CG CD OE1 OE2 REMARK 470 LYS A 36 CG CD CE NZ REMARK 470 GLN A 117 CG CD OE1 NE2 REMARK 470 VAL A 124 CA C O CB CG1 CG2 REMARK 470 U B 2 P OP1 OP2 O5' C5' C4' O4' REMARK 470 U B 2 C3' C2' O2' C1' N1 C2 O2 REMARK 470 U B 2 N3 C4 O4 C5 C6 REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A2040 DISTANCE = 6.40 ANGSTROMS 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 ZN B1009 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 104 NE2 REMARK 620 2 GLU A 55 OE1 114.9 REMARK 620 3 HIS A 123 ND1 103.7 106.0 REMARK 620 4 C B 6 N3 113.9 97.0 121.6 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1009 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2XS5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE RRM DOMAIN OF MOUSE DELETED IN AZOOSPERMIA- REMARK 900 LIKE IN COMPLEX WITH MVH RNA, UGUUC REMARK 900 RELATED ID: 2XSF RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE RRM DOMAIN OF MOUSE DELETED IN AZOOSPERMIA- REMARK 900 LIKE REMARK 900 RELATED ID: 2XS7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE RRM DOMAIN OF MOUSE DELETED IN AZOOSPERMIA- REMARK 900 LIKE IN COMPLEX WITH SYCP3 RNA, UUGUUU DBREF 2XS2 A 32 132 UNP Q64368 DAZL_MOUSE 32 132 DBREF 2XS2 B 1 8 PDB 2XS2 2XS2 1 8 SEQADV 2XS2 SER A 31 UNP Q64368 EXPRESSION TAG SEQADV 2XS2 SER A 120 UNP Q64368 CYS 120 ENGINEERED MUTATION SEQRES 1 A 102 SER LEU PRO GLU GLY LYS ILE MET PRO ASN THR VAL PHE SEQRES 2 A 102 VAL GLY GLY ILE ASP VAL ARG MET ASP GLU THR GLU ILE SEQRES 3 A 102 ARG SER PHE PHE ALA ARG TYR GLY SER VAL LYS GLU VAL SEQRES 4 A 102 LYS ILE ILE THR ASP ARG THR GLY VAL SER LYS GLY TYR SEQRES 5 A 102 GLY PHE VAL SER PHE TYR ASN ASP VAL ASP VAL GLN LYS SEQRES 6 A 102 ILE VAL GLU SER GLN ILE ASN PHE HIS GLY LYS LYS LEU SEQRES 7 A 102 LYS LEU GLY PRO ALA ILE ARG LYS GLN ASN LEU SER THR SEQRES 8 A 102 TYR HIS VAL GLN PRO ARG PRO LEU ILE PHE ASN SEQRES 1 B 8 U U G U U C U U HET ZN B1009 1 HETNAM ZN ZINC ION FORMUL 3 ZN ZN 2+ FORMUL 4 HOH *129(H2 O) HELIX 1 1 ASP A 52 ALA A 61 1 10 HELIX 2 2 ARG A 62 GLY A 64 5 3 HELIX 3 3 ASP A 92 VAL A 97 1 6 SHEET 1 AA 4 VAL A 66 THR A 73 0 SHEET 2 AA 4 SER A 79 PHE A 87 -1 N LYS A 80 O ILE A 72 SHEET 3 AA 4 LYS A 36 GLY A 45 -1 O ASN A 40 N PHE A 87 SHEET 4 AA 4 LYS A 109 ARG A 115 -1 O LYS A 109 N GLY A 45 SHEET 1 AB 2 ASN A 102 PHE A 103 0 SHEET 2 AB 2 LYS A 106 LYS A 107 -1 O LYS A 106 N PHE A 103 LINK ZN ZN B1009 NE2 HIS A 104 1555 3554 1.98 LINK ZN ZN B1009 OE1 GLU A 55 1555 3554 1.98 LINK ZN ZN B1009 ND1 HIS A 123 1555 1555 2.05 LINK ZN ZN B1009 N3 C B 6 1555 1555 2.02 SITE 1 AC1 4 GLU A 55 HIS A 104 HIS A 123 C B 6 CRYST1 38.100 52.060 60.490 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 0.026247 0.000000 0.000000 0.00000 SCALE2 0.000000 0.019209 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016532 0.00000 ATOM 1 N LEU A 32 20.708 51.136 7.616 0.46 23.91 N ANISOU 1 N LEU A 32 3115 2843 3127 162 -66 126 N ATOM 2 CA LEU A 32 19.761 50.897 8.744 0.46 24.15 C ANISOU 2 CA LEU A 32 3036 2909 3228 87 -78 164 C ATOM 3 C LEU A 32 18.342 50.902 8.214 0.46 23.82 C ANISOU 3 C LEU A 32 2982 2840 3228 35 -93 225 C ATOM 4 O LEU A 32 17.877 51.958 7.759 0.46 24.05 O ANISOU 4 O LEU A 32 2970 2829 3339 67 -87 190 O ATOM 5 CB LEU A 32 19.895 51.984 9.808 0.46 24.43 C ANISOU 5 CB LEU A 32 3228 2856 3196 222 -83 50 C ATOM 6 N PRO A 33 17.644 49.747 8.318 0.63 22.85 N ANISOU 6 N PRO A 33 2844 2771 3067 -33 -42 292 N ATOM 7 CA PRO A 33 16.420 49.451 7.555 0.63 21.78 C ANISOU 7 CA PRO A 33 2709 2666 2898 -46 8 241 C ATOM 8 C PRO A 33 15.432 50.606 7.586 0.63 20.43 C ANISOU 8 C PRO A 33 2536 2544 2682 -73 -17 198 C ATOM 9 O PRO A 33 15.242 51.242 8.621 0.63 20.29 O ANISOU 9 O PRO A 33 2491 2556 2661 -32 -92 85 O ATOM 10 CB PRO A 33 15.843 48.222 8.262 0.63 22.18 C ANISOU 10 CB PRO A 33 2792 2607 3027 -114 2 281 C ATOM 11 CG PRO A 33 17.075 47.559 8.898 0.63 22.23 C ANISOU 11 CG PRO A 33 2671 2650 3125 -57 80 241 C ATOM 12 CD PRO A 33 17.927 48.711 9.337 0.63 22.98 C ANISOU 12 CD PRO A 33 2823 2768 3138 -39 -103 312 C ATOM 13 N GLU A 34 14.814 50.868 6.444 0.50 18.24 N ANISOU 13 N GLU A 34 2072 2298 2560 -107 -78 207 N ATOM 14 CA GLU A 34 13.951 52.029 6.331 0.50 18.45 C ANISOU 14 CA GLU A 34 2121 2292 2597 -86 -92 161 C ATOM 15 C GLU A 34 12.618 51.639 5.757 0.50 18.35 C ANISOU 15 C GLU A 34 2127 2341 2501 -70 -101 80 C ATOM 16 O GLU A 34 12.456 50.625 5.100 0.50 17.33 O ANISOU 16 O GLU A 34 2004 1980 2598 21 -189 85 O ATOM 17 CB GLU A 34 14.575 53.107 5.438 0.50 18.74 C ANISOU 17 CB GLU A 34 2184 2232 2703 -161 -42 157 C ATOM 18 N AGLY A 35 11.594 52.435 5.970 0.34 19.32 N ANISOU 18 N AGLY A 35 2281 2457 2604 -108 -154 155 N ATOM 19 N BGLY A 35 11.670 52.500 6.071 0.66 19.47 N ANISOU 19 N BGLY A 35 2332 2437 2629 -41 -137 230 N ATOM 20 CA AGLY A 35 10.370 52.139 5.240 0.34 19.22 C ANISOU 20 CA AGLY A 35 2295 2575 2432 -345 -115 71 C ATOM 21 CA BGLY A 35 10.350 52.391 5.524 0.66 18.73 C ANISOU 21 CA BGLY A 35 2318 2483 2314 -306 -6 78 C ATOM 22 C AGLY A 35 9.359 51.217 5.898 0.34 18.92 C ANISOU 22 C AGLY A 35 2338 2514 2334 -421 -156 36 C ATOM 23 C BGLY A 35 9.379 51.683 6.432 0.66 17.79 C ANISOU 23 C BGLY A 35 2392 2320 2045 -199 40 11 C ATOM 24 O AGLY A 35 9.664 50.030 6.221 0.34 19.03 O ANISOU 24 O AGLY A 35 2173 2794 2264 -421 -236 -7 O ATOM 25 O BGLY A 35 9.722 51.092 7.433 0.66 18.45 O ANISOU 25 O BGLY A 35 2578 2340 2091 -49 175 78 O ATOM 26 N LYS A 36 8.152 51.780 6.029 1.00 18.59 N ANISOU 26 N LYS A 36 2388 2443 2229 -487 -1 -79 N ATOM 27 CA LYS A 36 7.048 51.192 6.721 1.00 17.14 C ANISOU 27 CA LYS A 36 2170 2440 1900 -579 -39 -65 C ATOM 28 C LYS A 36 6.422 50.130 5.822 1.00 16.19 C ANISOU 28 C LYS A 36 2176 2140 1835 -596 -89 35 C ATOM 29 O LYS A 36 6.330 50.316 4.591 1.00 17.94 O ANISOU 29 O LYS A 36 2635 2389 1791 -686 -89 83 O ATOM 30 CB LYS A 36 6.029 52.284 6.923 1.00 19.71 C ANISOU 30 CB LYS A 36 2631 2465 2392 -544 -125 -310 C ATOM 31 N ILE A 37 5.968 49.037 6.432 1.00 14.10 N ANISOU 31 N ILE A 37 1807 1934 1615 -413 -78 76 N ATOM 32 CA ILE A 37 5.224 47.986 5.715 1.00 14.05 C ANISOU 32 CA ILE A 37 1789 1860 1687 -190 -120 107 C ATOM 33 C ILE A 37 3.791 48.425 5.560 1.00 13.79 C ANISOU 33 C ILE A 37 1729 1939 1571 -121 15 9 C ATOM 34 O ILE A 37 3.143 48.764 6.561 1.00 16.02 O ANISOU 34 O ILE A 37 1967 2346 1772 -35 12 -173 O ATOM 35 CB ILE A 37 5.321 46.653 6.495 1.00 14.36 C ANISOU 35 CB ILE A 37 1965 1824 1665 -115 -121 117 C ATOM 36 CG1 ILE A 37 6.795 46.273 6.671 1.00 16.79 C ANISOU 36 CG1 ILE A 37 2151 2317 1908 215 -124 479 C ATOM 37 CG2 ILE A 37 4.543 45.596 5.788 1.00 16.18 C ANISOU 37 CG2 ILE A 37 2104 1992 2052 -464 -111 69 C ATOM 38 CD1 ILE A 37 7.065 45.056 7.549 1.00 19.13 C ANISOU 38 CD1 ILE A 37 2669 2616 1981 398 -111 490 C ATOM 39 N MET A 38 3.319 48.459 4.310 1.00 13.32 N ANISOU 39 N MET A 38 1725 1719 1613 -112 -113 -59 N ATOM 40 CA MET A 38 1.994 48.944 4.001 1.00 13.55 C ANISOU 40 CA MET A 38 1796 1693 1659 -34 19 13 C ATOM 41 C MET A 38 0.972 47.804 4.155 1.00 13.43 C ANISOU 41 C MET A 38 1725 1851 1526 -97 31 -45 C ATOM 42 O MET A 38 1.068 46.803 3.441 1.00 13.75 O ANISOU 42 O MET A 38 1727 1816 1681 11 48 27 O ATOM 43 CB MET A 38 1.953 49.524 2.579 1.00 14.24 C ANISOU 43 CB MET A 38 1902 1738 1771 -203 -34 75 C ATOM 44 CG MET A 38 2.881 50.736 2.358 1.00 16.76 C ANISOU 44 CG MET A 38 2262 1929 2174 -464 290 -176 C ATOM 45 SD MET A 38 2.276 52.181 3.274 1.00 24.76 S ANISOU 45 SD MET A 38 3483 2330 3594 -627 488 -123 S ATOM 46 CE MET A 38 3.356 52.034 4.491 1.00 19.53 C ANISOU 46 CE MET A 38 2951 1924 2542 -298 477 471 C ATOM 47 N PRO A 39 -0.037 47.975 5.021 1.00 13.95 N ANISOU 47 N PRO A 39 1627 1777 1894 -78 59 -80 N ATOM 48 CA PRO A 39 -0.996 46.863 5.144 1.00 13.64 C ANISOU 48 CA PRO A 39 1693 1874 1614 -232 199 -123 C ATOM 49 C PRO A 39 -1.803 46.617 3.870 1.00 12.04 C ANISOU 49 C PRO A 39 1389 1612 1574 -67 44 88 C ATOM 50 O PRO A 39 -2.082 47.547 3.103 1.00 12.69 O ANISOU 50 O PRO A 39 1437 1701 1681 28 -8 34 O ATOM 51 CB PRO A 39 -1.933 47.316 6.290 1.00 16.09 C ANISOU 51 CB PRO A 39 1930 2358 1823 -206 310 -270 C ATOM 52 CG PRO A 39 -1.773 48.771 6.366 1.00 20.77 C ANISOU 52 CG PRO A 39 2439 2676 2774 -280 553 -174 C ATOM 53 CD PRO A 39 -0.364 49.103 5.905 1.00 15.90 C ANISOU 53 CD PRO A 39 2057 2024 1961 -146 352 -154 C ATOM 54 N ASN A 40 -2.169 45.356 3.699 1.00 11.90 N ANISOU 54 N ASN A 40 1353 1575 1592 -44 51 -55 N ATOM 55 CA ASN A 40 -3.130 44.966 2.661 1.00 11.85 C ANISOU 55 CA ASN A 40 1250 1763 1488 -57 65 112 C ATOM 56 C ASN A 40 -2.668 45.390 1.277 1.00 11.83 C ANISOU 56 C ASN A 40 1334 1647 1511 0 78 160 C ATOM 57 O ASN A 40 -3.500 45.666 0.396 1.00 12.06 O ANISOU 57 O ASN A 40 1222 1733 1626 -11 22 198 O ATOM 58 CB ASN A 40 -4.541 45.513 3.009 1.00 12.87 C ANISOU 58 CB ASN A 40 1464 1769 1656 33 239 38 C ATOM 59 CG ASN A 40 -5.052 44.931 4.301 1.00 13.61 C ANISOU 59 CG ASN A 40 1528 1817 1825 -103 5 -24 C ATOM 60 OD1 ASN A 40 -4.750 43.774 4.612 1.00 13.96 O ANISOU 60 OD1 ASN A 40 1399 1831 2071 -338 193 125 O ATOM 61 ND2 ASN A 40 -5.828 45.695 5.050 1.00 17.17 N ANISOU 61 ND2 ASN A 40 2030 2600 1894 118 386 -292 N ATOM 62 N THR A 41 -1.341 45.356 1.066 1.00 10.86 N ANISOU 62 N THR A 41 1246 1418 1463 -97 25 241 N ATOM 63 CA THR A 41 -0.767 45.766 -0.197 1.00 10.61 C ANISOU 63 CA THR A 41 1277 1267 1486 -90 129 17 C ATOM 64 C THR A 41 0.320 44.747 -0.518 1.00 9.69 C ANISOU 64 C THR A 41 1044 1344 1294 -26 -30 118 C ATOM 65 O THR A 41 1.045 44.289 0.388 1.00 10.91 O ANISOU 65 O THR A 41 1109 1539 1494 -50 -135 165 O ATOM 66 CB THR A 41 -0.151 47.169 -0.053 1.00 10.74 C ANISOU 66 CB THR A 41 1222 1272 1584 -103 159 32 C ATOM 67 OG1 THR A 41 -1.139 48.080 0.436 1.00 12.87 O ANISOU 67 OG1 THR A 41 1517 1617 1755 229 145 68 O ATOM 68 CG2 THR A 41 0.378 47.671 -1.359 1.00 12.26 C ANISOU 68 CG2 THR A 41 1468 1702 1487 -282 35 291 C ATOM 69 N VAL A 42 0.470 44.410 -1.799 1.00 10.67 N ANISOU 69 N VAL A 42 1260 1386 1406 89 61 77 N ATOM 70 CA VAL A 42 1.463 43.461 -2.271 1.00 9.91 C ANISOU 70 CA VAL A 42 993 1385 1388 41 91 95 C ATOM 71 C VAL A 42 2.339 44.136 -3.329 1.00 10.67 C ANISOU 71 C VAL A 42 1194 1438 1420 45 30 201 C ATOM 72 O VAL A 42 1.810 44.720 -4.280 1.00 11.53 O ANISOU 72 O VAL A 42 1175 1611 1593 83 -111 85 O ATOM 73 CB VAL A 42 0.763 42.214 -2.852 1.00 10.90 C ANISOU 73 CB VAL A 42 1167 1337 1638 9 175 38 C ATOM 74 CG1 VAL A 42 1.785 41.219 -3.335 1.00 11.83 C ANISOU 74 CG1 VAL A 42 1255 1355 1883 97 217 116 C ATOM 75 CG2 VAL A 42 -0.188 41.567 -1.824 1.00 14.40 C ANISOU 75 CG2 VAL A 42 1384 1988 2096 -180 347 273 C ATOM 76 N PHE A 43 3.664 44.062 -3.165 1.00 9.76 N ANISOU 76 N PHE A 43 1113 1289 1306 -17 79 91 N ATOM 77 CA PHE A 43 4.590 44.461 -4.206 1.00 9.51 C ANISOU 77 CA PHE A 43 1092 1262 1256 -9 -68 41 C ATOM 78 C PHE A 43 4.572 43.383 -5.292 1.00 9.77 C ANISOU 78 C PHE A 43 1116 1180 1413 57 -11 131 C ATOM 79 O PHE A 43 4.657 42.171 -4.999 1.00 10.71 O ANISOU 79 O PHE A 43 1159 1298 1610 52 -80 197 O ATOM 80 CB PHE A 43 5.999 44.563 -3.601 1.00 10.49 C ANISOU 80 CB PHE A 43 1002 1584 1397 -30 -103 120 C ATOM 81 CG PHE A 43 7.094 44.684 -4.642 1.00 10.03 C ANISOU 81 CG PHE A 43 985 1464 1358 -42 -64 228 C ATOM 82 CD1 PHE A 43 7.543 45.944 -5.112 1.00 12.56 C ANISOU 82 CD1 PHE A 43 1590 1565 1617 -215 -36 261 C ATOM 83 CD2 PHE A 43 7.721 43.558 -5.145 1.00 11.12 C ANISOU 83 CD2 PHE A 43 1100 1573 1549 99 -33 261 C ATOM 84 CE1 PHE A 43 8.573 46.025 -6.062 1.00 12.30 C ANISOU 84 CE1 PHE A 43 1307 1555 1811 -31 82 347 C ATOM 85 CE2 PHE A 43 8.749 43.650 -6.105 1.00 11.49 C ANISOU 85 CE2 PHE A 43 949 1743 1673 -12 52 191 C ATOM 86 CZ PHE A 43 9.173 44.892 -6.542 1.00 12.32 C ANISOU 86 CZ PHE A 43 1300 1648 1732 -85 24 177 C ATOM 87 N VAL A 44 4.491 43.851 -6.539 1.00 11.13 N ANISOU 87 N VAL A 44 1291 1461 1477 10 -96 98 N ATOM 88 CA VAL A 44 4.505 42.958 -7.706 1.00 11.38 C ANISOU 88 CA VAL A 44 1262 1620 1441 -45 1 58 C ATOM 89 C VAL A 44 5.622 43.417 -8.628 1.00 11.42 C ANISOU 89 C VAL A 44 1397 1484 1457 93 97 149 C ATOM 90 O VAL A 44 5.505 44.464 -9.287 1.00 12.30 O ANISOU 90 O VAL A 44 1576 1463 1634 57 132 93 O ATOM 91 CB VAL A 44 3.153 42.976 -8.451 1.00 11.20 C ANISOU 91 CB VAL A 44 1383 1441 1429 -64 -34 160 C ATOM 92 CG1 VAL A 44 3.162 42.061 -9.670 1.00 14.52 C ANISOU 92 CG1 VAL A 44 2018 1658 1841 204 -108 -37 C ATOM 93 CG2 VAL A 44 2.038 42.616 -7.449 1.00 13.16 C ANISOU 93 CG2 VAL A 44 1338 1814 1846 -150 -119 302 C ATOM 94 N GLY A 45 6.694 42.626 -8.678 1.00 12.79 N ANISOU 94 N GLY A 45 1361 1678 1821 21 143 37 N ATOM 95 CA GLY A 45 7.817 42.964 -9.536 1.00 14.51 C ANISOU 95 CA GLY A 45 1568 1831 2114 89 271 56 C ATOM 96 C GLY A 45 7.900 42.002 -10.694 1.00 14.54 C ANISOU 96 C GLY A 45 1673 1724 2127 27 189 53 C ATOM 97 O GLY A 45 7.118 41.041 -10.824 1.00 14.43 O ANISOU 97 O GLY A 45 1757 1602 2124 65 38 10 O ATOM 98 N GLY A 46 8.824 42.287 -11.592 1.00 15.92 N ANISOU 98 N GLY A 46 1852 2007 2187 30 410 -108 N ATOM 99 CA GLY A 46 8.968 41.469 -12.774 1.00 17.87 C ANISOU 99 CA GLY A 46 2281 2180 2327 -126 468 -124 C ATOM 100 C GLY A 46 7.829 41.630 -13.757 1.00 17.74 C ANISOU 100 C GLY A 46 2257 2127 2355 -173 416 -127 C ATOM 101 O GLY A 46 7.542 40.705 -14.552 1.00 21.14 O ANISOU 101 O GLY A 46 2955 2277 2800 -234 336 -175 O ATOM 102 N ILE A 47 7.195 42.818 -13.743 1.00 18.40 N ANISOU 102 N ILE A 47 2316 2288 2384 -111 406 -22 N ATOM 103 CA ILE A 47 6.132 43.141 -14.690 1.00 19.01 C ANISOU 103 CA ILE A 47 2521 2331 2371 -349 234 -45 C ATOM 104 C ILE A 47 6.784 43.432 -16.059 1.00 21.14 C ANISOU 104 C ILE A 47 2711 2767 2552 -535 303 -135 C ATOM 105 O ILE A 47 7.625 44.314 -16.187 1.00 22.77 O ANISOU 105 O ILE A 47 3277 2823 2552 -788 231 -151 O ATOM 106 CB ILE A 47 5.209 44.306 -14.206 1.00 19.04 C ANISOU 106 CB ILE A 47 2547 2408 2277 -247 162 -56 C ATOM 107 CG1 ILE A 47 4.577 43.941 -12.861 1.00 19.39 C ANISOU 107 CG1 ILE A 47 2607 2402 2356 87 230 -37 C ATOM 108 CG2 ILE A 47 4.090 44.538 -15.249 1.00 20.70 C ANISOU 108 CG2 ILE A 47 2775 2480 2610 -369 -100 19 C ATOM 109 CD1 ILE A 47 3.800 45.093 -12.232 1.00 18.56 C ANISOU 109 CD1 ILE A 47 2566 1868 2617 268 -136 29 C ATOM 110 N ASP A 48 6.415 42.641 -17.053 1.00 24.51 N ANISOU 110 N ASP A 48 3243 3248 2819 -542 320 -261 N ATOM 111 CA ASP A 48 7.032 42.579 -18.372 1.00 26.88 C ANISOU 111 CA ASP A 48 3554 3499 3160 -478 258 -273 C ATOM 112 C ASP A 48 6.216 43.477 -19.291 1.00 27.05 C ANISOU 112 C ASP A 48 3680 3487 3110 -494 250 -212 C ATOM 113 O ASP A 48 5.015 43.678 -19.074 1.00 26.04 O ANISOU 113 O ASP A 48 3722 3269 2904 -533 329 -423 O ATOM 114 CB ASP A 48 6.926 41.113 -18.842 1.00 28.42 C ANISOU 114 CB ASP A 48 3712 3627 3458 -394 337 -248 C ATOM 115 CG ASP A 48 7.755 40.818 -20.049 1.00 30.71 C ANISOU 115 CG ASP A 48 3956 4131 3581 -337 276 -355 C ATOM 116 OD1 ASP A 48 9.009 40.672 -19.912 1.00 35.57 O ANISOU 116 OD1 ASP A 48 4279 4879 4356 -168 578 -320 O ATOM 117 OD2 ASP A 48 7.152 40.736 -21.133 1.00 34.16 O ANISOU 117 OD2 ASP A 48 4090 4944 3945 -526 191 -535 O ATOM 118 N VAL A 49 6.826 43.974 -20.369 1.00 27.95 N ANISOU 118 N VAL A 49 3745 3584 3288 -643 251 -182 N ATOM 119 CA VAL A 49 6.072 44.801 -21.313 1.00 29.23 C ANISOU 119 CA VAL A 49 3898 3745 3463 -564 241 -31 C ATOM 120 C VAL A 49 4.859 44.077 -22.018 1.00 29.31 C ANISOU 120 C VAL A 49 3908 3838 3388 -465 224 -2 C ATOM 121 O VAL A 49 3.877 44.729 -22.420 1.00 30.80 O ANISOU 121 O VAL A 49 4192 3999 3511 -436 143 0 O ATOM 122 CB VAL A 49 7.021 45.457 -22.366 1.00 30.14 C ANISOU 122 CB VAL A 49 4035 3844 3571 -581 303 -7 C ATOM 123 CG1 VAL A 49 7.576 44.414 -23.324 1.00 31.62 C ANISOU 123 CG1 VAL A 49 4229 3987 3797 -576 414 44 C ATOM 124 CG2 VAL A 49 6.286 46.566 -23.085 1.00 32.42 C ANISOU 124 CG2 VAL A 49 4262 4265 3788 -574 95 35 C ATOM 125 N ARG A 50 4.919 42.741 -22.109 1.00 28.28 N ANISOU 125 N ARG A 50 3840 3783 3123 -543 306 65 N ATOM 126 CA ARG A 50 3.847 41.950 -22.721 1.00 27.64 C ANISOU 126 CA ARG A 50 3710 3713 3077 -576 322 153 C ATOM 127 C ARG A 50 2.629 41.792 -21.787 1.00 25.78 C ANISOU 127 C ARG A 50 3530 3434 2828 -546 232 209 C ATOM 128 O ARG A 50 1.550 41.343 -22.215 1.00 26.64 O ANISOU 128 O ARG A 50 3782 3569 2768 -640 169 274 O ATOM 129 CB ARG A 50 4.390 40.582 -23.160 1.00 27.19 C ANISOU 129 CB ARG A 50 3711 3644 2974 -622 317 54 C ATOM 130 CG ARG A 50 5.613 40.654 -24.138 1.00 31.71 C ANISOU 130 CG ARG A 50 4220 4300 3529 -639 389 9 C ATOM 131 CD ARG A 50 5.878 39.349 -24.898 1.00 36.53 C ANISOU 131 CD ARG A 50 5078 4582 4218 -531 204 -182 C ATOM 132 NE ARG A 50 4.647 38.890 -25.547 1.00 40.44 N ANISOU 132 NE ARG A 50 5549 5137 4677 -750 -95 -22 N ATOM 133 CZ ARG A 50 4.172 39.328 -26.713 1.00 41.50 C ANISOU 133 CZ ARG A 50 5815 5223 4730 -811 -343 -32 C ATOM 134 NH1 ARG A 50 4.840 40.231 -27.430 1.00 42.74 N ANISOU 134 NH1 ARG A 50 6235 5538 4464 -763 -217 -4 N ATOM 135 NH2 ARG A 50 3.021 38.849 -27.165 1.00 43.28 N ANISOU 135 NH2 ARG A 50 5766 5478 5199 -907 -365 87 N ATOM 136 N MET A 51 2.794 42.165 -20.516 1.00 25.21 N ANISOU 136 N MET A 51 3389 3319 2868 -597 171 327 N ATOM 137 CA MET A 51 1.707 42.093 -19.538 1.00 24.15 C ANISOU 137 CA MET A 51 3268 3079 2829 -471 101 313 C ATOM 138 C MET A 51 0.873 43.361 -19.505 1.00 24.47 C ANISOU 138 C MET A 51 3398 2945 2954 -377 106 301 C ATOM 139 O MET A 51 1.275 44.381 -20.113 1.00 27.02 O ANISOU 139 O MET A 51 3834 3217 3214 -322 231 538 O ATOM 140 CB MET A 51 2.301 41.820 -18.143 1.00 22.05 C ANISOU 140 CB MET A 51 2992 2794 2591 -533 29 403 C ATOM 141 CG MET A 51 3.176 40.583 -18.062 1.00 21.65 C ANISOU 141 CG MET A 51 2873 2833 2519 -642 285 53 C ATOM 142 SD MET A 51 3.780 40.474 -16.355 1.00 21.24 S ANISOU 142 SD MET A 51 2747 2647 2676 -769 60 -378 S ATOM 143 CE MET A 51 4.908 39.087 -16.502 1.00 24.23 C ANISOU 143 CE MET A 51 2511 3207 3488 -415 172 -700 C ATOM 144 N ASP A 52 -0.265 43.314 -18.806 1.00 24.15 N ANISOU 144 N ASP A 52 3424 2897 2852 -275 55 236 N ATOM 145 CA AASP A 52 -1.204 44.435 -18.673 0.36 24.50 C ANISOU 145 CA AASP A 52 3515 2832 2960 -229 16 130 C ATOM 146 CA BASP A 52 -1.083 44.504 -18.598 0.64 24.16 C ANISOU 146 CA BASP A 52 3478 2824 2876 -202 -23 119 C ATOM 147 C ASP A 52 -1.742 44.549 -17.225 1.00 24.50 C ANISOU 147 C ASP A 52 3584 2747 2977 -169 -39 28 C ATOM 148 O ASP A 52 -1.778 43.560 -16.487 1.00 23.29 O ANISOU 148 O ASP A 52 3724 2270 2855 -266 -122 -48 O ATOM 149 CB AASP A 52 -2.345 44.219 -19.680 0.36 24.63 C ANISOU 149 CB AASP A 52 3503 2907 2945 -243 32 170 C ATOM 150 CB BASP A 52 -2.098 44.721 -19.739 0.64 23.98 C ANISOU 150 CB BASP A 52 3421 2870 2817 -195 -58 159 C ATOM 151 CG AASP A 52 -3.198 45.454 -19.916 0.36 25.18 C ANISOU 151 CG AASP A 52 3517 2951 3096 -269 39 213 C ATOM 152 CG BASP A 52 -3.429 44.010 -19.515 0.64 24.67 C ANISOU 152 CG BASP A 52 3420 2979 2973 11 -108 33 C ATOM 153 OD1AASP A 52 -3.664 46.071 -18.949 0.36 26.97 O ANISOU 153 OD1AASP A 52 3782 3266 3198 -231 165 358 O ATOM 154 OD1BASP A 52 -3.483 42.960 -18.827 0.64 23.83 O ANISOU 154 OD1BASP A 52 3558 2700 2793 180 80 -135 O ATOM 155 OD2AASP A 52 -3.456 45.779 -21.099 0.36 27.47 O ANISOU 155 OD2AASP A 52 3802 3166 3467 -285 -127 256 O ATOM 156 OD2BASP A 52 -4.449 44.514 -20.027 0.64 29.06 O ANISOU 156 OD2BASP A 52 3784 3493 3761 258 -237 232 O ATOM 157 N GLU A 53 -2.196 45.732 -16.835 1.00 25.17 N ANISOU 157 N GLU A 53 3660 2683 3218 -42 -98 26 N ATOM 158 CA AGLU A 53 -2.783 45.949 -15.527 0.57 24.98 C ANISOU 158 CA AGLU A 53 3640 2709 3142 1 -203 -20 C ATOM 159 CA BGLU A 53 -2.774 45.913 -15.516 0.43 25.04 C ANISOU 159 CA BGLU A 53 3582 2769 3162 3 -174 -22 C ATOM 160 C GLU A 53 -4.049 45.102 -15.349 1.00 24.72 C ANISOU 160 C GLU A 53 3569 2747 3076 25 -189 -51 C ATOM 161 O GLU A 53 -4.297 44.558 -14.280 1.00 24.03 O ANISOU 161 O GLU A 53 3652 2638 2838 18 -349 -102 O ATOM 162 CB AGLU A 53 -3.053 47.461 -15.325 0.57 26.38 C ANISOU 162 CB AGLU A 53 3873 2762 3388 51 -164 -6 C ATOM 163 CB BGLU A 53 -3.027 47.401 -15.216 0.43 26.14 C ANISOU 163 CB BGLU A 53 3747 2845 3339 62 -114 -20 C ATOM 164 CG AGLU A 53 -3.784 47.868 -14.032 0.57 27.73 C ANISOU 164 CG AGLU A 53 4149 3085 3301 108 -333 31 C ATOM 165 CG BGLU A 53 -1.797 48.262 -15.350 0.43 27.70 C ANISOU 165 CG BGLU A 53 3679 3301 3543 43 -154 43 C ATOM 166 CD AGLU A 53 -5.308 47.818 -14.149 0.57 29.10 C ANISOU 166 CD AGLU A 53 4306 3084 3666 321 -632 26 C ATOM 167 CD BGLU A 53 -2.052 49.730 -15.041 0.43 28.74 C ANISOU 167 CD BGLU A 53 3781 3425 3714 66 -10 22 C ATOM 168 OE1AGLU A 53 -5.802 47.679 -15.281 0.57 32.92 O ANISOU 168 OE1AGLU A 53 5354 3119 4034 366 -821 -403 O ATOM 169 OE1BGLU A 53 -2.715 50.030 -14.029 0.43 31.26 O ANISOU 169 OE1BGLU A 53 3894 3944 4039 188 33 -46 O ATOM 170 OE2AGLU A 53 -6.020 47.942 -13.121 0.57 30.84 O ANISOU 170 OE2AGLU A 53 4685 3522 3511 241 -823 103 O ATOM 171 OE2BGLU A 53 -1.558 50.593 -15.796 0.43 28.40 O ANISOU 171 OE2BGLU A 53 3631 3506 3652 213 -60 229 O ATOM 172 N THR A 54 -4.846 44.986 -16.408 1.00 23.93 N ANISOU 172 N THR A 54 3488 2703 2898 78 -303 -84 N ATOM 173 CA THR A 54 -6.136 44.311 -16.281 1.00 23.77 C ANISOU 173 CA THR A 54 3404 2862 2764 115 -311 -78 C ATOM 174 C THR A 54 -6.010 42.849 -15.856 1.00 20.75 C ANISOU 174 C THR A 54 2970 2633 2278 118 -309 -224 C ATOM 175 O THR A 54 -6.784 42.380 -15.027 1.00 21.28 O ANISOU 175 O THR A 54 3032 2749 2304 140 -360 -355 O ATOM 176 CB THR A 54 -6.995 44.359 -17.596 1.00 25.51 C ANISOU 176 CB THR A 54 3690 3121 2882 187 -298 -40 C ATOM 177 OG1 THR A 54 -6.338 43.637 -18.654 1.00 29.31 O ANISOU 177 OG1 THR A 54 4405 3623 3108 291 -238 61 O ATOM 178 CG2 THR A 54 -7.307 45.789 -18.013 1.00 28.12 C ANISOU 178 CG2 THR A 54 3862 3307 3515 203 -286 -10 C ATOM 179 N GLU A 55 -5.037 42.123 -16.412 1.00 19.93 N ANISOU 179 N GLU A 55 2993 2494 2083 8 -211 -247 N ATOM 180 CA GLU A 55 -4.937 40.704 -16.074 1.00 17.80 C ANISOU 180 CA GLU A 55 2543 2281 1937 6 3 -291 C ATOM 181 C GLU A 55 -4.419 40.566 -14.648 1.00 16.76 C ANISOU 181 C GLU A 55 2427 2028 1910 -93 26 -329 C ATOM 182 O GLU A 55 -4.749 39.612 -13.972 1.00 15.06 O ANISOU 182 O GLU A 55 2317 1754 1648 -184 85 -438 O ATOM 183 CB GLU A 55 -4.047 39.971 -17.073 1.00 18.25 C ANISOU 183 CB GLU A 55 2638 2429 1866 -163 56 -436 C ATOM 184 CG GLU A 55 -2.546 40.341 -17.034 1.00 18.92 C ANISOU 184 CG GLU A 55 2626 2409 2153 -241 193 -22 C ATOM 185 CD GLU A 55 -1.826 39.907 -18.287 1.00 19.74 C ANISOU 185 CD GLU A 55 2727 2405 2367 -599 249 -358 C ATOM 186 OE1 GLU A 55 -2.353 39.033 -19.001 1.00 16.93 O ANISOU 186 OE1 GLU A 55 2676 2217 1538 -436 285 -270 O ATOM 187 OE2 GLU A 55 -0.716 40.394 -18.564 1.00 20.34 O ANISOU 187 OE2 GLU A 55 2935 2485 2308 -891 239 -661 O ATOM 188 N ILE A 56 -3.606 41.503 -14.191 1.00 15.51 N ANISOU 188 N ILE A 56 2208 1967 1718 -94 -38 -355 N ATOM 189 CA ILE A 56 -3.138 41.479 -12.801 1.00 14.41 C ANISOU 189 CA ILE A 56 2038 1774 1664 -220 -15 -301 C ATOM 190 C ILE A 56 -4.309 41.766 -11.866 1.00 14.83 C ANISOU 190 C ILE A 56 2088 1754 1793 -104 -27 -198 C ATOM 191 O ILE A 56 -4.504 41.025 -10.887 1.00 13.89 O ANISOU 191 O ILE A 56 1937 1716 1623 -205 -10 -240 O ATOM 192 CB ILE A 56 -1.961 42.461 -12.584 1.00 14.31 C ANISOU 192 CB ILE A 56 2033 1772 1630 -230 56 -403 C ATOM 193 CG1 ILE A 56 -0.755 42.035 -13.457 1.00 17.15 C ANISOU 193 CG1 ILE A 56 2186 2163 2165 -486 354 -407 C ATOM 194 CG2 ILE A 56 -1.605 42.571 -11.085 1.00 15.84 C ANISOU 194 CG2 ILE A 56 2536 1971 1511 -544 -6 -409 C ATOM 195 CD1 ILE A 56 0.376 43.094 -13.484 1.00 19.20 C ANISOU 195 CD1 ILE A 56 2243 2527 2523 -914 487 -544 C ATOM 196 N ARG A 57 -5.085 42.805 -12.166 1.00 15.08 N ANISOU 196 N ARG A 57 1995 2018 1714 35 -119 -223 N ATOM 197 CA AARG A 57 -6.284 43.131 -11.429 0.54 15.98 C ANISOU 197 CA AARG A 57 2144 2062 1862 176 -88 -287 C ATOM 198 CA BARG A 57 -6.290 43.091 -11.369 0.46 16.07 C ANISOU 198 CA BARG A 57 2148 2121 1838 130 -73 -285 C ATOM 199 C ARG A 57 -7.227 41.907 -11.308 1.00 16.50 C ANISOU 199 C ARG A 57 2129 2221 1919 132 21 -257 C ATOM 200 O ARG A 57 -7.760 41.578 -10.241 1.00 16.84 O ANISOU 200 O ARG A 57 2207 2333 1856 -18 63 -462 O ATOM 201 CB AARG A 57 -6.932 44.338 -12.130 0.54 17.32 C ANISOU 201 CB AARG A 57 2304 2267 2007 250 -114 -188 C ATOM 202 CB BARG A 57 -7.089 44.316 -11.840 0.46 17.09 C ANISOU 202 CB BARG A 57 2264 2315 1912 162 -115 -196 C ATOM 203 CG AARG A 57 -8.095 44.933 -11.414 0.54 18.47 C ANISOU 203 CG AARG A 57 2347 2303 2367 490 -203 -175 C ATOM 204 CG BARG A 57 -8.325 44.556 -10.947 0.46 18.84 C ANISOU 204 CG BARG A 57 2453 2602 2101 202 -102 -99 C ATOM 205 CD AARG A 57 -8.440 46.409 -11.714 0.54 22.87 C ANISOU 205 CD AARG A 57 2836 2628 3223 954 -634 -78 C ATOM 206 CD BARG A 57 -9.471 45.349 -11.572 0.46 21.78 C ANISOU 206 CD BARG A 57 2494 3038 2744 295 -60 -21 C ATOM 207 NE AARG A 57 -9.334 46.727 -10.623 0.54 26.68 N ANISOU 207 NE AARG A 57 2968 3482 3686 829 -538 -32 N ATOM 208 NE BARG A 57 -10.667 45.309 -10.712 0.46 25.12 N ANISOU 208 NE BARG A 57 2917 3425 3200 134 -124 425 N ATOM 209 CZ AARG A 57 -9.156 47.640 -9.679 0.54 24.06 C ANISOU 209 CZ AARG A 57 2480 3142 3519 1090 -733 38 C ATOM 210 CZ BARG A 57 -10.980 44.341 -9.840 0.46 23.89 C ANISOU 210 CZ BARG A 57 2901 3226 2949 251 -369 341 C ATOM 211 NH1AARG A 57 -8.152 48.499 -9.709 0.54 24.54 N ANISOU 211 NH1AARG A 57 2311 3257 3754 1213 -753 118 N ATOM 212 NH1BARG A 57 -10.208 43.250 -9.663 0.46 20.34 N ANISOU 212 NH1BARG A 57 2567 2885 2275 311 -61 189 N ATOM 213 NH2AARG A 57 -10.065 47.731 -8.729 0.54 27.01 N ANISOU 213 NH2AARG A 57 2863 4077 3322 665 -645 432 N ATOM 214 NH2BARG A 57 -12.082 44.473 -9.137 0.46 24.75 N ANISOU 214 NH2BARG A 57 2904 3630 2870 47 -636 379 N ATOM 215 N SER A 58 -7.471 41.258 -12.445 1.00 15.81 N ANISOU 215 N SER A 58 2095 2087 1823 186 -31 -486 N ATOM 216 CA SER A 58 -8.482 40.194 -12.508 1.00 16.68 C ANISOU 216 CA SER A 58 2242 2235 1858 117 101 -382 C ATOM 217 C SER A 58 -7.987 39.027 -11.687 1.00 15.12 C ANISOU 217 C SER A 58 1866 2030 1847 115 120 -376 C ATOM 218 O SER A 58 -8.787 38.318 -11.075 1.00 17.41 O ANISOU 218 O SER A 58 1909 2522 2181 35 347 -408 O ATOM 219 CB SER A 58 -8.764 39.762 -13.953 1.00 17.33 C ANISOU 219 CB SER A 58 2221 2362 2002 78 -190 -499 C ATOM 220 OG SER A 58 -9.467 40.774 -14.632 1.00 22.26 O ANISOU 220 OG SER A 58 3110 2656 2688 283 -144 -333 O ATOM 221 N PHE A 59 -6.673 38.767 -11.709 1.00 15.18 N ANISOU 221 N PHE A 59 1861 1958 1945 87 218 -453 N ATOM 222 CA PHE A 59 -6.116 37.658 -10.952 1.00 13.21 C ANISOU 222 CA PHE A 59 1514 1753 1751 5 253 -354 C ATOM 223 C PHE A 59 -6.227 37.895 -9.462 1.00 12.71 C ANISOU 223 C PHE A 59 1487 1670 1669 -64 236 -150 C ATOM 224 O PHE A 59 -6.669 37.033 -8.694 1.00 13.64 O ANISOU 224 O PHE A 59 1687 1472 2022 -82 522 -208 O ATOM 225 CB PHE A 59 -4.648 37.389 -11.322 1.00 14.10 C ANISOU 225 CB PHE A 59 1530 1787 2040 112 226 -360 C ATOM 226 CG PHE A 59 -4.079 36.204 -10.631 1.00 16.07 C ANISOU 226 CG PHE A 59 1784 1948 2370 -86 481 -240 C ATOM 227 CD1 PHE A 59 -3.548 36.288 -9.361 1.00 18.18 C ANISOU 227 CD1 PHE A 59 2153 2242 2509 567 624 -49 C ATOM 228 CD2 PHE A 59 -4.066 34.985 -11.289 1.00 20.03 C ANISOU 228 CD2 PHE A 59 1933 1674 4003 9 -157 -365 C ATOM 229 CE1 PHE A 59 -3.078 35.135 -8.687 1.00 21.21 C ANISOU 229 CE1 PHE A 59 2126 2783 3147 416 1049 191 C ATOM 230 CE2 PHE A 59 -3.564 33.851 -10.641 1.00 22.21 C ANISOU 230 CE2 PHE A 59 2042 2547 3850 177 -184 272 C ATOM 231 CZ PHE A 59 -3.108 33.927 -9.329 1.00 20.85 C ANISOU 231 CZ PHE A 59 1875 2690 3354 201 569 -83 C ATOM 232 N PHE A 60 -5.837 39.097 -9.028 1.00 13.08 N ANISOU 232 N PHE A 60 1555 1615 1798 23 160 -284 N ATOM 233 CA PHE A 60 -5.770 39.369 -7.609 1.00 11.10 C ANISOU 233 CA PHE A 60 1243 1413 1559 -55 81 -63 C ATOM 234 C PHE A 60 -7.151 39.471 -6.966 1.00 11.40 C ANISOU 234 C PHE A 60 1323 1485 1524 30 60 -42 C ATOM 235 O PHE A 60 -7.251 39.405 -5.740 1.00 11.43 O ANISOU 235 O PHE A 60 1360 1432 1551 -63 133 -110 O ATOM 236 CB PHE A 60 -4.895 40.608 -7.327 1.00 11.51 C ANISOU 236 CB PHE A 60 1312 1347 1710 62 -32 -164 C ATOM 237 CG PHE A 60 -3.420 40.299 -7.283 1.00 12.21 C ANISOU 237 CG PHE A 60 1470 1652 1514 109 116 -127 C ATOM 238 CD1 PHE A 60 -2.681 40.148 -8.445 1.00 16.43 C ANISOU 238 CD1 PHE A 60 1943 2211 2085 559 528 -69 C ATOM 239 CD2 PHE A 60 -2.778 40.173 -6.078 1.00 15.69 C ANISOU 239 CD2 PHE A 60 1654 2562 1745 -195 -51 176 C ATOM 240 CE1 PHE A 60 -1.309 39.834 -8.383 1.00 16.07 C ANISOU 240 CE1 PHE A 60 2020 2189 1894 204 487 23 C ATOM 241 CE2 PHE A 60 -1.404 39.891 -6.024 1.00 16.51 C ANISOU 241 CE2 PHE A 60 1683 2651 1938 186 12 360 C ATOM 242 CZ PHE A 60 -0.674 39.731 -7.196 1.00 15.35 C ANISOU 242 CZ PHE A 60 1746 1971 2114 131 69 129 C ATOM 243 N ALA A 61 -8.190 39.585 -7.784 1.00 11.61 N ANISOU 243 N ALA A 61 1302 1554 1554 114 141 -69 N ATOM 244 CA ALA A 61 -9.568 39.532 -7.249 1.00 11.74 C ANISOU 244 CA ALA A 61 1245 1634 1579 22 -66 85 C ATOM 245 C ALA A 61 -9.854 38.225 -6.509 1.00 10.88 C ANISOU 245 C ALA A 61 1190 1456 1487 26 -77 15 C ATOM 246 O ALA A 61 -10.797 38.178 -5.701 1.00 12.05 O ANISOU 246 O ALA A 61 1220 1740 1618 -3 -70 178 O ATOM 247 CB ALA A 61 -10.583 39.699 -8.361 1.00 12.76 C ANISOU 247 CB ALA A 61 1425 1812 1611 225 -144 73 C ATOM 248 N ARG A 62 -9.073 37.159 -6.751 1.00 11.06 N ANISOU 248 N ARG A 62 1335 1341 1524 76 -68 53 N ATOM 249 CA ARG A 62 -9.294 35.909 -5.991 1.00 11.54 C ANISOU 249 CA ARG A 62 1349 1488 1545 20 -15 53 C ATOM 250 C ARG A 62 -9.087 36.097 -4.498 1.00 10.69 C ANISOU 250 C ARG A 62 1204 1336 1521 5 -18 91 C ATOM 251 O ARG A 62 -9.611 35.308 -3.707 1.00 12.12 O ANISOU 251 O ARG A 62 1492 1492 1620 -93 -58 120 O ATOM 252 CB ARG A 62 -8.400 34.766 -6.491 1.00 12.01 C ANISOU 252 CB ARG A 62 1381 1504 1678 86 -152 110 C ATOM 253 CG ARG A 62 -6.907 34.933 -6.238 1.00 12.27 C ANISOU 253 CG ARG A 62 1353 1634 1675 123 28 -173 C ATOM 254 CD ARG A 62 -6.106 33.800 -6.824 1.00 13.26 C ANISOU 254 CD ARG A 62 1562 1825 1651 229 241 2 C ATOM 255 NE ARG A 62 -6.311 32.541 -6.091 1.00 15.09 N ANISOU 255 NE ARG A 62 1810 1736 2186 -129 -36 -63 N ATOM 256 CZ ARG A 62 -6.517 31.328 -6.615 1.00 19.53 C ANISOU 256 CZ ARG A 62 2896 2210 2313 -300 -428 196 C ATOM 257 NH1 ARG A 62 -6.738 31.151 -7.921 1.00 20.32 N ANISOU 257 NH1 ARG A 62 2873 2381 2463 -146 -505 183 N ATOM 258 NH2 ARG A 62 -6.567 30.273 -5.820 1.00 22.76 N ANISOU 258 NH2 ARG A 62 3514 2520 2613 -379 -157 268 N ATOM 259 N TYR A 63 -8.339 37.143 -4.129 1.00 10.43 N ANISOU 259 N TYR A 63 1167 1349 1447 22 -143 -81 N ATOM 260 CA TYR A 63 -8.012 37.413 -2.701 1.00 11.59 C ANISOU 260 CA TYR A 63 1360 1442 1599 -203 -150 -48 C ATOM 261 C TYR A 63 -8.881 38.470 -2.059 1.00 11.36 C ANISOU 261 C TYR A 63 1336 1518 1460 -234 69 -76 C ATOM 262 O TYR A 63 -8.847 38.664 -0.835 1.00 11.74 O ANISOU 262 O TYR A 63 1478 1644 1336 -185 181 -66 O ATOM 263 CB TYR A 63 -6.544 37.895 -2.515 1.00 11.93 C ANISOU 263 CB TYR A 63 1380 1598 1552 -162 -30 -193 C ATOM 264 CG TYR A 63 -5.543 36.976 -3.191 1.00 12.63 C ANISOU 264 CG TYR A 63 1344 1658 1794 -78 -358 -307 C ATOM 265 CD1 TYR A 63 -5.280 35.706 -2.728 1.00 16.08 C ANISOU 265 CD1 TYR A 63 1628 2050 2432 191 -426 -271 C ATOM 266 CD2 TYR A 63 -4.845 37.438 -4.317 1.00 14.88 C ANISOU 266 CD2 TYR A 63 1403 2371 1878 -13 -34 -626 C ATOM 267 CE1 TYR A 63 -4.287 34.904 -3.401 1.00 15.40 C ANISOU 267 CE1 TYR A 63 1568 2060 2222 115 -233 -451 C ATOM 268 CE2 TYR A 63 -3.927 36.666 -4.993 1.00 15.47 C ANISOU 268 CE2 TYR A 63 1640 2023 2214 70 -323 -532 C ATOM 269 CZ TYR A 63 -3.655 35.426 -4.526 1.00 14.39 C ANISOU 269 CZ TYR A 63 1396 1865 2205 597 -246 -195 C ATOM 270 OH TYR A 63 -2.710 34.690 -5.256 1.00 20.16 O ANISOU 270 OH TYR A 63 1971 2967 2721 607 -137 -879 O ATOM 271 N GLY A 64 -9.661 39.197 -2.850 1.00 12.00 N ANISOU 271 N GLY A 64 1499 1411 1649 33 225 -86 N ATOM 272 CA GLY A 64 -10.431 40.282 -2.266 1.00 13.37 C ANISOU 272 CA GLY A 64 1655 1667 1758 41 327 -98 C ATOM 273 C GLY A 64 -10.843 41.338 -3.243 1.00 10.87 C ANISOU 273 C GLY A 64 1199 1433 1495 -148 90 -168 C ATOM 274 O GLY A 64 -10.767 41.132 -4.463 1.00 13.38 O ANISOU 274 O GLY A 64 1602 1851 1629 40 84 -211 O ATOM 275 N SER A 65 -11.314 42.449 -2.709 1.00 10.82 N ANISOU 275 N SER A 65 1213 1381 1515 60 12 -12 N ATOM 276 CA SER A 65 -11.752 43.579 -3.552 1.00 10.33 C ANISOU 276 CA SER A 65 1092 1333 1497 110 7 42 C ATOM 277 C SER A 65 -10.567 44.479 -3.773 1.00 10.34 C ANISOU 277 C SER A 65 1179 1416 1333 16 -55 -15 C ATOM 278 O SER A 65 -10.075 45.108 -2.835 1.00 11.40 O ANISOU 278 O SER A 65 1240 1502 1587 -35 -67 -81 O ATOM 279 CB SER A 65 -12.874 44.328 -2.861 1.00 12.34 C ANISOU 279 CB SER A 65 1354 1668 1667 276 22 -18 C ATOM 280 OG SER A 65 -13.272 45.397 -3.694 1.00 14.30 O ANISOU 280 OG SER A 65 1502 2089 1838 360 -23 288 O ATOM 281 N VAL A 66 -10.038 44.429 -4.986 1.00 10.79 N ANISOU 281 N VAL A 66 1170 1455 1473 -50 1 135 N ATOM 282 CA VAL A 66 -8.849 45.219 -5.337 1.00 11.45 C ANISOU 282 CA VAL A 66 1317 1459 1575 18 24 77 C ATOM 283 C VAL A 66 -9.156 46.707 -5.338 1.00 11.57 C ANISOU 283 C VAL A 66 1367 1431 1596 93 -97 131 C ATOM 284 O VAL A 66 -10.066 47.171 -6.046 1.00 14.77 O ANISOU 284 O VAL A 66 1684 1849 2076 75 -330 337 O ATOM 285 CB VAL A 66 -8.292 44.769 -6.710 1.00 11.35 C ANISOU 285 CB VAL A 66 1397 1353 1560 -107 164 57 C ATOM 286 CG1 VAL A 66 -7.157 45.701 -7.114 1.00 13.86 C ANISOU 286 CG1 VAL A 66 1694 1815 1756 -304 184 132 C ATOM 287 CG2 VAL A 66 -7.779 43.293 -6.623 1.00 13.89 C ANISOU 287 CG2 VAL A 66 1661 1694 1921 144 164 89 C ATOM 288 N LYS A 67 -8.383 47.463 -4.576 1.00 11.33 N ANISOU 288 N LYS A 67 1318 1317 1667 77 -13 13 N ATOM 289 CA LYS A 67 -8.503 48.916 -4.534 1.00 14.27 C ANISOU 289 CA LYS A 67 1754 1598 2067 128 -24 80 C ATOM 290 C LYS A 67 -7.750 49.570 -5.701 1.00 14.70 C ANISOU 290 C LYS A 67 1757 1564 2263 123 20 271 C ATOM 291 O LYS A 67 -8.322 50.343 -6.464 1.00 18.80 O ANISOU 291 O LYS A 67 2027 2258 2855 218 41 514 O ATOM 292 CB LYS A 67 -8.021 49.388 -3.158 1.00 15.24 C ANISOU 292 CB LYS A 67 1910 1677 2202 1 -188 -144 C ATOM 293 CG LYS A 67 -7.966 50.904 -2.959 1.00 17.81 C ANISOU 293 CG LYS A 67 2093 1865 2809 75 -68 -168 C ATOM 294 CD LYS A 67 -7.619 51.248 -1.512 1.00 22.70 C ANISOU 294 CD LYS A 67 3264 2066 3295 122 -273 -967 C ATOM 295 CE LYS A 67 -7.622 52.772 -1.281 1.00 30.28 C ANISOU 295 CE LYS A 67 4448 2747 4308 71 -157 -1210 C ATOM 296 NZ LYS A 67 -7.380 53.121 0.144 1.00 37.13 N ANISOU 296 NZ LYS A 67 5233 4215 4656 -246 -262 -1224 N ATOM 297 N GLU A 68 -6.494 49.200 -5.889 1.00 15.47 N ANISOU 297 N GLU A 68 1698 1912 2265 64 124 304 N ATOM 298 CA GLU A 68 -5.641 49.784 -6.898 1.00 16.57 C ANISOU 298 CA GLU A 68 1871 2018 2404 -25 8 272 C ATOM 299 C GLU A 68 -4.630 48.738 -7.399 1.00 14.43 C ANISOU 299 C GLU A 68 1660 1939 1881 94 -29 288 C ATOM 300 O GLU A 68 -4.116 47.952 -6.587 1.00 14.46 O ANISOU 300 O GLU A 68 1728 1903 1861 27 -93 444 O ATOM 301 CB GLU A 68 -4.882 50.931 -6.220 1.00 19.39 C ANISOU 301 CB GLU A 68 2462 2173 2731 54 33 79 C ATOM 302 CG GLU A 68 -3.994 51.742 -7.049 1.00 26.53 C ANISOU 302 CG GLU A 68 3340 3044 3695 -162 22 161 C ATOM 303 CD GLU A 68 -3.451 52.932 -6.242 1.00 30.21 C ANISOU 303 CD GLU A 68 3911 3403 4164 -898 -377 377 C ATOM 304 OE1 GLU A 68 -3.059 52.791 -5.048 1.00 32.89 O ANISOU 304 OE1 GLU A 68 4190 3942 4363 -1371 -575 494 O ATOM 305 OE2 GLU A 68 -3.404 54.015 -6.819 1.00 34.44 O ANISOU 305 OE2 GLU A 68 4412 3474 5199 230 -613 667 O ATOM 306 N VAL A 69 -4.371 48.722 -8.723 1.00 15.14 N ANISOU 306 N VAL A 69 1751 2095 1904 -68 -113 326 N ATOM 307 CA VAL A 69 -3.159 48.153 -9.303 1.00 15.11 C ANISOU 307 CA VAL A 69 1877 1960 1904 -187 -44 192 C ATOM 308 C VAL A 69 -2.338 49.310 -9.844 1.00 16.02 C ANISOU 308 C VAL A 69 1873 2034 2179 -130 -119 314 C ATOM 309 O VAL A 69 -2.725 49.933 -10.828 1.00 18.64 O ANISOU 309 O VAL A 69 2220 2485 2376 -206 -112 432 O ATOM 310 CB VAL A 69 -3.474 47.154 -10.445 1.00 15.89 C ANISOU 310 CB VAL A 69 2018 1974 2044 -322 -71 234 C ATOM 311 CG1 VAL A 69 -2.189 46.584 -11.036 1.00 18.52 C ANISOU 311 CG1 VAL A 69 2663 2451 1922 -256 191 48 C ATOM 312 CG2 VAL A 69 -4.404 46.087 -9.905 1.00 16.63 C ANISOU 312 CG2 VAL A 69 1954 2142 2221 -617 -275 149 C ATOM 313 N LYS A 70 -1.245 49.644 -9.168 1.00 14.86 N ANISOU 313 N LYS A 70 1635 1789 2221 -130 -27 329 N ATOM 314 CA LYS A 70 -0.507 50.887 -9.437 1.00 15.85 C ANISOU 314 CA LYS A 70 1761 1995 2264 -130 5 360 C ATOM 315 C LYS A 70 0.866 50.513 -9.925 1.00 16.09 C ANISOU 315 C LYS A 70 1856 2076 2181 -36 -12 457 C ATOM 316 O LYS A 70 1.702 50.048 -9.123 1.00 16.83 O ANISOU 316 O LYS A 70 1943 2273 2177 144 102 644 O ATOM 317 CB LYS A 70 -0.440 51.670 -8.118 1.00 17.34 C ANISOU 317 CB LYS A 70 2032 1994 2563 -255 -58 186 C ATOM 318 CG LYS A 70 0.273 53.011 -8.095 1.00 17.52 C ANISOU 318 CG LYS A 70 1971 2348 2338 -462 27 69 C ATOM 319 CD LYS A 70 0.128 53.629 -6.651 1.00 19.12 C ANISOU 319 CD LYS A 70 2408 2771 2084 -406 -351 97 C ATOM 320 CE LYS A 70 0.741 55.021 -6.389 1.00 19.87 C ANISOU 320 CE LYS A 70 2317 2143 3087 -81 223 275 C ATOM 321 NZ LYS A 70 2.141 55.034 -6.741 1.00 19.83 N ANISOU 321 NZ LYS A 70 2495 2421 2616 -335 78 169 N ATOM 322 N ILE A 71 1.118 50.717 -11.221 1.00 16.11 N ANISOU 322 N ILE A 71 1957 2007 2158 -73 7 323 N ATOM 323 CA ILE A 71 2.432 50.455 -11.816 1.00 16.20 C ANISOU 323 CA ILE A 71 2050 1971 2133 -48 49 353 C ATOM 324 C ILE A 71 3.289 51.707 -11.689 1.00 16.49 C ANISOU 324 C ILE A 71 1998 1886 2379 4 -55 404 C ATOM 325 O ILE A 71 2.808 52.812 -11.977 1.00 19.18 O ANISOU 325 O ILE A 71 2178 1964 3146 12 -169 711 O ATOM 326 CB ILE A 71 2.303 50.103 -13.294 1.00 18.33 C ANISOU 326 CB ILE A 71 2276 2367 2320 -176 -31 209 C ATOM 327 CG1 ILE A 71 1.290 48.987 -13.457 1.00 21.86 C ANISOU 327 CG1 ILE A 71 3179 2709 2418 -241 -129 16 C ATOM 328 CG2 ILE A 71 3.716 49.902 -13.963 1.00 19.02 C ANISOU 328 CG2 ILE A 71 2649 2762 1812 41 113 197 C ATOM 329 CD1 ILE A 71 1.678 47.770 -12.850 1.00 23.80 C ANISOU 329 CD1 ILE A 71 3436 2564 3040 -190 -365 -268 C ATOM 330 N ILE A 72 4.515 51.551 -11.210 1.00 13.90 N ANISOU 330 N ILE A 72 1732 1794 1752 -79 164 231 N ATOM 331 CA ILE A 72 5.407 52.681 -11.022 1.00 12.66 C ANISOU 331 CA ILE A 72 1673 1590 1545 -54 136 268 C ATOM 332 C ILE A 72 6.106 53.044 -12.338 1.00 13.31 C ANISOU 332 C ILE A 72 1837 1593 1624 93 239 238 C ATOM 333 O ILE A 72 6.592 52.137 -13.067 1.00 13.36 O ANISOU 333 O ILE A 72 2008 1559 1507 66 284 270 O ATOM 334 CB ILE A 72 6.442 52.374 -9.936 1.00 12.34 C ANISOU 334 CB ILE A 72 1707 1604 1376 -71 107 142 C ATOM 335 CG1 ILE A 72 5.743 51.970 -8.614 1.00 12.77 C ANISOU 335 CG1 ILE A 72 1840 1477 1534 -3 420 84 C ATOM 336 CG2 ILE A 72 7.396 53.556 -9.732 1.00 14.61 C ANISOU 336 CG2 ILE A 72 1646 1990 1912 -332 -40 279 C ATOM 337 CD1 ILE A 72 4.656 52.913 -8.151 1.00 13.05 C ANISOU 337 CD1 ILE A 72 1693 1495 1769 27 31 278 C ATOM 338 N THR A 73 6.059 54.335 -12.689 1.00 13.37 N ANISOU 338 N THR A 73 1864 1598 1614 13 387 383 N ATOM 339 CA THR A 73 6.727 54.843 -13.914 1.00 14.85 C ANISOU 339 CA THR A 73 2229 1866 1545 103 198 434 C ATOM 340 C THR A 73 7.717 55.911 -13.585 1.00 14.96 C ANISOU 340 C THR A 73 2131 1910 1643 31 406 308 C ATOM 341 O THR A 73 7.613 56.538 -12.544 1.00 16.21 O ANISOU 341 O THR A 73 2353 1984 1821 -383 593 365 O ATOM 342 CB THR A 73 5.729 55.438 -14.921 1.00 17.56 C ANISOU 342 CB THR A 73 2356 2279 2035 197 0 352 C ATOM 343 OG1 THR A 73 4.988 56.481 -14.270 1.00 21.23 O ANISOU 343 OG1 THR A 73 3308 2297 2459 418 -228 110 O ATOM 344 CG2 THR A 73 4.765 54.382 -15.397 1.00 18.36 C ANISOU 344 CG2 THR A 73 2552 2378 2045 140 -172 296 C ATOM 345 N ASP A 74 8.660 56.160 -14.502 1.00 14.61 N ANISOU 345 N ASP A 74 2021 1869 1658 -36 323 418 N ATOM 346 CA ASP A 74 9.528 57.341 -14.374 1.00 14.86 C ANISOU 346 CA ASP A 74 1947 1957 1742 5 307 521 C ATOM 347 C ASP A 74 8.801 58.587 -14.874 1.00 15.10 C ANISOU 347 C ASP A 74 1903 1988 1845 35 210 304 C ATOM 348 O ASP A 74 7.632 58.520 -15.276 1.00 14.64 O ANISOU 348 O ASP A 74 1953 2113 1494 0 334 357 O ATOM 349 CB ASP A 74 10.899 57.115 -15.028 1.00 14.96 C ANISOU 349 CB ASP A 74 1961 2021 1703 94 176 385 C ATOM 350 CG ASP A 74 10.870 57.100 -16.520 1.00 14.79 C ANISOU 350 CG ASP A 74 1757 2041 1820 122 226 349 C ATOM 351 OD1 ASP A 74 9.865 57.534 -17.125 1.00 16.87 O ANISOU 351 OD1 ASP A 74 2316 2222 1871 151 237 464 O ATOM 352 OD2 ASP A 74 11.916 56.704 -17.095 1.00 19.48 O ANISOU 352 OD2 ASP A 74 2346 2999 2054 556 351 184 O ATOM 353 N ARG A 75 9.510 59.714 -14.854 1.00 15.28 N ANISOU 353 N ARG A 75 2077 1868 1861 -60 325 580 N ATOM 354 CA ARG A 75 8.854 60.991 -15.124 1.00 16.09 C ANISOU 354 CA ARG A 75 2198 2054 1858 40 189 419 C ATOM 355 C ARG A 75 8.431 61.123 -16.592 1.00 15.61 C ANISOU 355 C ARG A 75 2008 2146 1776 107 391 363 C ATOM 356 O ARG A 75 7.629 61.983 -16.916 1.00 15.33 O ANISOU 356 O ARG A 75 2208 1824 1793 24 395 590 O ATOM 357 CB ARG A 75 9.778 62.150 -14.732 1.00 18.42 C ANISOU 357 CB ARG A 75 2631 2147 2219 -78 219 351 C ATOM 358 CG ARG A 75 11.071 62.155 -15.579 1.00 24.28 C ANISOU 358 CG ARG A 75 3069 3121 3035 -59 294 368 C ATOM 359 CD ARG A 75 11.852 63.454 -15.612 1.00 33.95 C ANISOU 359 CD ARG A 75 4243 3913 4744 -348 -54 123 C ATOM 360 NE ARG A 75 12.243 63.908 -14.297 1.00 40.14 N ANISOU 360 NE ARG A 75 5068 4909 5271 -237 21 -323 N ATOM 361 CZ ARG A 75 12.527 65.177 -14.011 1.00 44.49 C ANISOU 361 CZ ARG A 75 5812 5206 5885 -286 14 -252 C ATOM 362 NH1 ARG A 75 12.440 66.122 -14.956 1.00 45.65 N ANISOU 362 NH1 ARG A 75 5937 5492 5913 -181 171 -142 N ATOM 363 NH2 ARG A 75 12.885 65.506 -12.775 1.00 46.44 N ANISOU 363 NH2 ARG A 75 5986 5711 5948 -224 -113 -292 N ATOM 364 N THR A 76 8.982 60.271 -17.454 1.00 16.23 N ANISOU 364 N THR A 76 2211 2196 1757 170 360 364 N ATOM 365 CA THR A 76 8.605 60.260 -18.856 1.00 17.26 C ANISOU 365 CA THR A 76 2356 2305 1896 339 341 197 C ATOM 366 C THR A 76 7.557 59.189 -19.144 1.00 15.61 C ANISOU 366 C THR A 76 2123 2160 1645 331 327 235 C ATOM 367 O THR A 76 7.227 58.907 -20.305 1.00 18.38 O ANISOU 367 O THR A 76 2719 2429 1833 624 112 176 O ATOM 368 CB THR A 76 9.821 60.181 -19.781 1.00 17.03 C ANISOU 368 CB THR A 76 2261 2164 2043 253 371 449 C ATOM 369 OG1 THR A 76 10.759 59.243 -19.263 1.00 21.01 O ANISOU 369 OG1 THR A 76 2885 2874 2222 493 539 552 O ATOM 370 CG2 THR A 76 10.535 61.549 -19.864 1.00 18.90 C ANISOU 370 CG2 THR A 76 2519 2526 2135 -210 346 373 C ATOM 371 N GLY A 77 6.954 58.598 -18.100 1.00 16.79 N ANISOU 371 N GLY A 77 2181 2247 1952 441 473 225 N ATOM 372 CA GLY A 77 5.929 57.634 -18.329 1.00 16.89 C ANISOU 372 CA GLY A 77 2264 2390 1764 319 121 215 C ATOM 373 C GLY A 77 6.431 56.224 -18.608 1.00 17.32 C ANISOU 373 C GLY A 77 2199 2487 1893 235 138 145 C ATOM 374 O GLY A 77 5.629 55.358 -18.864 1.00 17.69 O ANISOU 374 O GLY A 77 2274 2479 1966 -4 200 220 O ATOM 375 N VAL A 78 7.744 55.956 -18.517 1.00 16.34 N ANISOU 375 N VAL A 78 2135 2281 1791 319 43 286 N ATOM 376 CA VAL A 78 8.293 54.631 -18.785 1.00 15.85 C ANISOU 376 CA VAL A 78 2219 2087 1714 95 73 369 C ATOM 377 C VAL A 78 8.200 53.749 -17.543 1.00 16.18 C ANISOU 377 C VAL A 78 2285 2115 1746 129 -75 247 C ATOM 378 O VAL A 78 8.682 54.120 -16.463 1.00 16.13 O ANISOU 378 O VAL A 78 2389 2146 1591 -8 19 167 O ATOM 379 CB VAL A 78 9.758 54.738 -19.308 1.00 16.07 C ANISOU 379 CB VAL A 78 2214 2202 1688 336 193 284 C ATOM 380 CG1 VAL A 78 10.313 53.361 -19.585 1.00 17.57 C ANISOU 380 CG1 VAL A 78 2694 2055 1926 235 204 335 C ATOM 381 CG2 VAL A 78 9.824 55.605 -20.586 1.00 18.54 C ANISOU 381 CG2 VAL A 78 2995 2290 1758 281 198 486 C ATOM 382 N SER A 79 7.556 52.593 -17.693 1.00 16.56 N ANISOU 382 N SER A 79 2365 2122 1802 -70 34 393 N ATOM 383 CA SER A 79 7.420 51.649 -16.551 1.00 16.43 C ANISOU 383 CA SER A 79 2281 2119 1842 -36 -28 324 C ATOM 384 C SER A 79 8.758 51.255 -15.934 1.00 16.29 C ANISOU 384 C SER A 79 2206 2132 1851 83 183 350 C ATOM 385 O SER A 79 9.742 51.001 -16.650 1.00 17.97 O ANISOU 385 O SER A 79 2328 2395 2104 -4 236 339 O ATOM 386 CB SER A 79 6.679 50.389 -16.999 1.00 18.14 C ANISOU 386 CB SER A 79 2372 2334 2184 -128 -94 243 C ATOM 387 OG SER A 79 6.663 49.408 -15.970 1.00 18.51 O ANISOU 387 OG SER A 79 2508 2346 2179 27 -44 142 O ATOM 388 N LYS A 80 8.788 51.197 -14.612 1.00 14.34 N ANISOU 388 N LYS A 80 1991 1860 1596 -17 118 356 N ATOM 389 CA LYS A 80 9.927 50.672 -13.917 1.00 14.53 C ANISOU 389 CA LYS A 80 1846 1858 1817 -14 231 316 C ATOM 390 C LYS A 80 9.856 49.170 -13.762 1.00 14.84 C ANISOU 390 C LYS A 80 1896 1998 1742 -5 236 273 C ATOM 391 O LYS A 80 10.765 48.597 -13.173 1.00 15.63 O ANISOU 391 O LYS A 80 1806 2148 1984 105 339 469 O ATOM 392 CB LYS A 80 10.088 51.357 -12.549 1.00 15.09 C ANISOU 392 CB LYS A 80 2035 1784 1912 -11 263 319 C ATOM 393 CG LYS A 80 10.261 52.903 -12.646 1.00 16.58 C ANISOU 393 CG LYS A 80 2298 1901 2099 -205 296 293 C ATOM 394 CD LYS A 80 10.813 53.525 -11.358 1.00 18.16 C ANISOU 394 CD LYS A 80 2596 2151 2149 -148 12 496 C ATOM 395 CE LYS A 80 10.806 55.027 -11.456 1.00 18.22 C ANISOU 395 CE LYS A 80 2445 2249 2226 -585 -57 200 C ATOM 396 NZ LYS A 80 11.451 55.637 -10.261 1.00 22.97 N ANISOU 396 NZ LYS A 80 3067 2971 2688 -579 -280 -162 N ATOM 397 N GLY A 81 8.779 48.551 -14.237 1.00 13.88 N ANISOU 397 N GLY A 81 1904 1755 1613 127 381 50 N ATOM 398 CA GLY A 81 8.675 47.094 -14.208 1.00 14.32 C ANISOU 398 CA GLY A 81 1982 1665 1794 52 343 99 C ATOM 399 C GLY A 81 8.182 46.521 -12.875 1.00 13.22 C ANISOU 399 C GLY A 81 1749 1521 1750 43 266 41 C ATOM 400 O GLY A 81 8.303 45.303 -12.641 1.00 14.11 O ANISOU 400 O GLY A 81 1953 1501 1905 32 138 -46 O ATOM 401 N TYR A 82 7.591 47.365 -12.022 1.00 12.40 N ANISOU 401 N TYR A 82 1588 1519 1604 75 338 138 N ATOM 402 CA TYR A 82 7.007 46.861 -10.778 1.00 11.80 C ANISOU 402 CA TYR A 82 1435 1505 1543 84 153 122 C ATOM 403 C TYR A 82 5.860 47.752 -10.395 1.00 11.97 C ANISOU 403 C TYR A 82 1639 1388 1521 -1 107 87 C ATOM 404 O TYR A 82 5.701 48.890 -10.931 1.00 12.70 O ANISOU 404 O TYR A 82 1690 1461 1673 72 65 233 O ATOM 405 CB TYR A 82 8.045 46.780 -9.617 1.00 12.31 C ANISOU 405 CB TYR A 82 1623 1443 1609 -9 -56 154 C ATOM 406 CG TYR A 82 8.596 48.115 -9.113 1.00 11.40 C ANISOU 406 CG TYR A 82 1487 1374 1471 -38 -78 252 C ATOM 407 CD1 TYR A 82 9.759 48.709 -9.674 1.00 12.29 C ANISOU 407 CD1 TYR A 82 1664 1473 1532 -19 -32 338 C ATOM 408 CD2 TYR A 82 7.951 48.791 -8.073 1.00 12.62 C ANISOU 408 CD2 TYR A 82 1745 1451 1597 65 -147 36 C ATOM 409 CE1 TYR A 82 10.230 49.937 -9.176 1.00 13.23 C ANISOU 409 CE1 TYR A 82 1955 1445 1625 -78 -173 403 C ATOM 410 CE2 TYR A 82 8.423 50.008 -7.573 1.00 13.13 C ANISOU 410 CE2 TYR A 82 1508 1646 1835 -229 -176 333 C ATOM 411 CZ TYR A 82 9.561 50.562 -8.124 1.00 13.55 C ANISOU 411 CZ TYR A 82 1734 1649 1765 -262 65 319 C ATOM 412 OH TYR A 82 9.982 51.754 -7.604 1.00 15.66 O ANISOU 412 OH TYR A 82 2053 1998 1898 -291 -50 204 O ATOM 413 N GLY A 83 5.036 47.230 -9.472 1.00 11.78 N ANISOU 413 N GLY A 83 1436 1464 1574 -28 147 24 N ATOM 414 CA GLY A 83 3.864 47.967 -9.028 1.00 11.88 C ANISOU 414 CA GLY A 83 1470 1543 1499 -40 97 143 C ATOM 415 C GLY A 83 3.314 47.369 -7.758 1.00 10.94 C ANISOU 415 C GLY A 83 1430 1424 1303 -39 -6 123 C ATOM 416 O GLY A 83 3.986 46.557 -7.099 1.00 11.62 O ANISOU 416 O GLY A 83 1417 1489 1507 41 -46 204 O ATOM 417 N PHE A 84 2.133 47.858 -7.355 1.00 11.04 N ANISOU 417 N PHE A 84 1331 1421 1441 -95 57 118 N ATOM 418 CA PHE A 84 1.531 47.488 -6.088 1.00 10.98 C ANISOU 418 CA PHE A 84 1266 1402 1501 -204 29 84 C ATOM 419 C PHE A 84 0.065 47.223 -6.232 1.00 11.47 C ANISOU 419 C PHE A 84 1223 1441 1692 -12 -95 310 C ATOM 420 O PHE A 84 -0.646 48.011 -6.847 1.00 12.57 O ANISOU 420 O PHE A 84 1282 1427 2067 47 -155 442 O ATOM 421 CB PHE A 84 1.705 48.625 -5.074 1.00 11.70 C ANISOU 421 CB PHE A 84 1373 1402 1669 6 36 73 C ATOM 422 CG PHE A 84 3.155 48.957 -4.818 1.00 10.94 C ANISOU 422 CG PHE A 84 1255 1425 1474 -69 -201 94 C ATOM 423 CD1 PHE A 84 3.860 48.279 -3.823 1.00 11.12 C ANISOU 423 CD1 PHE A 84 1387 1391 1443 36 -184 167 C ATOM 424 CD2 PHE A 84 3.866 49.864 -5.651 1.00 12.09 C ANISOU 424 CD2 PHE A 84 1489 1372 1732 -76 -62 23 C ATOM 425 CE1 PHE A 84 5.208 48.527 -3.596 1.00 11.64 C ANISOU 425 CE1 PHE A 84 1390 1426 1604 -79 118 182 C ATOM 426 CE2 PHE A 84 5.225 50.106 -5.442 1.00 12.07 C ANISOU 426 CE2 PHE A 84 1779 1367 1437 -120 -113 2 C ATOM 427 CZ PHE A 84 5.909 49.405 -4.415 1.00 10.85 C ANISOU 427 CZ PHE A 84 1373 1535 1212 -6 76 322 C ATOM 428 N VAL A 85 -0.382 46.135 -5.620 1.00 10.60 N ANISOU 428 N VAL A 85 1090 1398 1537 -169 -38 155 N ATOM 429 CA VAL A 85 -1.820 45.782 -5.611 1.00 10.83 C ANISOU 429 CA VAL A 85 1157 1460 1498 -97 -4 100 C ATOM 430 C VAL A 85 -2.312 45.968 -4.186 1.00 9.83 C ANISOU 430 C VAL A 85 1174 1192 1366 -47 -21 158 C ATOM 431 O VAL A 85 -1.760 45.377 -3.274 1.00 11.22 O ANISOU 431 O VAL A 85 1189 1602 1470 156 -36 184 O ATOM 432 CB VAL A 85 -2.070 44.315 -6.081 1.00 10.80 C ANISOU 432 CB VAL A 85 1224 1382 1496 -102 89 -58 C ATOM 433 CG1 VAL A 85 -3.560 44.004 -6.041 1.00 13.51 C ANISOU 433 CG1 VAL A 85 1461 1709 1962 -340 81 36 C ATOM 434 CG2 VAL A 85 -1.537 44.105 -7.485 1.00 13.95 C ANISOU 434 CG2 VAL A 85 1633 1883 1782 -192 226 -39 C ATOM 435 N SER A 86 -3.296 46.836 -3.982 1.00 10.33 N ANISOU 435 N SER A 86 1128 1340 1456 -74 156 -2 N ATOM 436 CA SER A 86 -3.853 47.031 -2.652 1.00 10.65 C ANISOU 436 CA SER A 86 1150 1435 1458 -83 14 0 C ATOM 437 C SER A 86 -5.303 46.582 -2.624 1.00 9.71 C ANISOU 437 C SER A 86 1116 1297 1275 -4 -48 54 C ATOM 438 O SER A 86 -5.976 46.520 -3.671 1.00 10.88 O ANISOU 438 O SER A 86 1068 1632 1435 77 -128 133 O ATOM 439 CB SER A 86 -3.709 48.494 -2.243 1.00 12.61 C ANISOU 439 CB SER A 86 1387 1522 1881 64 -12 -31 C ATOM 440 OG SER A 86 -4.380 49.289 -3.227 1.00 15.12 O ANISOU 440 OG SER A 86 1831 1678 2236 119 -5 96 O ATOM 441 N PHE A 87 -5.781 46.314 -1.401 1.00 10.22 N ANISOU 441 N PHE A 87 1200 1335 1347 -26 107 -8 N ATOM 442 CA PHE A 87 -7.123 45.712 -1.173 1.00 11.02 C ANISOU 442 CA PHE A 87 1213 1315 1656 14 32 -4 C ATOM 443 C PHE A 87 -7.951 46.539 -0.210 1.00 11.60 C ANISOU 443 C PHE A 87 1334 1522 1549 141 -32 -111 C ATOM 444 O PHE A 87 -7.393 47.147 0.732 1.00 11.95 O ANISOU 444 O PHE A 87 1338 1507 1695 10 -78 -124 O ATOM 445 CB PHE A 87 -6.994 44.291 -0.606 1.00 10.65 C ANISOU 445 CB PHE A 87 1128 1218 1698 -12 118 32 C ATOM 446 CG PHE A 87 -6.411 43.314 -1.589 1.00 10.31 C ANISOU 446 CG PHE A 87 1252 1309 1357 -51 270 -17 C ATOM 447 CD1 PHE A 87 -5.028 43.097 -1.709 1.00 12.39 C ANISOU 447 CD1 PHE A 87 1288 1659 1761 -8 275 134 C ATOM 448 CD2 PHE A 87 -7.271 42.596 -2.426 1.00 10.71 C ANISOU 448 CD2 PHE A 87 1315 1178 1574 -6 161 6 C ATOM 449 CE1 PHE A 87 -4.528 42.157 -2.624 1.00 12.59 C ANISOU 449 CE1 PHE A 87 1394 1652 1738 59 302 96 C ATOM 450 CE2 PHE A 87 -6.796 41.666 -3.350 1.00 11.76 C ANISOU 450 CE2 PHE A 87 1431 1504 1530 168 236 -70 C ATOM 451 CZ PHE A 87 -5.422 41.438 -3.458 1.00 12.13 C ANISOU 451 CZ PHE A 87 1381 1657 1570 77 178 216 C ATOM 452 N TYR A 88 -9.277 46.529 -0.419 1.00 11.56 N ANISOU 452 N TYR A 88 1293 1505 1592 215 60 -53 N ATOM 453 CA TYR A 88 -10.187 47.109 0.554 1.00 11.22 C ANISOU 453 CA TYR A 88 1229 1450 1581 194 168 -92 C ATOM 454 C TYR A 88 -10.341 46.225 1.762 1.00 12.29 C ANISOU 454 C TYR A 88 1429 1449 1788 11 206 -80 C ATOM 455 O TYR A 88 -10.489 46.736 2.887 1.00 14.90 O ANISOU 455 O TYR A 88 2120 1580 1959 14 295 -166 O ATOM 456 CB TYR A 88 -11.559 47.359 -0.079 1.00 12.80 C ANISOU 456 CB TYR A 88 1359 1649 1855 161 67 23 C ATOM 457 CG TYR A 88 -11.576 48.483 -1.060 1.00 14.02 C ANISOU 457 CG TYR A 88 1526 1845 1954 214 103 54 C ATOM 458 CD1 TYR A 88 -11.393 49.806 -0.645 1.00 16.93 C ANISOU 458 CD1 TYR A 88 2142 2031 2260 469 -269 126 C ATOM 459 CD2 TYR A 88 -11.807 48.230 -2.414 1.00 13.82 C ANISOU 459 CD2 TYR A 88 1337 1944 1970 351 72 158 C ATOM 460 CE1 TYR A 88 -11.443 50.871 -1.588 1.00 18.90 C ANISOU 460 CE1 TYR A 88 2577 2033 2572 464 -74 386 C ATOM 461 CE2 TYR A 88 -11.854 49.267 -3.361 1.00 16.12 C ANISOU 461 CE2 TYR A 88 1664 2356 2105 325 41 305 C ATOM 462 CZ TYR A 88 -11.665 50.589 -2.932 1.00 17.17 C ANISOU 462 CZ TYR A 88 1898 2057 2569 451 1 617 C ATOM 463 OH TYR A 88 -11.699 51.632 -3.843 1.00 23.52 O ANISOU 463 OH TYR A 88 2881 2719 3336 422 -151 1031 O ATOM 464 N ASN A 89 -10.354 44.926 1.552 1.00 11.86 N ANISOU 464 N ASN A 89 1283 1503 1719 24 184 -103 N ATOM 465 CA ASN A 89 -10.455 43.969 2.648 1.00 10.78 C ANISOU 465 CA ASN A 89 1190 1481 1422 5 19 -100 C ATOM 466 C ASN A 89 -9.076 43.655 3.266 1.00 11.52 C ANISOU 466 C ASN A 89 1323 1520 1532 43 6 93 C ATOM 467 O ASN A 89 -8.056 43.908 2.636 1.00 12.64 O ANISOU 467 O ASN A 89 1301 1653 1848 51 106 283 O ATOM 468 CB ASN A 89 -11.123 42.663 2.160 1.00 10.91 C ANISOU 468 CB ASN A 89 1250 1412 1482 -91 157 -148 C ATOM 469 CG ASN A 89 -10.379 41.995 1.024 1.00 9.48 C ANISOU 469 CG ASN A 89 1056 1257 1288 -69 -32 -14 C ATOM 470 OD1 ASN A 89 -10.127 42.599 -0.035 1.00 10.55 O ANISOU 470 OD1 ASN A 89 1288 1336 1381 -76 -111 -16 O ATOM 471 ND2 ASN A 89 -10.023 40.737 1.254 1.00 10.33 N ANISOU 471 ND2 ASN A 89 1092 1318 1514 -9 -112 68 N ATOM 472 N ASP A 90 -9.068 43.123 4.481 1.00 11.98 N ANISOU 472 N ASP A 90 1330 1472 1748 75 -90 125 N ATOM 473 CA ASP A 90 -7.854 42.553 5.047 1.00 11.67 C ANISOU 473 CA ASP A 90 1341 1506 1586 165 -105 221 C ATOM 474 C ASP A 90 -7.459 41.285 4.343 1.00 11.98 C ANISOU 474 C ASP A 90 1350 1602 1600 63 54 135 C ATOM 475 O ASP A 90 -8.255 40.372 4.184 1.00 11.71 O ANISOU 475 O ASP A 90 1142 1666 1640 105 -124 45 O ATOM 476 CB ASP A 90 -8.052 42.295 6.525 1.00 13.37 C ANISOU 476 CB ASP A 90 1529 1855 1696 -53 83 -71 C ATOM 477 CG ASP A 90 -8.415 43.554 7.259 1.00 15.15 C ANISOU 477 CG ASP A 90 2012 1958 1787 -42 493 -41 C ATOM 478 OD1 ASP A 90 -7.738 44.575 7.110 1.00 16.99 O ANISOU 478 OD1 ASP A 90 2129 2257 2067 -366 295 -258 O ATOM 479 OD2 ASP A 90 -9.451 43.546 7.951 1.00 21.03 O ANISOU 479 OD2 ASP A 90 2123 3131 2734 -118 825 -355 O ATOM 480 N VAL A 91 -6.218 41.241 3.867 1.00 12.44 N ANISOU 480 N VAL A 91 1342 1654 1731 107 129 188 N ATOM 481 CA VAL A 91 -5.655 40.057 3.245 1.00 12.60 C ANISOU 481 CA VAL A 91 1414 1653 1721 115 -54 178 C ATOM 482 C VAL A 91 -4.449 39.600 4.052 1.00 12.17 C ANISOU 482 C VAL A 91 1273 1596 1752 25 52 96 C ATOM 483 O VAL A 91 -3.850 40.396 4.777 1.00 13.58 O ANISOU 483 O VAL A 91 1405 1695 2059 100 33 -13 O ATOM 484 CB VAL A 91 -5.244 40.327 1.762 1.00 12.39 C ANISOU 484 CB VAL A 91 1427 1498 1782 43 -79 150 C ATOM 485 CG1 VAL A 91 -6.492 40.599 0.935 1.00 12.72 C ANISOU 485 CG1 VAL A 91 1205 1759 1867 215 -314 12 C ATOM 486 CG2 VAL A 91 -4.274 41.467 1.639 1.00 11.86 C ANISOU 486 CG2 VAL A 91 1178 1499 1826 -154 -36 185 C ATOM 487 N ASP A 92 -4.092 38.321 3.886 1.00 12.69 N ANISOU 487 N ASP A 92 1307 1636 1876 127 105 373 N ATOM 488 CA ASP A 92 -2.850 37.827 4.502 1.00 12.40 C ANISOU 488 CA ASP A 92 1321 1643 1747 12 69 283 C ATOM 489 C ASP A 92 -1.768 37.976 3.407 1.00 12.47 C ANISOU 489 C ASP A 92 1345 1650 1741 44 9 150 C ATOM 490 O ASP A 92 -1.588 37.102 2.555 1.00 12.23 O ANISOU 490 O ASP A 92 1314 1566 1767 -77 -60 164 O ATOM 491 CB ASP A 92 -3.061 36.365 4.917 1.00 13.31 C ANISOU 491 CB ASP A 92 1428 1640 1988 188 17 363 C ATOM 492 CG ASP A 92 -1.842 35.745 5.574 1.00 13.39 C ANISOU 492 CG ASP A 92 1417 1810 1858 -204 -121 496 C ATOM 493 OD1 ASP A 92 -0.762 36.356 5.504 1.00 14.26 O ANISOU 493 OD1 ASP A 92 1388 1996 2033 -245 3 369 O ATOM 494 OD2 ASP A 92 -1.982 34.638 6.122 1.00 15.40 O ANISOU 494 OD2 ASP A 92 1553 2048 2248 -77 44 537 O ATOM 495 N VAL A 93 -0.993 39.053 3.503 1.00 11.91 N ANISOU 495 N VAL A 93 1126 1628 1772 -35 139 209 N ATOM 496 CA VAL A 93 0.032 39.343 2.519 1.00 12.06 C ANISOU 496 CA VAL A 93 1262 1598 1722 -86 129 159 C ATOM 497 C VAL A 93 1.052 38.195 2.486 1.00 11.62 C ANISOU 497 C VAL A 93 1251 1565 1598 -123 42 124 C ATOM 498 O VAL A 93 1.580 37.849 1.428 1.00 12.88 O ANISOU 498 O VAL A 93 1404 1713 1775 -321 230 147 O ATOM 499 CB VAL A 93 0.674 40.705 2.824 1.00 12.13 C ANISOU 499 CB VAL A 93 1109 1619 1879 -42 25 182 C ATOM 500 CG1 VAL A 93 1.939 40.911 1.982 1.00 13.18 C ANISOU 500 CG1 VAL A 93 1344 1970 1690 -226 282 283 C ATOM 501 CG2 VAL A 93 -0.294 41.836 2.494 1.00 13.48 C ANISOU 501 CG2 VAL A 93 1127 1756 2238 35 -80 293 C ATOM 502 N GLN A 94 1.431 37.685 3.663 1.00 12.31 N ANISOU 502 N GLN A 94 1243 1693 1741 95 151 232 N ATOM 503 CA AGLN A 94 2.411 36.604 3.733 0.54 12.90 C ANISOU 503 CA AGLN A 94 1286 1792 1821 210 175 124 C ATOM 504 CA BGLN A 94 2.403 36.584 3.733 0.46 13.25 C ANISOU 504 CA BGLN A 94 1358 1789 1885 216 191 156 C ATOM 505 C GLN A 94 1.965 35.415 2.878 1.00 13.00 C ANISOU 505 C GLN A 94 1270 1694 1973 184 230 121 C ATOM 506 O GLN A 94 2.757 34.799 2.181 1.00 14.52 O ANISOU 506 O GLN A 94 1349 1870 2295 101 368 39 O ATOM 507 CB AGLN A 94 2.677 36.241 5.206 0.54 13.53 C ANISOU 507 CB AGLN A 94 1356 1942 1840 320 66 78 C ATOM 508 CB BGLN A 94 2.639 36.123 5.176 0.46 14.21 C ANISOU 508 CB BGLN A 94 1492 1964 1943 299 100 154 C ATOM 509 CG AGLN A 94 3.407 37.361 5.993 0.54 15.02 C ANISOU 509 CG AGLN A 94 1620 2008 2079 255 83 -122 C ATOM 510 CG BGLN A 94 3.804 35.150 5.280 0.46 16.36 C ANISOU 510 CG BGLN A 94 1983 1977 2256 456 185 134 C ATOM 511 CD AGLN A 94 4.916 37.323 5.827 0.54 14.20 C ANISOU 511 CD AGLN A 94 1561 1644 2191 82 195 -198 C ATOM 512 CD BGLN A 94 4.435 35.129 6.657 0.46 20.49 C ANISOU 512 CD BGLN A 94 2586 2434 2763 240 -136 21 C ATOM 513 OE1AGLN A 94 5.630 38.323 5.439 0.54 14.02 O ANISOU 513 OE1AGLN A 94 1704 1614 2009 -170 -22 -203 O ATOM 514 OE1BGLN A 94 5.165 36.051 7.057 0.46 21.38 O ANISOU 514 OE1BGLN A 94 2154 3238 2728 132 -175 -230 O ATOM 515 NE2AGLN A 94 5.444 36.138 6.114 0.54 13.68 N ANISOU 515 NE2AGLN A 94 1356 1868 1971 33 61 265 N ATOM 516 NE2BGLN A 94 4.175 34.068 7.384 0.46 22.89 N ANISOU 516 NE2BGLN A 94 3179 2653 2862 -13 45 315 N ATOM 517 N LYS A 95 0.695 35.040 2.959 1.00 13.18 N ANISOU 517 N LYS A 95 1261 1707 2039 60 217 246 N ATOM 518 CA LYS A 95 0.190 33.974 2.131 1.00 14.15 C ANISOU 518 CA LYS A 95 1321 1867 2185 23 250 70 C ATOM 519 C LYS A 95 0.130 34.332 0.640 1.00 12.97 C ANISOU 519 C LYS A 95 1223 1615 2087 -115 191 -80 C ATOM 520 O LYS A 95 0.536 33.534 -0.220 1.00 14.33 O ANISOU 520 O LYS A 95 1484 1790 2168 -124 320 0 O ATOM 521 CB LYS A 95 -1.181 33.511 2.656 1.00 16.09 C ANISOU 521 CB LYS A 95 1445 2005 2662 13 286 -18 C ATOM 522 CG LYS A 95 -1.773 32.355 1.972 1.00 18.87 C ANISOU 522 CG LYS A 95 1992 2462 2714 97 126 32 C ATOM 523 CD LYS A 95 -0.960 31.112 2.156 1.00 22.46 C ANISOU 523 CD LYS A 95 2477 2612 3443 342 -181 95 C ATOM 524 CE LYS A 95 -0.726 30.766 3.606 1.00 22.46 C ANISOU 524 CE LYS A 95 2410 2582 3539 636 -421 513 C ATOM 525 NZ LYS A 95 -0.101 29.396 3.736 1.00 29.27 N ANISOU 525 NZ LYS A 95 3294 2759 5068 408 -329 877 N ATOM 526 N ILE A 96 -0.328 35.550 0.331 1.00 12.96 N ANISOU 526 N ILE A 96 1095 1796 2032 -102 38 177 N ATOM 527 CA ILE A 96 -0.371 35.958 -1.081 1.00 13.75 C ANISOU 527 CA ILE A 96 1370 1823 2028 -81 -38 114 C ATOM 528 C ILE A 96 0.996 35.863 -1.759 1.00 12.82 C ANISOU 528 C ILE A 96 1414 1596 1861 -131 -63 38 C ATOM 529 O ILE A 96 1.110 35.415 -2.895 1.00 13.69 O ANISOU 529 O ILE A 96 1365 1896 1941 -234 -103 78 O ATOM 530 CB ILE A 96 -1.021 37.356 -1.275 1.00 14.14 C ANISOU 530 CB ILE A 96 1433 1796 2142 -169 -58 261 C ATOM 531 CG1 ILE A 96 -2.497 37.307 -0.805 1.00 15.86 C ANISOU 531 CG1 ILE A 96 1471 2105 2447 61 5 -91 C ATOM 532 CG2 ILE A 96 -0.911 37.811 -2.727 1.00 15.60 C ANISOU 532 CG2 ILE A 96 1929 1897 2100 -166 -382 156 C ATOM 533 CD1 ILE A 96 -3.160 38.678 -0.780 1.00 15.89 C ANISOU 533 CD1 ILE A 96 1653 2117 2265 183 -84 281 C ATOM 534 N VAL A 97 2.025 36.334 -1.043 1.00 11.78 N ANISOU 534 N VAL A 97 1149 1632 1693 -88 -91 220 N ATOM 535 CA VAL A 97 3.351 36.370 -1.669 1.00 13.06 C ANISOU 535 CA VAL A 97 1384 1724 1853 -152 32 51 C ATOM 536 C VAL A 97 3.948 34.993 -1.933 1.00 13.49 C ANISOU 536 C VAL A 97 1508 1889 1728 -115 -126 38 C ATOM 537 O VAL A 97 4.904 34.903 -2.671 1.00 13.99 O ANISOU 537 O VAL A 97 1322 2219 1771 -122 -63 -21 O ATOM 538 CB VAL A 97 4.344 37.216 -0.908 1.00 13.24 C ANISOU 538 CB VAL A 97 1482 1595 1953 -24 -300 116 C ATOM 539 CG1 VAL A 97 3.870 38.665 -0.773 1.00 13.71 C ANISOU 539 CG1 VAL A 97 1666 1568 1975 -201 -294 29 C ATOM 540 CG2 VAL A 97 4.780 36.639 0.385 1.00 15.12 C ANISOU 540 CG2 VAL A 97 1772 2018 1954 -98 -401 -13 C ATOM 541 N GLU A 98 3.341 33.934 -1.390 1.00 12.72 N ANISOU 541 N GLU A 98 1480 1609 1740 -35 -139 91 N ATOM 542 CA GLU A 98 3.727 32.567 -1.717 1.00 13.97 C ANISOU 542 CA GLU A 98 1675 1787 1845 -111 -21 13 C ATOM 543 C GLU A 98 3.240 32.122 -3.092 1.00 14.45 C ANISOU 543 C GLU A 98 1757 1814 1916 -97 116 -28 C ATOM 544 O GLU A 98 3.682 31.074 -3.576 1.00 16.95 O ANISOU 544 O GLU A 98 2231 2108 2101 -101 100 -191 O ATOM 545 CB GLU A 98 3.216 31.586 -0.646 1.00 13.50 C ANISOU 545 CB GLU A 98 1554 1682 1892 -10 -91 84 C ATOM 546 CG GLU A 98 3.855 31.831 0.717 1.00 12.64 C ANISOU 546 CG GLU A 98 1561 1622 1616 -61 40 185 C ATOM 547 CD GLU A 98 3.263 31.045 1.857 1.00 13.79 C ANISOU 547 CD GLU A 98 1586 1752 1902 -306 3 326 C ATOM 548 OE1 GLU A 98 2.394 30.169 1.624 1.00 18.86 O ANISOU 548 OE1 GLU A 98 2281 2287 2596 -699 -124 194 O ATOM 549 OE2 GLU A 98 3.699 31.279 3.016 1.00 16.29 O ANISOU 549 OE2 GLU A 98 2027 2139 2021 -459 -254 469 O ATOM 550 N SER A 99 2.294 32.860 -3.660 1.00 15.27 N ANISOU 550 N SER A 99 1706 2191 1902 -352 -3 -40 N ATOM 551 CA SER A 99 1.654 32.402 -4.914 1.00 16.51 C ANISOU 551 CA SER A 99 1916 2364 1991 -103 -34 -60 C ATOM 552 C SER A 99 2.602 32.396 -6.107 1.00 14.35 C ANISOU 552 C SER A 99 1683 1916 1853 -69 -97 29 C ATOM 553 O SER A 99 3.421 33.288 -6.246 1.00 14.87 O ANISOU 553 O SER A 99 1577 1849 2224 -84 -105 -24 O ATOM 554 CB SER A 99 0.474 33.300 -5.217 1.00 16.73 C ANISOU 554 CB SER A 99 1618 2702 2035 -158 9 -102 C ATOM 555 OG SER A 99 -0.502 33.213 -4.181 1.00 25.55 O ANISOU 555 OG SER A 99 2584 4238 2886 178 483 -129 O ATOM 556 N GLN A 100 2.459 31.403 -6.972 1.00 16.18 N ANISOU 556 N GLN A 100 2046 1916 2183 46 -214 9 N ATOM 557 CA GLN A 100 3.206 31.336 -8.212 1.00 16.78 C ANISOU 557 CA GLN A 100 2227 1882 2265 118 -88 -153 C ATOM 558 C GLN A 100 2.275 31.852 -9.287 1.00 17.17 C ANISOU 558 C GLN A 100 2186 2124 2213 -57 -132 -182 C ATOM 559 O GLN A 100 1.327 31.147 -9.689 1.00 19.69 O ANISOU 559 O GLN A 100 2443 2444 2592 -367 -217 -235 O ATOM 560 CB GLN A 100 3.583 29.879 -8.513 1.00 19.37 C ANISOU 560 CB GLN A 100 2698 2014 2646 327 -47 -173 C ATOM 561 CG GLN A 100 3.940 29.118 -7.268 1.00 26.53 C ANISOU 561 CG GLN A 100 3651 3195 3234 629 136 -7 C ATOM 562 CD GLN A 100 5.287 29.532 -6.737 1.00 30.21 C ANISOU 562 CD GLN A 100 3697 4092 3687 878 199 -208 C ATOM 563 OE1 GLN A 100 6.307 29.387 -7.414 1.00 35.29 O ANISOU 563 OE1 GLN A 100 4043 4958 4408 1068 595 -159 O ATOM 564 NE2 GLN A 100 5.309 30.063 -5.538 1.00 31.49 N ANISOU 564 NE2 GLN A 100 4075 4188 3700 1446 -47 -36 N ATOM 565 N ILE A 101 2.475 33.098 -9.689 1.00 15.71 N ANISOU 565 N ILE A 101 1849 2224 1894 79 119 10 N ATOM 566 CA ILE A 101 1.573 33.775 -10.628 1.00 16.28 C ANISOU 566 CA ILE A 101 1985 2175 2025 68 -11 -38 C ATOM 567 C ILE A 101 2.401 34.059 -11.888 1.00 15.96 C ANISOU 567 C ILE A 101 1961 2147 1954 32 69 -134 C ATOM 568 O ILE A 101 3.350 34.833 -11.845 1.00 16.19 O ANISOU 568 O ILE A 101 1892 2139 2120 -64 229 -347 O ATOM 569 CB ILE A 101 1.061 35.143 -10.017 1.00 16.33 C ANISOU 569 CB ILE A 101 1878 2255 2069 471 80 128 C ATOM 570 CG1 ILE A 101 0.483 34.962 -8.618 1.00 17.30 C ANISOU 570 CG1 ILE A 101 2165 2146 2263 249 -185 -431 C ATOM 571 CG2 ILE A 101 0.046 35.800 -10.977 1.00 17.93 C ANISOU 571 CG2 ILE A 101 1926 2391 2496 384 -218 329 C ATOM 572 CD1 ILE A 101 0.028 36.234 -7.881 1.00 20.74 C ANISOU 572 CD1 ILE A 101 2579 2584 2716 839 -179 -417 C ATOM 573 N ASN A 102 2.027 33.435 -13.009 1.00 16.62 N ANISOU 573 N ASN A 102 2149 2156 2009 127 77 -239 N ATOM 574 CA ASN A 102 2.706 33.669 -14.271 1.00 17.55 C ANISOU 574 CA ASN A 102 2419 2099 2148 256 70 -128 C ATOM 575 C ASN A 102 1.811 34.392 -15.282 1.00 16.12 C ANISOU 575 C ASN A 102 2209 1993 1920 90 42 -206 C ATOM 576 O ASN A 102 0.624 34.102 -15.381 1.00 18.19 O ANISOU 576 O ASN A 102 2515 2246 2148 -112 -154 -132 O ATOM 577 CB ASN A 102 3.209 32.335 -14.876 1.00 20.56 C ANISOU 577 CB ASN A 102 3030 2332 2448 289 -24 -262 C ATOM 578 CG ASN A 102 3.984 31.491 -13.873 1.00 24.95 C ANISOU 578 CG ASN A 102 3286 2794 3397 424 -142 -46 C ATOM 579 OD1 ASN A 102 5.116 31.797 -13.538 1.00 29.85 O ANISOU 579 OD1 ASN A 102 3522 2989 4831 386 -433 63 O ATOM 580 ND2 ASN A 102 3.357 30.433 -13.384 1.00 29.94 N ANISOU 580 ND2 ASN A 102 3809 3179 4385 440 -85 367 N ATOM 581 N PHE A 103 2.409 35.332 -16.026 1.00 16.34 N ANISOU 581 N PHE A 103 2240 2134 1833 24 157 -284 N ATOM 582 CA PHE A 103 1.773 35.920 -17.199 1.00 15.82 C ANISOU 582 CA PHE A 103 2062 2089 1860 -34 130 -299 C ATOM 583 C PHE A 103 2.805 36.020 -18.319 1.00 16.64 C ANISOU 583 C PHE A 103 2137 2318 1867 -214 133 -357 C ATOM 584 O PHE A 103 3.933 36.427 -18.074 1.00 17.32 O ANISOU 584 O PHE A 103 2097 2523 1961 -132 54 -311 O ATOM 585 CB PHE A 103 1.293 37.338 -16.889 1.00 15.70 C ANISOU 585 CB PHE A 103 2028 2067 1870 86 244 -171 C ATOM 586 CG PHE A 103 0.130 37.398 -15.955 1.00 13.78 C ANISOU 586 CG PHE A 103 1770 1922 1541 -118 5 -117 C ATOM 587 CD1 PHE A 103 -1.088 36.945 -16.370 1.00 15.71 C ANISOU 587 CD1 PHE A 103 1880 2164 1923 -224 -63 278 C ATOM 588 CD2 PHE A 103 0.290 37.830 -14.653 1.00 14.71 C ANISOU 588 CD2 PHE A 103 2097 1954 1536 141 33 -34 C ATOM 589 CE1 PHE A 103 -2.174 36.977 -15.558 1.00 18.64 C ANISOU 589 CE1 PHE A 103 1796 2945 2341 29 -113 254 C ATOM 590 CE2 PHE A 103 -0.819 37.890 -13.783 1.00 15.49 C ANISOU 590 CE2 PHE A 103 1886 1881 2118 44 2 40 C ATOM 591 CZ PHE A 103 -2.047 37.448 -14.234 1.00 16.88 C ANISOU 591 CZ PHE A 103 1699 2541 2172 -25 59 215 C ATOM 592 N HIS A 104 2.407 35.703 -19.558 1.00 17.72 N ANISOU 592 N HIS A 104 2377 2463 1889 -207 160 -310 N ATOM 593 CA HIS A 104 3.257 35.943 -20.734 1.00 18.56 C ANISOU 593 CA HIS A 104 2458 2554 2037 -163 260 -397 C ATOM 594 C HIS A 104 4.646 35.339 -20.588 1.00 19.98 C ANISOU 594 C HIS A 104 2606 2756 2227 -128 239 -391 C ATOM 595 O HIS A 104 5.654 35.959 -20.977 1.00 20.45 O ANISOU 595 O HIS A 104 2513 3108 2147 -154 398 -463 O ATOM 596 CB HIS A 104 3.215 37.437 -21.157 1.00 19.73 C ANISOU 596 CB HIS A 104 2567 2719 2208 -88 249 -336 C ATOM 597 CG HIS A 104 1.834 37.865 -21.516 1.00 18.82 C ANISOU 597 CG HIS A 104 2453 2774 1922 -311 60 -290 C ATOM 598 ND1 HIS A 104 1.339 37.756 -22.804 1.00 18.90 N ANISOU 598 ND1 HIS A 104 2792 2612 1774 -539 -187 -124 N ATOM 599 CD2 HIS A 104 0.799 38.281 -20.741 1.00 18.76 C ANISOU 599 CD2 HIS A 104 3070 2219 1835 -308 441 -417 C ATOM 600 CE1 HIS A 104 0.066 38.115 -22.803 1.00 19.41 C ANISOU 600 CE1 HIS A 104 2789 2537 2045 -359 316 -189 C ATOM 601 NE2 HIS A 104 -0.292 38.413 -21.557 1.00 17.37 N ANISOU 601 NE2 HIS A 104 3219 1903 1478 -433 438 -194 N ATOM 602 N GLY A 105 4.696 34.135 -20.021 1.00 19.72 N ANISOU 602 N GLY A 105 2569 2656 2267 -32 354 -546 N ATOM 603 CA GLY A 105 5.964 33.401 -19.875 1.00 20.72 C ANISOU 603 CA GLY A 105 2591 2826 2454 33 214 -504 C ATOM 604 C GLY A 105 6.892 33.840 -18.748 1.00 21.84 C ANISOU 604 C GLY A 105 2579 3099 2619 175 275 -490 C ATOM 605 O GLY A 105 8.040 33.362 -18.668 1.00 24.38 O ANISOU 605 O GLY A 105 2881 3343 3036 328 249 -542 O ATOM 606 N LYS A 106 6.394 34.710 -17.857 1.00 20.68 N ANISOU 606 N LYS A 106 2593 2916 2348 249 332 -452 N ATOM 607 CA LYS A 106 7.230 35.263 -16.801 1.00 20.89 C ANISOU 607 CA LYS A 106 2490 3052 2395 211 296 -349 C ATOM 608 C LYS A 106 6.510 35.118 -15.441 1.00 19.55 C ANISOU 608 C LYS A 106 2377 2866 2185 317 176 -246 C ATOM 609 O LYS A 106 5.279 35.279 -15.345 1.00 20.04 O ANISOU 609 O LYS A 106 2542 2942 2129 339 46 -268 O ATOM 610 CB LYS A 106 7.507 36.749 -17.065 1.00 21.46 C ANISOU 610 CB LYS A 106 2613 3192 2347 155 392 -230 C ATOM 611 CG LYS A 106 8.130 37.100 -18.409 1.00 27.42 C ANISOU 611 CG LYS A 106 3458 3973 2984 -11 375 -70 C ATOM 612 CD LYS A 106 9.566 36.741 -18.473 1.00 33.30 C ANISOU 612 CD LYS A 106 3905 4652 4094 226 440 25 C ATOM 613 CE LYS A 106 10.098 36.927 -19.894 1.00 38.17 C ANISOU 613 CE LYS A 106 4500 5429 4571 166 708 57 C ATOM 614 NZ LYS A 106 11.576 36.788 -19.899 1.00 41.86 N ANISOU 614 NZ LYS A 106 4670 5909 5324 237 458 206 N ATOM 615 N LYS A 107 7.270 34.830 -14.392 1.00 18.18 N ANISOU 615 N LYS A 107 2243 2650 2011 305 221 -247 N ATOM 616 CA LYS A 107 6.725 34.652 -13.049 1.00 16.75 C ANISOU 616 CA LYS A 107 2031 2331 2003 320 85 -157 C ATOM 617 C LYS A 107 6.839 35.965 -12.293 1.00 15.95 C ANISOU 617 C LYS A 107 1832 2113 2114 143 89 -190 C ATOM 618 O LYS A 107 7.916 36.545 -12.185 1.00 17.90 O ANISOU 618 O LYS A 107 1874 2525 2400 169 250 -230 O ATOM 619 CB LYS A 107 7.473 33.550 -12.302 1.00 17.25 C ANISOU 619 CB LYS A 107 2123 2317 2113 383 -104 -4 C ATOM 620 CG LYS A 107 6.978 33.306 -10.857 1.00 18.08 C ANISOU 620 CG LYS A 107 2276 2234 2357 637 35 -100 C ATOM 621 CD LYS A 107 7.877 32.273 -10.138 1.00 20.90 C ANISOU 621 CD LYS A 107 2765 2560 2613 496 -151 173 C ATOM 622 CE LYS A 107 7.504 32.249 -8.652 1.00 23.12 C ANISOU 622 CE LYS A 107 2619 3382 2783 365 -255 643 C ATOM 623 NZ LYS A 107 8.466 31.468 -7.900 1.00 27.36 N ANISOU 623 NZ LYS A 107 3456 3428 3509 610 -618 516 N ATOM 624 N LEU A 108 5.713 36.437 -11.736 1.00 13.63 N ANISOU 624 N LEU A 108 1565 1950 1663 225 121 -143 N ATOM 625 CA LEU A 108 5.738 37.648 -10.947 1.00 13.17 C ANISOU 625 CA LEU A 108 1583 1750 1671 84 66 -84 C ATOM 626 C LEU A 108 6.561 37.487 -9.690 1.00 12.32 C ANISOU 626 C LEU A 108 1437 1497 1744 68 96 -24 C ATOM 627 O LEU A 108 6.556 36.416 -9.055 1.00 13.39 O ANISOU 627 O LEU A 108 1653 1672 1760 71 -1 26 O ATOM 628 CB LEU A 108 4.323 38.111 -10.613 1.00 13.01 C ANISOU 628 CB LEU A 108 1495 1656 1790 232 -29 -155 C ATOM 629 CG LEU A 108 3.447 38.490 -11.820 1.00 14.68 C ANISOU 629 CG LEU A 108 1699 1964 1912 182 -111 -155 C ATOM 630 CD1 LEU A 108 2.076 38.915 -11.341 1.00 15.40 C ANISOU 630 CD1 LEU A 108 1460 2032 2359 286 -316 -378 C ATOM 631 CD2 LEU A 108 4.068 39.642 -12.585 1.00 17.76 C ANISOU 631 CD2 LEU A 108 2105 2489 2153 508 -252 337 C ATOM 632 N LYS A 109 7.252 38.565 -9.335 1.00 11.58 N ANISOU 632 N LYS A 109 1172 1692 1534 -23 24 -88 N ATOM 633 CA LYS A 109 8.129 38.568 -8.158 1.00 12.18 C ANISOU 633 CA LYS A 109 1409 1641 1577 18 42 -30 C ATOM 634 C LYS A 109 7.434 39.314 -7.018 1.00 12.21 C ANISOU 634 C LYS A 109 1492 1575 1570 110 138 66 C ATOM 635 O LYS A 109 7.315 40.543 -7.062 1.00 14.00 O ANISOU 635 O LYS A 109 1808 1622 1886 302 508 221 O ATOM 636 CB LYS A 109 9.417 39.282 -8.520 1.00 13.58 C ANISOU 636 CB LYS A 109 1436 2002 1719 25 267 -24 C ATOM 637 CG LYS A 109 10.166 38.570 -9.607 1.00 15.30 C ANISOU 637 CG LYS A 109 1566 2189 2055 68 138 -123 C ATOM 638 CD LYS A 109 11.348 39.409 -10.113 1.00 19.08 C ANISOU 638 CD LYS A 109 1655 2925 2668 -95 246 38 C ATOM 639 CE LYS A 109 12.009 38.707 -11.275 1.00 24.83 C ANISOU 639 CE LYS A 109 2613 3572 3249 217 310 -70 C ATOM 640 NZ LYS A 109 12.541 37.377 -10.883 1.00 30.15 N ANISOU 640 NZ LYS A 109 3077 3985 4392 211 465 -16 N ATOM 641 N LEU A 110 6.963 38.578 -6.023 1.00 11.03 N ANISOU 641 N LEU A 110 1240 1468 1482 80 75 62 N ATOM 642 CA LEU A 110 6.055 39.157 -5.048 1.00 10.92 C ANISOU 642 CA LEU A 110 1250 1445 1454 -4 122 53 C ATOM 643 C LEU A 110 6.769 39.479 -3.750 1.00 10.81 C ANISOU 643 C LEU A 110 1218 1513 1376 181 9 -12 C ATOM 644 O LEU A 110 7.728 38.795 -3.370 1.00 13.73 O ANISOU 644 O LEU A 110 1711 1917 1589 533 -22 -23 O ATOM 645 CB LEU A 110 4.918 38.173 -4.774 1.00 11.74 C ANISOU 645 CB LEU A 110 1488 1486 1486 -94 98 132 C ATOM 646 CG LEU A 110 4.132 37.717 -6.017 1.00 11.26 C ANISOU 646 CG LEU A 110 1175 1520 1583 -51 -23 260 C ATOM 647 CD1 LEU A 110 3.053 36.740 -5.609 1.00 14.05 C ANISOU 647 CD1 LEU A 110 1678 1600 2057 -199 -68 480 C ATOM 648 CD2 LEU A 110 3.519 38.906 -6.797 1.00 13.61 C ANISOU 648 CD2 LEU A 110 1407 1842 1922 44 -133 304 C ATOM 649 N GLY A 111 6.267 40.456 -3.010 1.00 9.66 N ANISOU 649 N GLY A 111 1082 1358 1229 -172 99 -104 N ATOM 650 CA GLY A 111 6.827 40.701 -1.666 1.00 9.66 C ANISOU 650 CA GLY A 111 1034 1307 1328 -30 35 -105 C ATOM 651 C GLY A 111 5.883 41.574 -0.844 1.00 9.25 C ANISOU 651 C GLY A 111 1005 1149 1358 14 22 179 C ATOM 652 O GLY A 111 4.979 42.209 -1.393 1.00 10.07 O ANISOU 652 O GLY A 111 1117 1285 1423 84 -24 223 O ATOM 653 N PRO A 112 6.134 41.701 0.472 1.00 10.07 N ANISOU 653 N PRO A 112 1095 1325 1403 5 1 87 N ATOM 654 CA PRO A 112 5.411 42.736 1.233 1.00 9.99 C ANISOU 654 CA PRO A 112 1279 1243 1272 -41 82 108 C ATOM 655 C PRO A 112 5.749 44.114 0.644 1.00 10.02 C ANISOU 655 C PRO A 112 1147 1268 1390 -123 63 66 C ATOM 656 O PRO A 112 6.836 44.318 0.069 1.00 11.38 O ANISOU 656 O PRO A 112 1168 1522 1633 35 89 303 O ATOM 657 CB PRO A 112 6.021 42.631 2.642 1.00 11.52 C ANISOU 657 CB PRO A 112 1459 1566 1352 0 -8 147 C ATOM 658 CG PRO A 112 6.554 41.150 2.679 1.00 11.65 C ANISOU 658 CG PRO A 112 1475 1546 1404 203 158 82 C ATOM 659 CD PRO A 112 7.092 40.946 1.290 1.00 10.39 C ANISOU 659 CD PRO A 112 1180 1387 1378 103 57 348 C ATOM 660 N ALA A 113 4.805 45.064 0.755 1.00 9.73 N ANISOU 660 N ALA A 113 1228 1126 1341 28 4 158 N ATOM 661 CA ALA A 113 5.002 46.408 0.188 1.00 9.85 C ANISOU 661 CA ALA A 113 1151 1248 1342 -20 -67 123 C ATOM 662 C ALA A 113 5.611 47.279 1.273 1.00 10.67 C ANISOU 662 C ALA A 113 1332 1422 1299 -10 -136 281 C ATOM 663 O ALA A 113 5.041 47.390 2.371 1.00 12.21 O ANISOU 663 O ALA A 113 1530 1670 1436 -257 -11 164 O ATOM 664 CB ALA A 113 3.671 46.950 -0.242 1.00 10.89 C ANISOU 664 CB ALA A 113 1189 1400 1548 289 -51 140 C ATOM 665 N ILE A 114 6.698 47.960 0.926 1.00 11.61 N ANISOU 665 N ILE A 114 1422 1376 1612 -157 -221 293 N ATOM 666 CA ILE A 114 7.422 48.843 1.854 1.00 12.70 C ANISOU 666 CA ILE A 114 1568 1488 1768 -222 -284 300 C ATOM 667 C ILE A 114 7.486 50.246 1.221 1.00 13.12 C ANISOU 667 C ILE A 114 1757 1578 1647 -77 -102 325 C ATOM 668 O ILE A 114 7.855 50.373 0.023 1.00 12.71 O ANISOU 668 O ILE A 114 1680 1577 1569 -265 -123 169 O ATOM 669 CB ILE A 114 8.804 48.259 2.176 1.00 15.10 C ANISOU 669 CB ILE A 114 1679 1789 2268 -314 -427 357 C ATOM 670 CG1 ILE A 114 8.588 47.006 3.099 1.00 17.89 C ANISOU 670 CG1 ILE A 114 1878 2448 2468 -205 -691 559 C ATOM 671 CG2 ILE A 114 9.690 49.244 2.921 1.00 17.80 C ANISOU 671 CG2 ILE A 114 1886 2427 2447 -743 -553 471 C ATOM 672 CD1 ILE A 114 9.868 46.486 3.648 1.00 19.70 C ANISOU 672 CD1 ILE A 114 2274 2967 2241 64 -751 416 C ATOM 673 N ARG A 115 7.040 51.256 1.992 1.00 14.85 N ANISOU 673 N ARG A 115 2239 1510 1892 -275 -70 220 N ATOM 674 CA AARG A 115 7.062 52.660 1.539 0.65 16.72 C ANISOU 674 CA AARG A 115 2474 1906 1970 -158 -39 252 C ATOM 675 CA BARG A 115 7.048 52.656 1.551 0.35 17.63 C ANISOU 675 CA BARG A 115 2581 2008 2107 -171 -69 207 C ATOM 676 C ARG A 115 8.118 53.393 2.306 1.00 18.70 C ANISOU 676 C ARG A 115 2825 2097 2181 -264 -1 162 C ATOM 677 O ARG A 115 8.042 53.530 3.530 1.00 18.70 O ANISOU 677 O ARG A 115 2948 2135 2021 -254 -127 63 O ATOM 678 CB AARG A 115 5.642 53.259 1.642 0.65 17.80 C ANISOU 678 CB AARG A 115 2570 1884 2306 -126 197 163 C ATOM 679 CB BARG A 115 5.673 53.309 1.767 0.35 18.75 C ANISOU 679 CB BARG A 115 2690 2059 2373 -133 82 141 C ATOM 680 CG AARG A 115 5.513 54.743 1.563 0.65 16.90 C ANISOU 680 CG AARG A 115 2619 2099 1701 126 -39 92 C ATOM 681 CG BARG A 115 5.322 54.334 0.712 0.35 21.14 C ANISOU 681 CG BARG A 115 2974 2733 2324 78 -229 72 C ATOM 682 CD AARG A 115 4.045 55.098 1.659 0.65 17.97 C ANISOU 682 CD AARG A 115 2570 2802 1456 136 18 89 C ATOM 683 CD BARG A 115 4.046 55.118 1.040 0.35 23.00 C ANISOU 683 CD BARG A 115 3085 3170 2484 159 24 121 C ATOM 684 NE AARG A 115 3.205 54.748 0.495 0.65 16.35 N ANISOU 684 NE AARG A 115 2481 2057 1674 -8 -93 432 N ATOM 685 NE BARG A 115 2.837 54.292 1.023 0.35 22.53 N ANISOU 685 NE BARG A 115 3167 3076 2316 86 93 424 N ATOM 686 CZ AARG A 115 3.337 55.295 -0.729 0.65 16.45 C ANISOU 686 CZ AARG A 115 2536 2174 1539 17 -195 338 C ATOM 687 CZ BARG A 115 1.940 54.258 0.041 0.35 22.21 C ANISOU 687 CZ BARG A 115 3106 2982 2348 108 58 178 C ATOM 688 NH1AARG A 115 4.279 56.171 -1.001 0.65 19.91 N ANISOU 688 NH1AARG A 115 2645 2645 2275 -16 -403 399 N ATOM 689 NH1BARG A 115 2.101 55.006 -1.037 0.35 22.66 N ANISOU 689 NH1BARG A 115 3211 3204 2192 545 -19 90 N ATOM 690 NH2AARG A 115 2.523 54.976 -1.704 0.65 17.18 N ANISOU 690 NH2AARG A 115 2618 2080 1830 -219 28 -132 N ATOM 691 NH2BARG A 115 0.874 53.466 0.137 0.35 18.99 N ANISOU 691 NH2BARG A 115 2564 3372 1277 80 -332 489 N ATOM 692 N LYS A 116 9.145 53.803 1.576 1.00 20.85 N ANISOU 692 N LYS A 116 2861 2628 2432 -448 -150 15 N ATOM 693 CA LYS A 116 10.160 54.684 2.134 1.00 24.38 C ANISOU 693 CA LYS A 116 3136 3015 3109 -339 -221 -145 C ATOM 694 C LYS A 116 9.670 56.164 2.084 1.00 27.10 C ANISOU 694 C LYS A 116 3531 3233 3531 -237 -244 -55 C ATOM 695 O LYS A 116 8.626 56.484 1.495 1.00 27.13 O ANISOU 695 O LYS A 116 3660 3040 3606 -236 -280 -106 O ATOM 696 CB LYS A 116 11.476 54.506 1.369 1.00 24.93 C ANISOU 696 CB LYS A 116 2988 3354 3129 -388 -346 -191 C ATOM 697 CG LYS A 116 11.964 53.095 1.348 1.00 25.44 C ANISOU 697 CG LYS A 116 2688 3696 3280 -357 -412 -99 C ATOM 698 CD LYS A 116 12.877 52.906 0.184 1.00 28.40 C ANISOU 698 CD LYS A 116 3271 4162 3355 103 -300 10 C ATOM 699 CE LYS A 116 13.315 51.486 0.066 1.00 31.75 C ANISOU 699 CE LYS A 116 3775 4236 4052 112 -340 -89 C ATOM 700 NZ LYS A 116 14.466 51.490 -0.879 1.00 36.59 N ANISOU 700 NZ LYS A 116 4127 5084 4692 129 -71 211 N ATOM 701 N GLN A 117 10.415 57.050 2.721 1.00 30.95 N ANISOU 701 N GLN A 117 4049 3747 3960 -166 -257 -196 N ATOM 702 CA GLN A 117 10.169 58.491 2.600 1.00 32.24 C ANISOU 702 CA GLN A 117 4204 3858 4186 -92 -185 -138 C ATOM 703 C GLN A 117 10.168 58.966 1.146 1.00 32.61 C ANISOU 703 C GLN A 117 4209 4041 4141 -117 -125 -222 C ATOM 704 O GLN A 117 10.944 58.470 0.305 1.00 35.11 O ANISOU 704 O GLN A 117 4326 4382 4629 -147 -58 -154 O ATOM 705 CB GLN A 117 11.236 59.269 3.370 1.00 32.83 C ANISOU 705 CB GLN A 117 4306 4052 4114 -59 -288 -180 C ATOM 706 N HIS A 123 6.534 67.271 -7.133 0.75 25.20 N ANISOU 706 N HIS A 123 3339 3138 3097 -129 -265 -53 N ATOM 707 CA HIS A 123 5.856 66.272 -7.953 0.75 23.43 C ANISOU 707 CA HIS A 123 3122 2887 2893 -12 -266 65 C ATOM 708 C HIS A 123 6.832 65.360 -8.678 0.75 23.62 C ANISOU 708 C HIS A 123 3161 2810 3002 -66 -179 61 C ATOM 709 O HIS A 123 6.744 64.138 -8.555 0.75 25.06 O ANISOU 709 O HIS A 123 3263 2928 3328 -77 -162 126 O ATOM 710 CB HIS A 123 4.954 66.934 -8.985 0.75 23.21 C ANISOU 710 CB HIS A 123 3155 2834 2828 47 -243 70 C ATOM 711 CG HIS A 123 3.672 67.427 -8.414 1.00 23.45 C ANISOU 711 CG HIS A 123 3231 2866 2812 165 -262 15 C ATOM 712 ND1 HIS A 123 2.491 66.719 -8.486 1.00 20.32 N ANISOU 712 ND1 HIS A 123 3234 2236 2249 30 34 232 N ATOM 713 CD2 HIS A 123 3.396 68.561 -7.727 1.00 24.65 C ANISOU 713 CD2 HIS A 123 3674 2448 3244 302 -145 -93 C ATOM 714 CE1 HIS A 123 1.527 67.431 -7.925 1.00 25.64 C ANISOU 714 CE1 HIS A 123 3868 2663 3208 468 -73 -102 C ATOM 715 NE2 HIS A 123 2.056 68.543 -7.441 1.00 25.27 N ANISOU 715 NE2 HIS A 123 3728 2847 3024 30 -232 245 N ATOM 716 N VAL A 124 7.749 65.956 -9.444 0.75 24.28 N ANISOU 716 N VAL A 124 3289 2976 2961 -130 -232 179 N TER 717 VAL A 124 ATOM 718 O3' U B 2 14.286 46.908 -12.319 0.50 25.75 O ANISOU 718 O3' U B 2 2696 4258 2828 -520 1103 940 O ATOM 719 P G B 3 14.974 47.207 -10.880 1.00 31.86 P ANISOU 719 P G B 3 3474 4848 3782 -514 720 626 P ATOM 720 OP1 G B 3 14.875 48.685 -10.624 1.00 33.81 O ANISOU 720 OP1 G B 3 3521 5019 4304 -312 215 388 O ATOM 721 OP2 G B 3 16.290 46.608 -10.857 1.00 32.56 O ANISOU 721 OP2 G B 3 3575 4827 3966 368 614 495 O ATOM 722 O5' G B 3 14.143 46.398 -9.777 1.00 21.44 O ANISOU 722 O5' G B 3 2458 3295 2394 -540 789 513 O ATOM 723 C5' G B 3 12.999 47.043 -9.314 1.00 21.09 C ANISOU 723 C5' G B 3 2827 2628 2558 36 370 171 C ATOM 724 C4' G B 3 12.741 46.671 -7.886 1.00 17.00 C ANISOU 724 C4' G B 3 2123 2041 2293 -283 -98 384 C ATOM 725 O4' G B 3 12.350 45.277 -7.875 1.00 15.16 O ANISOU 725 O4' G B 3 1404 2096 2259 -64 -97 507 O ATOM 726 C3' G B 3 13.905 46.821 -6.907 1.00 14.62 C ANISOU 726 C3' G B 3 1570 1836 2148 -285 121 -86 C ATOM 727 O3' G B 3 13.406 47.280 -5.672 1.00 14.55 O ANISOU 727 O3' G B 3 1597 1828 2102 146 -51 104 O ATOM 728 C2' G B 3 14.399 45.388 -6.783 1.00 14.91 C ANISOU 728 C2' G B 3 1378 1984 2302 -265 -12 387 C ATOM 729 O2' G B 3 15.118 45.153 -5.591 1.00 14.72 O ANISOU 729 O2' G B 3 1408 1910 2272 -175 -80 339 O ATOM 730 C1' G B 3 13.077 44.633 -6.842 1.00 14.10 C ANISOU 730 C1' G B 3 1486 1726 2145 18 -18 442 C ATOM 731 N9 G B 3 13.217 43.219 -7.145 1.00 13.59 N ANISOU 731 N9 G B 3 1383 1809 1969 24 -72 208 N ATOM 732 C8 G B 3 13.986 42.641 -8.121 1.00 15.45 C ANISOU 732 C8 G B 3 1660 2126 2084 -72 149 77 C ATOM 733 N7 G B 3 13.898 41.335 -8.141 1.00 15.85 N ANISOU 733 N7 G B 3 1636 1999 2384 -106 183 86 N ATOM 734 C5 G B 3 13.003 41.032 -7.119 1.00 12.97 C ANISOU 734 C5 G B 3 1314 1711 1899 65 37 241 C ATOM 735 C6 G B 3 12.511 39.788 -6.649 1.00 12.82 C ANISOU 735 C6 G B 3 1479 1673 1716 40 -189 219 C ATOM 736 O6 G B 3 12.800 38.637 -7.042 1.00 15.13 O ANISOU 736 O6 G B 3 1684 1762 2301 -205 -75 185 O ATOM 737 N1 G B 3 11.624 39.956 -5.590 1.00 12.30 N ANISOU 737 N1 G B 3 1432 1615 1625 156 -263 131 N ATOM 738 C2 G B 3 11.230 41.153 -5.039 1.00 12.32 C ANISOU 738 C2 G B 3 1407 1617 1655 271 -24 212 C ATOM 739 N2 G B 3 10.365 41.119 -4.010 1.00 12.91 N ANISOU 739 N2 G B 3 1584 1524 1794 53 178 171 N ATOM 740 N3 G B 3 11.721 42.332 -5.453 1.00 13.24 N ANISOU 740 N3 G B 3 1362 1742 1925 84 -150 274 N ATOM 741 C4 G B 3 12.576 42.175 -6.496 1.00 12.16 C ANISOU 741 C4 G B 3 1304 1498 1817 123 -160 271 C ATOM 742 P U B 4 14.012 48.529 -4.905 1.00 17.06 P ANISOU 742 P U B 4 1634 2043 2804 -216 174 215 P ATOM 743 OP1 U B 4 14.738 49.375 -5.871 1.00 20.29 O ANISOU 743 OP1 U B 4 2004 2357 3346 -265 594 315 O ATOM 744 OP2 U B 4 14.684 48.092 -3.654 1.00 18.35 O ANISOU 744 OP2 U B 4 1718 2457 2794 114 51 153 O ATOM 745 O5' U B 4 12.674 49.277 -4.397 1.00 15.07 O ANISOU 745 O5' U B 4 1749 1678 2298 136 210 237 O ATOM 746 C5' U B 4 11.734 49.866 -5.311 1.00 14.68 C ANISOU 746 C5' U B 4 1635 1550 2391 126 172 615 C ATOM 747 C4' U B 4 10.468 50.146 -4.562 1.00 12.92 C ANISOU 747 C4' U B 4 1535 1574 1798 -301 195 220 C ATOM 748 O4' U B 4 9.813 48.877 -4.367 1.00 12.89 O ANISOU 748 O4' U B 4 1592 1517 1786 -97 -202 442 O ATOM 749 C3' U B 4 10.669 50.722 -3.168 1.00 13.76 C ANISOU 749 C3' U B 4 1793 1622 1813 -113 57 451 C ATOM 750 O3' U B 4 9.571 51.585 -2.815 1.00 13.20 O ANISOU 750 O3' U B 4 1552 1579 1882 -205 -49 196 O ATOM 751 C2' U B 4 10.643 49.480 -2.254 1.00 12.08 C ANISOU 751 C2' U B 4 1684 1207 1699 -327 -107 305 C ATOM 752 O2' U B 4 10.322 49.744 -0.894 1.00 13.02 O ANISOU 752 O2' U B 4 1650 1589 1708 -317 -187 312 O ATOM 753 C1' U B 4 9.576 48.671 -2.982 1.00 12.11 C ANISOU 753 C1' U B 4 1666 1309 1623 -30 -326 140 C ATOM 754 N1 U B 4 9.647 47.222 -2.731 1.00 10.85 N ANISOU 754 N1 U B 4 1233 1389 1499 -75 38 212 N ATOM 755 C2 U B 4 8.586 46.643 -2.056 1.00 10.14 C ANISOU 755 C2 U B 4 1189 1270 1394 -63 7 143 C ATOM 756 O2 U B 4 7.656 47.281 -1.608 1.00 10.94 O ANISOU 756 O2 U B 4 1246 1352 1558 -155 83 143 O ATOM 757 N3 U B 4 8.681 45.293 -1.864 1.00 11.04 N ANISOU 757 N3 U B 4 1254 1307 1630 90 -115 235 N ATOM 758 C4 U B 4 9.663 44.455 -2.359 1.00 11.28 C ANISOU 758 C4 U B 4 1311 1314 1658 32 -16 117 C ATOM 759 O4 U B 4 9.587 43.248 -2.155 1.00 12.20 O ANISOU 759 O4 U B 4 1365 1396 1875 101 34 244 O ATOM 760 C5 U B 4 10.725 45.153 -3.101 1.00 13.18 C ANISOU 760 C5 U B 4 1612 1331 2063 103 142 496 C ATOM 761 C6 U B 4 10.671 46.475 -3.255 1.00 11.77 C ANISOU 761 C6 U B 4 1419 1346 1705 181 -45 87 C ATOM 762 P U B 5 9.765 53.163 -2.584 1.00 14.36 P ANISOU 762 P U B 5 1921 1563 1970 -274 -85 311 P ATOM 763 OP1 U B 5 11.124 53.607 -3.026 1.00 17.29 O ANISOU 763 OP1 U B 5 1922 1908 2739 -417 111 392 O ATOM 764 OP2 U B 5 9.260 53.519 -1.244 1.00 15.45 O ANISOU 764 OP2 U B 5 2160 1618 2089 -23 -138 148 O ATOM 765 O5' U B 5 8.668 53.765 -3.539 1.00 13.37 O ANISOU 765 O5' U B 5 1864 1405 1811 -73 106 267 O ATOM 766 C5' U B 5 8.789 53.643 -4.993 1.00 14.38 C ANISOU 766 C5' U B 5 2067 1668 1728 -144 23 463 C ATOM 767 C4' U B 5 7.503 54.135 -5.653 1.00 13.93 C ANISOU 767 C4' U B 5 1721 1458 2111 -79 209 388 C ATOM 768 O4' U B 5 6.447 53.182 -5.303 1.00 13.06 O ANISOU 768 O4' U B 5 1797 1507 1658 -19 174 298 O ATOM 769 C3' U B 5 6.978 55.493 -5.194 1.00 13.63 C ANISOU 769 C3' U B 5 1814 1652 1709 131 8 308 C ATOM 770 O3' U B 5 6.248 56.098 -6.245 1.00 14.50 O ANISOU 770 O3' U B 5 1931 1678 1898 36 -105 464 O ATOM 771 C2' U B 5 5.992 55.115 -4.110 1.00 12.40 C ANISOU 771 C2' U B 5 1710 1447 1552 24 24 59 C ATOM 772 O2' U B 5 5.025 56.100 -3.823 1.00 14.39 O ANISOU 772 O2' U B 5 1964 1713 1789 103 68 105 O ATOM 773 C1' U B 5 5.353 53.856 -4.706 1.00 12.44 C ANISOU 773 C1' U B 5 1731 1473 1521 -52 178 222 C ATOM 774 N1 U B 5 4.769 52.944 -3.688 1.00 12.76 N ANISOU 774 N1 U B 5 1707 1626 1513 4 -104 382 N ATOM 775 C2 U B 5 3.430 52.648 -3.794 1.00 13.41 C ANISOU 775 C2 U B 5 1742 1706 1647 73 53 301 C ATOM 776 O2 U B 5 2.718 53.069 -4.687 1.00 13.92 O ANISOU 776 O2 U B 5 1850 1705 1732 57 -183 338 O ATOM 777 N3 U B 5 2.939 51.796 -2.814 1.00 12.63 N ANISOU 777 N3 U B 5 1834 1443 1519 -64 55 277 N ATOM 778 C4 U B 5 3.685 51.213 -1.772 1.00 13.20 C ANISOU 778 C4 U B 5 1710 1659 1647 18 3 61 C ATOM 779 O4 U B 5 3.096 50.457 -0.981 1.00 14.67 O ANISOU 779 O4 U B 5 2220 1726 1626 -46 180 270 O ATOM 780 C5 U B 5 5.085 51.564 -1.765 1.00 13.24 C ANISOU 780 C5 U B 5 1866 1749 1412 -226 14 154 C ATOM 781 C6 U B 5 5.584 52.389 -2.707 1.00 13.19 C ANISOU 781 C6 U B 5 1710 1631 1671 -19 -197 350 C ATOM 782 P C B 6 6.829 57.337 -7.124 1.00 15.81 P ANISOU 782 P C B 6 2236 1805 1965 -114 32 375 P ATOM 783 OP1 C B 6 6.251 57.194 -8.444 1.00 16.07 O ANISOU 783 OP1 C B 6 2378 1723 2002 -16 -130 20 O ATOM 784 OP2 C B 6 8.309 57.426 -6.937 1.00 19.01 O ANISOU 784 OP2 C B 6 2656 2372 2191 42 188 418 O ATOM 785 O5' C B 6 6.150 58.601 -6.475 1.00 14.43 O ANISOU 785 O5' C B 6 2162 1735 1584 -4 13 198 O ATOM 786 C5' C B 6 6.514 59.044 -5.166 1.00 13.97 C ANISOU 786 C5' C B 6 1824 1871 1610 -188 -176 16 C ATOM 787 C4' C B 6 5.602 60.167 -4.731 1.00 14.37 C ANISOU 787 C4' C B 6 2366 1672 1422 -124 142 120 C ATOM 788 O4' C B 6 5.933 61.324 -5.544 1.00 16.44 O ANISOU 788 O4' C B 6 2430 1770 2046 -187 3 231 O ATOM 789 C3' C B 6 4.109 59.954 -4.987 1.00 15.90 C ANISOU 789 C3' C B 6 2544 1888 1608 99 275 109 C ATOM 790 O3' C B 6 3.457 59.231 -3.960 1.00 15.92 O ANISOU 790 O3' C B 6 2262 2217 1568 129 -10 176 O ATOM 791 C2' C B 6 3.607 61.392 -5.028 1.00 16.63 C ANISOU 791 C2' C B 6 2588 1948 1780 106 130 327 C ATOM 792 O2' C B 6 3.471 61.989 -3.724 1.00 19.73 O ANISOU 792 O2' C B 6 3429 2210 1854 237 -37 346 O ATOM 793 C1' C B 6 4.738 62.069 -5.756 1.00 17.01 C ANISOU 793 C1' C B 6 2667 2086 1710 139 145 75 C ATOM 794 N1 C B 6 4.530 62.174 -7.253 1.00 15.28 N ANISOU 794 N1 C B 6 2365 1834 1607 138 37 225 N ATOM 795 C2 C B 6 3.624 63.147 -7.700 1.00 15.85 C ANISOU 795 C2 C B 6 2232 1990 1797 241 21 101 C ATOM 796 O2 C B 6 3.031 63.811 -6.858 1.00 17.16 O ANISOU 796 O2 C B 6 2582 2023 1912 56 191 158 O ATOM 797 N3 C B 6 3.438 63.341 -9.046 1.00 13.62 N ANISOU 797 N3 C B 6 2138 1483 1554 94 87 139 N ATOM 798 C4 C B 6 4.099 62.546 -9.919 1.00 14.53 C ANISOU 798 C4 C B 6 1946 1768 1807 230 100 150 C ATOM 799 N4 C B 6 3.911 62.808 -11.231 1.00 16.32 N ANISOU 799 N4 C B 6 2339 2095 1766 -17 -8 463 N ATOM 800 C5 C B 6 5.052 61.564 -9.493 1.00 17.13 C ANISOU 800 C5 C B 6 2604 2049 1853 292 26 439 C ATOM 801 C6 C B 6 5.225 61.401 -8.162 1.00 16.76 C ANISOU 801 C6 C B 6 2470 2160 1736 84 139 187 C ATOM 802 P U B 7 2.474 58.062 -4.350 1.00 17.11 P ANISOU 802 P U B 7 2255 2185 2059 63 129 477 P ATOM 803 OP1 U B 7 1.990 57.512 -3.061 1.00 19.91 O ANISOU 803 OP1 U B 7 2542 2687 2333 -121 392 859 O ATOM 804 OP2 U B 7 3.113 57.189 -5.370 1.00 17.04 O ANISOU 804 OP2 U B 7 2584 1955 1935 240 160 524 O ATOM 805 O5' U B 7 1.249 58.768 -5.112 1.00 17.49 O ANISOU 805 O5' U B 7 2353 2188 2102 236 217 302 O ATOM 806 C5' U B 7 0.530 59.857 -4.509 1.00 16.47 C ANISOU 806 C5' U B 7 2271 2097 1888 502 143 160 C ATOM 807 C4' U B 7 -0.195 60.652 -5.583 1.00 16.02 C ANISOU 807 C4' U B 7 2210 2026 1851 228 137 454 C ATOM 808 O4' U B 7 0.715 60.962 -6.670 1.00 16.67 O ANISOU 808 O4' U B 7 2211 2358 1763 2 61 82 O ATOM 809 C3' U B 7 -1.368 59.908 -6.204 1.00 17.83 C ANISOU 809 C3' U B 7 2254 2297 2222 187 71 416 C ATOM 810 O3' U B 7 -2.445 60.801 -6.465 1.00 20.68 O ANISOU 810 O3' U B 7 2654 3016 2187 573 212 536 O ATOM 811 C2' U B 7 -0.762 59.439 -7.533 1.00 18.00 C ANISOU 811 C2' U B 7 2444 2452 1940 -87 -81 208 C ATOM 812 O2' U B 7 -1.700 59.180 -8.558 1.00 19.84 O ANISOU 812 O2' U B 7 2546 2974 2015 -90 -22 197 O ATOM 813 C1' U B 7 0.198 60.556 -7.902 1.00 15.21 C ANISOU 813 C1' U B 7 2065 2014 1700 6 0 77 C ATOM 814 N1 U B 7 1.231 60.039 -8.776 1.00 14.93 N ANISOU 814 N1 U B 7 2208 1875 1588 198 -236 128 N ATOM 815 C2 U B 7 1.185 60.397 -10.131 1.00 14.37 C ANISOU 815 C2 U B 7 2000 1870 1588 228 -85 291 C ATOM 816 O2 U B 7 0.348 61.160 -10.565 1.00 15.86 O ANISOU 816 O2 U B 7 2125 2032 1869 305 94 329 O ATOM 817 N3 U B 7 2.157 59.833 -10.924 1.00 16.56 N ANISOU 817 N3 U B 7 2123 1819 2349 142 73 206 N ATOM 818 C4 U B 7 3.154 58.954 -10.487 1.00 16.56 C ANISOU 818 C4 U B 7 2320 1934 2034 255 206 248 C ATOM 819 O4 U B 7 3.940 58.517 -11.322 1.00 16.21 O ANISOU 819 O4 U B 7 2431 1983 1742 444 215 291 O ATOM 820 C5 U B 7 3.166 58.620 -9.057 1.00 15.69 C ANISOU 820 C5 U B 7 2314 1797 1850 56 334 21 C ATOM 821 C6 U B 7 2.204 59.182 -8.277 1.00 15.79 C ANISOU 821 C6 U B 7 2166 1848 1982 390 -65 93 C ATOM 822 P U B 8 -3.325 61.461 -5.327 1.00 23.78 P ANISOU 822 P U B 8 2940 3745 2348 325 578 516 P ATOM 823 OP1 U B 8 -3.067 62.916 -5.386 1.00 24.81 O ANISOU 823 OP1 U B 8 3694 3694 2037 432 688 218 O ATOM 824 OP2 U B 8 -3.089 60.711 -4.043 1.00 25.68 O ANISOU 824 OP2 U B 8 3607 3828 2322 620 557 769 O ATOM 825 O5' U B 8 -4.812 61.148 -5.881 1.00 27.56 O ANISOU 825 O5' U B 8 2960 4263 3249 435 335 482 O ATOM 826 C5' U B 8 -5.231 59.777 -6.103 1.00 36.56 C ANISOU 826 C5' U B 8 4433 5008 4450 101 144 141 C ATOM 827 C4' U B 8 -6.746 59.633 -5.975 1.00 44.34 C ANISOU 827 C4' U B 8 4967 6229 5651 30 11 84 C ATOM 828 O4' U B 8 -7.200 59.875 -4.607 1.00 47.30 O ANISOU 828 O4' U B 8 5575 6671 5723 105 10 83 O ATOM 829 C3' U B 8 -7.502 60.627 -6.851 1.00 47.17 C ANISOU 829 C3' U B 8 5493 6484 5943 71 -110 90 C ATOM 830 O3' U B 8 -8.721 60.067 -7.307 1.00 50.42 O ANISOU 830 O3' U B 8 5663 7093 6398 -144 -223 -31 O ATOM 831 C2' U B 8 -7.722 61.794 -5.898 1.00 49.16 C ANISOU 831 C2' U B 8 5842 6617 6217 120 -103 -60 C ATOM 832 O2' U B 8 -8.808 62.597 -6.318 1.00 50.44 O ANISOU 832 O2' U B 8 5791 6866 6508 181 -232 -101 O ATOM 833 C1' U B 8 -7.970 61.070 -4.564 1.00 50.83 C ANISOU 833 C1' U B 8 6167 6784 6360 147 31 -50 C ATOM 834 N1 U B 8 -7.589 61.885 -3.348 1.00 54.73 N ANISOU 834 N1 U B 8 6787 7315 6691 26 54 -206 N ATOM 835 C2 U B 8 -8.590 62.478 -2.577 1.00 57.30 C ANISOU 835 C2 U B 8 7041 7596 7132 75 68 -275 C ATOM 836 O2 U B 8 -9.786 62.376 -2.826 1.00 58.44 O ANISOU 836 O2 U B 8 7038 7908 7256 -2 199 -199 O ATOM 837 N3 U B 8 -8.144 63.205 -1.486 1.00 58.30 N ANISOU 837 N3 U B 8 7289 7617 7242 13 40 -372 N ATOM 838 C4 U B 8 -6.821 63.394 -1.103 1.00 58.61 C ANISOU 838 C4 U B 8 7373 7594 7300 -74 67 -402 C ATOM 839 O4 U B 8 -6.567 64.064 -0.103 1.00 59.65 O ANISOU 839 O4 U B 8 7745 7531 7387 -138 186 -448 O ATOM 840 C5 U B 8 -5.838 62.750 -1.946 1.00 57.63 C ANISOU 840 C5 U B 8 7241 7527 7129 -85 107 -369 C ATOM 841 C6 U B 8 -6.252 62.039 -3.009 1.00 56.29 C ANISOU 841 C6 U B 8 6879 7483 7022 -4 65 -259 C TER 842 U B 8 HETATM 843 ZN ZN B1009 2.135 64.864 -9.284 1.00 16.54 ZN ANISOU 843 ZN ZN B1009 2676 1900 1709 243 93 203 ZN HETATM 844 O HOH A2001 16.176 52.490 13.159 1.00 35.37 O ANISOU 844 O HOH A2001 4527 4901 4009 99 148 -730 O HETATM 845 O HOH A2002 15.624 49.188 4.235 1.00 33.79 O ANISOU 845 O HOH A2002 4723 4364 3748 -12 1212 -161 O HETATM 846 O HOH A2003 13.437 49.411 2.864 1.00 34.37 O ANISOU 846 O HOH A2003 2729 4719 5610 -87 68 -542 O HETATM 847 O HOH A2004 11.999 49.852 8.172 1.00 23.83 O ANISOU 847 O HOH A2004 3229 2799 3023 -85 90 -432 O HETATM 848 O HOH A2005 1.974 46.758 8.148 1.00 29.14 O ANISOU 848 O HOH A2005 3840 3561 3667 -306 345 672 O HETATM 849 O HOH A2006 2.566 50.877 8.230 1.00 47.60 O ANISOU 849 O HOH A2006 3961 7688 6434 -1562 1613 -3951 O HETATM 850 O HOH A2007 5.623 49.009 9.303 1.00 21.92 O ANISOU 850 O HOH A2007 2623 3640 2064 -867 -332 310 O HETATM 851 O HOH A2008 -3.029 50.095 3.117 1.00 63.12 O ANISOU 851 O HOH A2008 12381 5167 6434 848 808 1166 O HETATM 852 O HOH A2009 -4.064 43.050 7.189 1.00 31.05 O ANISOU 852 O HOH A2009 3953 5364 2478 316 259 989 O HETATM 853 O HOH A2010 -1.151 43.539 5.773 1.00 21.63 O ANISOU 853 O HOH A2010 3325 2140 2751 -502 -685 736 O HETATM 854 O HOH A2011 2.580 44.685 2.604 1.00 11.45 O ANISOU 854 O HOH A2011 1232 1567 1550 -136 48 367 O HETATM 855 O HOH A2012 -1.079 50.700 -0.505 1.00 24.62 O ANISOU 855 O HOH A2012 4068 2699 2586 334 613 190 O HETATM 856 O HOH A2013 10.967 44.112 -10.571 1.00 23.59 O ANISOU 856 O HOH A2013 2215 2778 3969 -307 437 176 O HETATM 857 O HOH A2014 1.210 44.209 7.027 1.00 27.89 O ANISOU 857 O HOH A2014 3646 3552 3397 -654 240 244 O HETATM 858 O HOH A2015 4.004 45.504 10.079 1.00 34.84 O ANISOU 858 O HOH A2015 3654 5310 4270 -519 -167 1918 O HETATM 859 O HOH A2016 3.498 46.235 -18.750 1.00 41.91 O ANISOU 859 O HOH A2016 6042 5531 4350 -299 1033 677 O HETATM 860 O HOH A2017 7.194 38.096 -21.723 1.00 36.65 O ANISOU 860 O HOH A2017 4191 5356 4375 -1257 -155 38 O HETATM 861 O HOH A2018 10.964 40.085 -17.904 1.00 55.71 O ANISOU 861 O HOH A2018 4465 6925 9777 756 -62 2330 O HETATM 862 O HOH A2019 2.318 43.003 4.857 1.00 19.45 O ANISOU 862 O HOH A2019 3101 2071 2218 -749 -271 296 O HETATM 863 O HOH A2020 0.940 40.866 -24.945 1.00 36.02 O ANISOU 863 O HOH A2020 5627 5329 2728 -755 22 362 O HETATM 864 O HOH A2021 13.019 42.446 -11.572 1.00 31.65 O ANISOU 864 O HOH A2021 4732 3319 3972 354 1069 888 O HETATM 865 O HOH A2022 2.019 43.131 -25.822 1.00 49.91 O ANISOU 865 O HOH A2022 6236 7836 4890 -2867 -449 211 O HETATM 866 O HOH A2023 -6.167 49.931 -11.344 1.00 91.36 O ANISOU 866 O HOH A2023 6476 16204 12031 5267 -1368 900 O HETATM 867 O HOH A2024 -3.646 31.796 -1.096 1.00 27.05 O ANISOU 867 O HOH A2024 2397 4186 3695 -181 101 503 O HETATM 868 O HOH A2025 -13.928 49.081 -6.483 1.00 40.78 O ANISOU 868 O HOH A2025 6452 3939 5102 287 -570 1179 O HETATM 869 O HOH A2026 -11.362 43.010 -7.059 1.00 16.97 O ANISOU 869 O HOH A2026 1738 2459 2251 -111 -18 -723 O HETATM 870 O HOH A2027 -11.954 41.551 -11.459 1.00 37.72 O ANISOU 870 O HOH A2027 4798 6231 3302 1719 -1528 -802 O HETATM 871 O HOH A2028 2.286 56.473 -17.615 1.00 42.65 O ANISOU 871 O HOH A2028 4780 5229 6194 -470 2865 -1804 O HETATM 872 O HOH A2029 8.025 60.756 -11.598 1.00 30.78 O ANISOU 872 O HOH A2029 3299 5350 3045 202 622 1384 O HETATM 873 O HOH A2030 -9.567 43.740 -14.648 1.00 43.00 O ANISOU 873 O HOH A2030 4990 4761 6587 948 -3214 -1684 O HETATM 874 O HOH A2031 -11.439 38.543 -11.693 1.00 24.73 O ANISOU 874 O HOH A2031 2721 3579 3094 349 -395 -1029 O HETATM 875 O HOH A2032 12.280 46.318 -15.787 1.00 43.87 O ANISOU 875 O HOH A2032 4812 5997 5858 32 2620 -824 O HETATM 876 O HOH A2033 12.106 42.019 -14.364 1.00 48.24 O ANISOU 876 O HOH A2033 5183 6467 6679 1260 795 -377 O HETATM 877 O HOH A2034 -13.072 36.463 -6.512 1.00 22.86 O ANISOU 877 O HOH A2034 2497 2644 3544 183 -7 -208 O HETATM 878 O HOH A2035 -5.901 31.887 -3.163 1.00 21.41 O ANISOU 878 O HOH A2035 2967 2494 2670 -492 -243 680 O HETATM 879 O HOH A2036 -9.486 34.507 -1.052 1.00 16.06 O ANISOU 879 O HOH A2036 1376 2700 2026 -37 -110 696 O HETATM 880 O HOH A2037 -4.983 48.053 8.033 1.00 48.97 O ANISOU 880 O HOH A2037 5542 6039 7024 -1649 2371 -1950 O HETATM 881 O HOH A2038 -5.049 33.875 0.573 1.00 20.34 O ANISOU 881 O HOH A2038 2067 2623 3038 -193 -108 180 O HETATM 882 O HOH A2039 -7.828 36.738 0.871 1.00 18.99 O ANISOU 882 O HOH A2039 2192 2768 2256 -814 -781 949 O HETATM 883 O HOH A2040 1.860 42.190 8.875 1.00 36.86 O ANISOU 883 O HOH A2040 5916 4030 4059 -440 -292 736 O HETATM 884 O HOH A2041 -12.708 46.258 -6.253 1.00 22.13 O ANISOU 884 O HOH A2041 2004 3594 2810 6 -408 555 O HETATM 885 O HOH A2042 -11.032 50.522 -6.953 1.00 48.91 O ANISOU 885 O HOH A2042 3153 7879 7551 856 -702 4175 O HETATM 886 O HOH A2043 -9.095 51.287 2.295 1.00 45.06 O ANISOU 886 O HOH A2043 6669 5551 4901 -653 -735 -919 O HETATM 887 O HOH A2044 4.865 30.669 -17.644 1.00 37.99 O ANISOU 887 O HOH A2044 5723 3986 4723 1860 86 -412 O HETATM 888 O HOH A2045 -2.094 56.319 -5.524 1.00 37.31 O ANISOU 888 O HOH A2045 5954 2709 5512 236 415 353 O HETATM 889 O HOH A2046 -0.872 53.862 -3.273 1.00 30.49 O ANISOU 889 O HOH A2046 5491 2373 3718 1053 464 242 O HETATM 890 O HOH A2047 2.437 55.138 -9.665 1.00 23.27 O ANISOU 890 O HOH A2047 2975 2859 3006 48 23 821 O HETATM 891 O HOH A2048 -0.861 52.002 -12.845 1.00 34.14 O ANISOU 891 O HOH A2048 3295 5882 3794 1285 -1222 1070 O HETATM 892 O HOH A2049 8.597 57.706 -2.743 1.00 38.70 O ANISOU 892 O HOH A2049 6831 3393 4479 -942 -2374 1038 O HETATM 893 O HOH A2050 7.912 58.298 -10.463 1.00 26.44 O ANISOU 893 O HOH A2050 3635 4071 2337 -1780 150 -3 O HETATM 894 O HOH A2051 3.321 58.331 -15.825 1.00 34.49 O ANISOU 894 O HOH A2051 3755 4932 4416 1181 -17 415 O HETATM 895 O HOH A2052 12.691 57.325 -19.585 1.00 27.77 O ANISOU 895 O HOH A2052 4641 3700 2208 -1284 991 -21 O HETATM 896 O HOH A2053 5.947 63.341 -15.241 1.00 19.61 O ANISOU 896 O HOH A2053 2918 2371 2159 511 569 874 O HETATM 897 O HOH A2054 11.750 59.846 -13.007 1.00 29.46 O ANISOU 897 O HOH A2054 3824 3479 3890 -268 -1280 -268 O HETATM 898 O HOH A2055 11.675 53.645 -16.196 1.00 31.32 O ANISOU 898 O HOH A2055 4213 3898 3787 -724 188 468 O HETATM 899 O HOH A2056 6.619 51.801 -20.265 1.00 31.21 O ANISOU 899 O HOH A2056 4950 4693 2213 -2032 -731 836 O HETATM 900 O HOH A2057 12.515 51.385 -16.724 1.00 41.73 O ANISOU 900 O HOH A2057 3955 6991 4908 1437 566 2004 O HETATM 901 O HOH A2058 5.975 46.948 -17.239 1.00 36.43 O ANISOU 901 O HOH A2058 5873 3965 4003 -966 -953 355 O HETATM 902 O HOH A2059 11.684 46.112 -12.571 1.00 23.93 O ANISOU 902 O HOH A2059 2430 2870 3790 287 596 335 O HETATM 903 O HOH A2060 10.585 58.335 -10.635 1.00 29.36 O ANISOU 903 O HOH A2060 4485 2965 3704 155 96 607 O HETATM 904 O HOH A2061 13.945 54.369 -9.700 1.00 43.08 O ANISOU 904 O HOH A2061 5157 5903 5306 1030 -915 2368 O HETATM 905 O HOH A2062 10.352 44.028 -14.579 1.00 34.29 O ANISOU 905 O HOH A2062 3112 3822 6094 581 909 -519 O HETATM 906 O HOH A2063 12.399 52.602 -8.255 1.00 21.93 O ANISOU 906 O HOH A2063 2640 2541 3149 -651 -104 69 O HETATM 907 O HOH A2064 -1.672 49.854 -4.707 1.00 16.99 O ANISOU 907 O HOH A2064 1700 2348 2406 208 -95 290 O HETATM 908 O HOH A2065 -4.107 51.902 -2.527 1.00 35.19 O ANISOU 908 O HOH A2065 4138 2361 6870 75 825 -385 O HETATM 909 O HOH A2066 -5.710 49.497 1.354 1.00 51.52 O ANISOU 909 O HOH A2066 5815 5920 7839 -2150 -1125 -83 O HETATM 910 O HOH A2067 -7.394 47.721 3.445 1.00 28.42 O ANISOU 910 O HOH A2067 2877 4529 3391 438 -2 -34 O HETATM 911 O HOH A2068 -10.984 49.453 3.260 1.00 30.23 O ANISOU 911 O HOH A2068 4256 2828 4399 272 1090 136 O HETATM 912 O HOH A2069 -7.888 46.696 8.409 1.00 37.55 O ANISOU 912 O HOH A2069 4547 3562 6155 -1589 1284 -1447 O HETATM 913 O HOH A2070 -8.887 42.801 10.728 1.00 28.92 O ANISOU 913 O HOH A2070 3602 3542 3842 -1059 1078 -269 O HETATM 914 O HOH A2071 -1.361 40.788 5.922 1.00 16.77 O ANISOU 914 O HOH A2071 2121 2014 2235 19 189 71 O HETATM 915 O HOH A2072 -5.516 36.665 2.173 1.00 22.94 O ANISOU 915 O HOH A2072 1736 1942 5037 79 -958 -516 O HETATM 916 O HOH A2073 0.200 33.106 6.716 1.00 34.42 O ANISOU 916 O HOH A2073 3853 3685 5537 834 -2244 2206 O HETATM 917 O HOH A2074 -2.064 34.127 8.812 1.00 38.14 O ANISOU 917 O HOH A2074 4506 4019 5966 1089 105 1943 O HETATM 918 O HOH A2075 3.704 40.657 5.310 1.00 20.53 O ANISOU 918 O HOH A2075 2148 2972 2678 51 141 758 O HETATM 919 O HOH A2076 4.866 36.854 9.671 1.00 42.43 O ANISOU 919 O HOH A2076 5831 6082 4209 1410 448 -1596 O HETATM 920 O HOH A2077 1.496 39.541 6.763 1.00 36.56 O ANISOU 920 O HOH A2077 4463 4948 4478 955 2093 1413 O HETATM 921 O HOH A2078 -0.902 31.803 -1.675 1.00 24.80 O ANISOU 921 O HOH A2078 2478 3837 3105 -281 -111 -965 O HETATM 922 O HOH A2079 -1.165 27.325 2.070 1.00 50.00 O ANISOU 922 O HOH A2079 6550 5983 6463 -1100 -2417 1357 O HETATM 923 O HOH A2080 1.105 28.736 -0.213 1.00 39.20 O ANISOU 923 O HOH A2080 6408 4390 4094 -2856 -139 418 O HETATM 924 O HOH A2081 2.278 32.071 5.528 1.00 41.18 O ANISOU 924 O HOH A2081 3224 7493 4929 1030 -375 834 O HETATM 925 O HOH A2082 5.578 29.183 -2.386 1.00 34.43 O ANISOU 925 O HOH A2082 4165 4720 4197 1438 -765 -1018 O HETATM 926 O HOH A2083 3.460 27.819 3.903 1.00 42.82 O ANISOU 926 O HOH A2083 4338 6224 5705 566 701 1901 O HETATM 927 O HOH A2084 5.758 33.869 -5.023 1.00 14.14 O ANISOU 927 O HOH A2084 1400 1714 2256 152 -10 -69 O HETATM 928 O HOH A2085 -2.758 31.882 -4.299 1.00 38.19 O ANISOU 928 O HOH A2085 5278 3584 5649 -1616 -1474 621 O HETATM 929 O HOH A2086 0.566 29.332 -6.332 1.00 38.87 O ANISOU 929 O HOH A2086 6976 4263 3529 -3835 164 -9 O HETATM 930 O HOH A2087 0.358 31.099 -12.348 1.00 40.95 O ANISOU 930 O HOH A2087 4854 3749 6956 -1642 -24 350 O HETATM 931 O HOH A2088 7.317 31.531 -5.380 1.00 23.76 O ANISOU 931 O HOH A2088 3744 2248 3034 598 -670 -260 O HETATM 932 O HOH A2089 0.504 31.993 -17.852 1.00 33.96 O ANISOU 932 O HOH A2089 4366 4484 4050 547 -359 -1313 O HETATM 933 O HOH A2090 1.163 29.333 -16.093 1.00 43.89 O ANISOU 933 O HOH A2090 4233 5062 7378 424 287 -280 O HETATM 934 O HOH A2091 -1.792 33.622 -16.592 1.00 21.75 O ANISOU 934 O HOH A2091 3209 2784 2269 -595 -321 349 O HETATM 935 O HOH A2092 2.943 32.416 -18.650 1.00 30.68 O ANISOU 935 O HOH A2092 3520 4377 3760 -807 116 -204 O HETATM 936 O HOH A2093 9.055 38.344 -14.015 1.00 27.95 O ANISOU 936 O HOH A2093 4146 2859 3612 -347 1127 -198 O HETATM 937 O HOH A2094 10.194 34.448 -14.842 1.00 29.45 O ANISOU 937 O HOH A2094 2713 4594 3879 430 569 -820 O HETATM 938 O HOH A2095 4.653 34.486 -8.505 1.00 19.17 O ANISOU 938 O HOH A2095 2447 2722 2114 -813 31 -79 O HETATM 939 O HOH A2096 7.530 35.646 -6.094 1.00 13.09 O ANISOU 939 O HOH A2096 1481 1632 1857 55 -190 -35 O HETATM 940 O HOH A2097 6.567 55.746 4.975 1.00 40.44 O ANISOU 940 O HOH A2097 7600 3809 3956 1646 1112 -13 O HETATM 941 O HOH A2098 7.895 55.750 -0.856 1.00 28.01 O ANISOU 941 O HOH A2098 4810 2899 2931 1117 787 -27 O HETATM 942 O HOH B2001 14.888 46.252 -14.800 1.00 52.90 O ANISOU 942 O HOH B2001 6816 6921 6362 2069 4620 777 O HETATM 943 O HOH B2002 14.035 44.942 -3.079 1.00 29.06 O ANISOU 943 O HOH B2002 1124 7315 2601 540 -191 1320 O HETATM 944 O HOH B2003 13.218 49.823 -12.400 1.00 38.60 O ANISOU 944 O HOH B2003 2476 7473 4715 502 32 1084 O HETATM 945 O HOH B2004 15.788 44.165 -10.918 1.00 42.83 O ANISOU 945 O HOH B2004 3845 9328 3099 -1349 939 -534 O HETATM 946 O HOH B2005 14.673 37.650 -8.411 1.00 34.11 O ANISOU 946 O HOH B2005 4247 4900 3813 1232 1446 -220 O HETATM 947 O HOH B2006 13.979 50.396 -8.361 1.00 28.80 O ANISOU 947 O HOH B2006 3891 3272 3778 -325 846 755 O HETATM 948 O HOH B2007 14.604 48.252 -0.735 1.00 27.31 O ANISOU 948 O HOH B2007 2153 4337 3885 -638 315 -138 O HETATM 949 O HOH B2008 17.340 49.283 -6.738 1.00 33.83 O ANISOU 949 O HOH B2008 2924 4478 5451 -514 561 632 O HETATM 950 O HOH B2009 14.864 52.017 -5.523 1.00 40.56 O ANISOU 950 O HOH B2009 4685 3188 7537 -1585 2680 -127 O HETATM 951 O HOH B2010 12.079 47.988 0.385 1.00 24.25 O ANISOU 951 O HOH B2010 1715 3986 3513 -220 -351 1718 O HETATM 952 O HOH B2011 13.708 52.962 -3.190 1.00 37.86 O ANISOU 952 O HOH B2011 2903 5080 6401 -761 1211 -1330 O HETATM 953 O HOH B2012 11.692 56.377 -2.002 1.00 41.18 O ANISOU 953 O HOH B2012 6898 4185 4561 -2156 1105 327 O HETATM 954 O HOH B2013 0.068 51.283 -3.016 1.00 15.71 O ANISOU 954 O HOH B2013 1866 1974 2126 25 144 151 O HETATM 955 O HOH B2014 4.887 56.092 -10.520 1.00 15.78 O ANISOU 955 O HOH B2014 2250 1963 1780 328 -39 -25 O HETATM 956 O HOH B2015 10.015 55.484 -7.854 1.00 21.63 O ANISOU 956 O HOH B2015 2648 2759 2809 91 364 166 O HETATM 957 O HOH B2016 5.697 61.717 -13.133 1.00 27.41 O ANISOU 957 O HOH B2016 4335 3077 3000 1174 1293 835 O HETATM 958 O HOH B2017 3.710 60.761 -1.275 1.00 39.39 O ANISOU 958 O HOH B2017 6342 6118 2504 -88 -210 1637 O HETATM 959 O HOH B2018 1.060 63.230 -3.826 1.00 32.67 O ANISOU 959 O HOH B2018 3164 4245 5002 -121 502 -986 O HETATM 960 O HOH B2019 3.156 65.990 -5.028 1.00 44.60 O ANISOU 960 O HOH B2019 8001 3879 5065 -62 -1156 -548 O HETATM 961 O HOH B2020 10.262 57.556 -4.717 1.00 34.37 O ANISOU 961 O HOH B2020 4310 4711 4037 -336 119 519 O HETATM 962 O HOH B2021 9.532 59.866 -7.435 1.00 40.00 O ANISOU 962 O HOH B2021 3826 5383 5986 -2138 447 130 O HETATM 963 O HOH B2022 9.066 61.990 -5.713 1.00 46.06 O ANISOU 963 O HOH B2022 5046 5924 6527 -2527 -425 -778 O HETATM 964 O HOH B2023 5.564 59.180 -13.324 1.00 30.52 O ANISOU 964 O HOH B2023 4707 2647 4240 -684 2296 -281 O HETATM 965 O HOH B2024 0.281 56.855 -10.083 1.00 30.30 O ANISOU 965 O HOH B2024 3224 5010 3278 926 67 763 O HETATM 966 O HOH B2025 2.050 58.914 -0.791 1.00 36.02 O ANISOU 966 O HOH B2025 6907 4248 2529 448 548 650 O HETATM 967 O HOH B2026 -0.720 56.477 -2.999 1.00 40.67 O ANISOU 967 O HOH B2026 2672 5365 7413 -233 173 1857 O HETATM 968 O HOH B2027 -1.246 61.989 -2.389 1.00 36.70 O ANISOU 968 O HOH B2027 4494 5361 4088 1724 71 -7 O HETATM 969 O HOH B2028 15.366 43.486 -14.745 1.00 46.41 O ANISOU 969 O HOH B2028 4283 8974 4375 -459 563 1649 O HETATM 970 O HOH B2029 11.717 45.265 0.724 1.00 20.62 O ANISOU 970 O HOH B2029 1891 3213 2727 -176 272 376 O HETATM 971 O HOH B2030 6.578 59.769 -0.745 1.00 47.94 O ANISOU 971 O HOH B2030 6940 5981 5292 1073 276 2733 O HETATM 972 O HOH B2031 6.960 60.794 2.547 1.00 48.14 O ANISOU 972 O HOH B2031 6491 3437 8362 -53 -1019 -1881 O CONECT 712 843 CONECT 797 843 CONECT 843 712 797 MASTER 322 0 1 3 6 0 1 6 933 2 3 9 END
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Related entries of code: 2xs2
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
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Protein Sequence Similarity
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Complexes with the same small molecule ligand
PDB Code
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Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
2xs2
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
RRM domain of mouse deleted in azoospermia (DAZ)-like (DAZL, 32-132)
Ligand Name
RNA, 5'-UUGUUCUU-3'
EC.Number
E.C.-.-.-.-
Resolution
1.35(Å)
Affinity (Kd/Ki/IC50)
Kd=38.2nM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) Proc.Natl.Acad.Sci.USA Vol. 108: pp. 18266
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q64368
Entrez Gene ID
NCBI Entrez Gene ID:
13164
ASD
Information of known allosteric effects of PDB entries
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