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*** TOXIN 30-AUG-12 4GV5 ***elNémo ID: 23011323363465737Job options:ID = 23011323363465737 JOBID = TOXIN 30-AUG-12 4GV5 USERID = unknown PRIVAT = 0 NMODES = 10 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER TOXIN 30-AUG-12 4GV5 TITLE X-RAY STRUCTURE OF CROTAMINE, A CELL-PENETRATING PEPTIDE FROM THE TITLE 2 BRAZILIAN SNAKE CROTALUS DURISSUS TERRIFICUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: CROTAMINE ILE-19; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: CRO_ILE-19 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CROTALUS DURISSUS TERRIFICUS; SOURCE 3 ORGANISM_COMMON: SOUTH AMERICAN RATTLESNAKE; SOURCE 4 ORGANISM_TAXID: 8732 KEYWDS ALPHA HELIX & BETA SHEET, ION CHANNEL INHIBITOR, ANTIBACTERIAL KEYWDS 2 PEPTIDE, EXTRACELLULAR REGION, TOXIN EXPDTA X-RAY DIFFRACTION AUTHOR M.A.CORONADO,A.GABDULKHAKOV,D.GEORGIEVA,B.SANKARAN,M.T.MURAKAMI, AUTHOR 2 R.K.ARNI,C.BETZEL REVDAT 5 07-MAR-18 4GV5 1 REMARK REVDAT 4 23-OCT-13 4GV5 1 JRNL REVDAT 3 02-OCT-13 4GV5 1 DBREF SOURCE REVDAT 2 11-SEP-13 4GV5 1 REMARK REVDAT 1 04-SEP-13 4GV5 0 JRNL AUTH M.A.CORONADO,A.GABDULKHAKOV,D.GEORGIEVA,B.SANKARAN, JRNL AUTH 2 M.T.MURAKAMI,R.K.ARNI,C.BETZEL JRNL TITL STRUCTURE OF THE POLYPEPTIDE CROTAMINE FROM THE BRAZILIAN JRNL TITL 2 RATTLESNAKE CROTALUS DURISSUS TERRIFICUS. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 1958 2013 JRNL REFN ISSN 0907-4449 JRNL PMID 24100315 JRNL DOI 10.1107/S0907444913018003 REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0117 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) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 20890 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) : 0.170 REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1121 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) : 1.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1125 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.06 REMARK 3 BIN R VALUE (WORKING SET) : 0.5500 REMARK 3 BIN FREE R VALUE SET COUNT : 63 REMARK 3 BIN FREE R VALUE : 0.6910 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1014 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 51 REMARK 3 SOLVENT ATOMS : 62 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.73 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.67000 REMARK 3 B22 (A**2) : -0.86000 REMARK 3 B33 (A**2) : 1.53000 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): 0.096 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.092 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.493 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1116 ; 0.034 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1471 ; 2.856 ; 1.975 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 127 ; 6.475 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 39 ;23.802 ;21.538 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 221 ;18.430 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;22.576 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 126 ; 0.196 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 784 ; 0.012 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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): 1116 ;11.826 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 31 ;27.031 ; 5.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1122 ;36.112 ; 5.000 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 : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN REMARK 3 THE INPUT REMARK 4 REMARK 4 4GV5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-12. REMARK 100 THE DEPOSITION ID IS D_1000074671. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.1 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY REMARK 200 BEAMLINE : P14 (MX2) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.12 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20890 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 10.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: AUTOSOL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.51 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM THIOCYANATE, 1.9 M REMARK 280 AMMONIUM SULPHATE, PH 6.1, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y,-Z REMARK 290 8555 X,-Y,-Z+1/2 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 33.46100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.09950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.16500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.09950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.46100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.16500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 33.46100 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.16500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.09950 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.16500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.46100 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 40.09950 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 74.33000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 40.09950 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3560 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8100 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 -1.000000 0.000000 0.000000 66.92200 REMARK 350 BIOMT2 1 0.000000 -1.000000 0.000000 37.16500 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH C 212 LIES ON A SPECIAL POSITION. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 MET A 28 -132.02 47.26 REMARK 500 MET B 28 -130.86 48.04 REMARK 500 MET C 28 -129.55 46.75 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 103 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 104 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 103 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN C 102 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 103 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 104 DBREF 4GV5 A 1 42 UNP P01475 MYXC_CRODU 1 42 DBREF 4GV5 B 1 42 UNP P01475 MYXC_CRODU 1 42 DBREF 4GV5 C 1 42 UNP P01475 MYXC_CRODU 1 42 SEQRES 1 A 42 TYR LYS GLN CYS HIS LYS LYS GLY GLY HIS CYS PHE PRO SEQRES 2 A 42 LYS GLU LYS ILE CYS LEU PRO PRO SER SER ASP PHE GLY SEQRES 3 A 42 LYS MET ASP CYS ARG TRP ARG TRP LYS CYS CYS LYS LYS SEQRES 4 A 42 GLY SER GLY SEQRES 1 B 42 TYR LYS GLN CYS HIS LYS LYS GLY GLY HIS CYS PHE PRO SEQRES 2 B 42 LYS GLU LYS ILE CYS LEU PRO PRO SER SER ASP PHE GLY SEQRES 3 B 42 LYS MET ASP CYS ARG TRP ARG TRP LYS CYS CYS LYS LYS SEQRES 4 B 42 GLY SER GLY SEQRES 1 C 42 TYR LYS GLN CYS HIS LYS LYS GLY GLY HIS CYS PHE PRO SEQRES 2 C 42 LYS GLU LYS ILE CYS LEU PRO PRO SER SER ASP PHE GLY SEQRES 3 C 42 LYS MET ASP CYS ARG TRP ARG TRP LYS CYS CYS LYS LYS SEQRES 4 C 42 GLY SER GLY HET SCN A 101 3 HET SCN A 102 3 HET GOL A 103 6 HET GOL A 104 6 HET SO4 B 101 5 HET SO4 B 102 5 HET SCN B 103 3 HET SO4 C 101 5 HET SCN C 102 3 HET GOL C 103 6 HET GOL C 104 6 HETNAM SCN THIOCYANATE ION HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 SCN 4(C N S 1-) FORMUL 6 GOL 4(C3 H8 O3) FORMUL 8 SO4 3(O4 S 2-) FORMUL 15 HOH *62(H2 O) HELIX 1 1 TYR A 1 LYS A 7 1 7 HELIX 2 2 PRO A 20 ASP A 24 1 5 SHEET 1 1 1 GLY A 9 PRO A 13 0 SHEET 2 2 1 TRP A 34 LYS A 38 0 SSBOND 1 CYS A 4 CYS A 36 1555 1555 2.13 SSBOND 2 CYS A 11 CYS A 30 1555 1555 2.13 SSBOND 3 CYS A 18 CYS A 37 1555 1555 2.02 SSBOND 4 CYS B 4 CYS B 36 1555 1555 2.05 SSBOND 5 CYS B 11 CYS B 30 1555 1555 2.06 SSBOND 6 CYS B 18 CYS B 37 1555 1555 2.00 SSBOND 7 CYS C 4 CYS C 36 1555 1555 2.13 SSBOND 8 CYS C 11 CYS C 30 1555 1555 2.08 LINK SG CYS C 18 SG CYS C 37 1555 1555 1.70 CISPEP 1 LEU A 19 PRO A 20 0 -3.40 CISPEP 2 LEU B 19 PRO B 20 0 0.95 CISPEP 3 LEU C 19 PRO C 20 0 10.95 SITE 1 AC1 4 ILE A 17 HOH A 204 TYR C 1 TRP C 34 SITE 1 AC2 5 PRO A 13 LYS A 14 GLU A 15 PRO B 21 SITE 2 AC2 5 PRO C 13 SITE 1 AC3 5 LYS A 14 TRP A 32 ARG A 33 PRO B 21 SITE 2 AC3 5 SER B 22 SITE 1 AC4 4 GLN A 3 TRP A 32 ARG A 33 HOH A 215 SITE 1 AC5 6 LYS B 2 GLN B 3 TRP B 32 ARG B 33 SITE 2 AC5 6 HOH B 209 HOH B 211 SITE 1 AC6 6 TYR B 1 HIS B 10 CYS B 11 HOH B 213 SITE 2 AC6 6 ARG C 31 TRP C 32 SITE 1 AC7 5 PHE B 12 PRO B 13 ILE B 17 GLY B 42 SITE 2 AC7 5 GOL C 103 SITE 1 AC8 6 PHE A 12 PRO A 13 LYS A 16 HIS C 10 SITE 2 AC8 6 CYS C 11 HOH C 204 SITE 1 AC9 2 TRP C 32 ARG C 33 SITE 1 BC1 7 PHE B 12 GLY B 42 SCN B 103 ARG C 31 SITE 2 BC1 7 TRP C 32 ARG C 33 TRP C 34 SITE 1 BC2 7 LEU B 19 PRO B 20 PRO B 21 PRO C 13 SITE 2 BC2 7 LYS C 14 GLU C 15 LYS C 16 CRYST1 66.922 74.330 80.199 90.00 90.00 90.00 I 21 21 21 24 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 0.014943 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013454 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012469 0.00000 ATOM 1 N TYR A 1 24.311 40.954 45.768 1.00 48.43 N ANISOU 1 N TYR A 1 6674 7165 4561 -1383 1803 -302 N ATOM 2 CA TYR A 1 22.901 40.559 45.929 1.00 46.14 C ANISOU 2 CA TYR A 1 6349 4789 6394 -158 1927 -1208 C ATOM 3 C TYR A 1 22.740 39.866 47.274 1.00 50.30 C ANISOU 3 C TYR A 1 6924 6579 5608 897 489 -947 C ATOM 4 O TYR A 1 23.578 39.023 47.619 1.00 48.29 O ANISOU 4 O TYR A 1 6325 5751 6271 196 -141 -688 O ATOM 5 CB TYR A 1 22.554 39.627 44.799 1.00 46.55 C ANISOU 5 CB TYR A 1 8175 4578 4932 -1960 -1004 486 C ATOM 6 CG TYR A 1 22.522 40.362 43.516 1.00 39.39 C ANISOU 6 CG TYR A 1 6216 5801 2947 22 1429 72 C ATOM 7 CD1 TYR A 1 21.545 41.330 43.290 1.00 64.59 C ANISOU 7 CD1 TYR A 1 6778 8253 9507 -365 -736 2417 C ATOM 8 CD2 TYR A 1 23.481 40.137 42.519 1.00 42.00 C ANISOU 8 CD2 TYR A 1 7965 5930 2064 1402 2007 250 C ATOM 9 CE1 TYR A 1 21.507 42.019 42.090 1.00 84.67 C ANISOU 9 CE1 TYR A 1 12819 8250 11100 -653 3177 3303 C ATOM 10 CE2 TYR A 1 23.428 40.798 41.291 1.00 42.01 C ANISOU 10 CE2 TYR A 1 8103 4983 2875 963 -142 537 C ATOM 11 CZ TYR A 1 22.470 41.761 41.105 1.00 58.47 C ANISOU 11 CZ TYR A 1 9210 6541 6463 -368 -949 771 C ATOM 12 OH TYR A 1 22.402 42.469 39.919 1.00 62.09 O ANISOU 12 OH TYR A 1 11715 6953 4923 -396 801 -864 O ATOM 13 N LYS A 2 21.671 40.199 48.001 1.00 41.64 N ANISOU 13 N LYS A 2 5750 4508 5563 -149 700 -1120 N ATOM 14 CA LYS A 2 21.496 39.794 49.427 1.00 41.06 C ANISOU 14 CA LYS A 2 4983 5356 5259 149 2324 -1046 C ATOM 15 C LYS A 2 21.742 38.292 49.675 1.00 37.57 C ANISOU 15 C LYS A 2 3562 5711 5000 79 248 -1697 C ATOM 16 O LYS A 2 22.587 37.955 50.467 1.00 42.63 O ANISOU 16 O LYS A 2 5395 5518 5285 653 -256 -2190 O ATOM 17 CB LYS A 2 20.069 40.193 49.936 1.00 47.38 C ANISOU 17 CB LYS A 2 5466 5424 7109 1213 3447 -1822 C ATOM 18 CG LYS A 2 19.769 40.064 51.444 1.00 72.13 C ANISOU 18 CG LYS A 2 6964 11056 9386 -2051 2264 -4277 C ATOM 19 CD LYS A 2 18.363 40.553 51.803 1.00 63.74 C ANISOU 19 CD LYS A 2 6635 8674 8906 128 -1773 -4014 C ATOM 20 CE LYS A 2 18.211 40.865 53.306 1.00 85.58 C ANISOU 20 CE LYS A 2 7630 16059 8826 539 2270 -1666 C ATOM 21 NZ LYS A 2 16.785 40.750 53.766 1.00114.43 N ANISOU 21 NZ LYS A 2 13291 21439 8747 4159 3598 2752 N ATOM 22 N GLN A 3 20.983 37.403 49.013 1.00 37.10 N ANISOU 22 N GLN A 3 5055 5047 3992 -779 1012 -1367 N ATOM 23 CA GLN A 3 20.983 35.955 49.346 1.00 40.92 C ANISOU 23 CA GLN A 3 4805 5768 4972 289 161 -1255 C ATOM 24 C GLN A 3 22.294 35.285 48.988 1.00 33.20 C ANISOU 24 C GLN A 3 4323 4546 3745 -501 277 -874 C ATOM 25 O GLN A 3 22.844 34.461 49.802 1.00 35.66 O ANISOU 25 O GLN A 3 5161 5226 3161 -65 537 -733 O ATOM 26 CB GLN A 3 19.767 35.192 48.794 1.00 37.76 C ANISOU 26 CB GLN A 3 3789 6107 4450 -644 459 -1001 C ATOM 27 CG GLN A 3 18.456 35.922 49.091 1.00 37.23 C ANISOU 27 CG GLN A 3 3844 5878 4423 -521 -357 -9 C ATOM 28 CD GLN A 3 18.133 35.872 50.562 1.00 42.35 C ANISOU 28 CD GLN A 3 4680 5983 5428 1106 527 -68 C ATOM 29 OE1 GLN A 3 18.730 35.029 51.312 1.00 40.67 O ANISOU 29 OE1 GLN A 3 4827 7604 3021 -224 1036 -225 O ATOM 30 NE2 GLN A 3 17.205 36.737 51.025 1.00 43.32 N ANISOU 30 NE2 GLN A 3 4856 6446 5154 1051 881 -878 N ATOM 31 N CYS A 4 22.849 35.700 47.831 1.00 32.29 N ANISOU 31 N CYS A 4 3390 4970 3906 -653 1725 -1370 N ATOM 32 CA CYS A 4 24.146 35.145 47.360 1.00 30.30 C ANISOU 32 CA CYS A 4 3075 6031 2404 137 791 -976 C ATOM 33 C CYS A 4 25.199 35.612 48.402 1.00 34.59 C ANISOU 33 C CYS A 4 3847 4753 4540 -39 23 -55 C ATOM 34 O CYS A 4 26.002 34.803 48.928 1.00 32.96 O ANISOU 34 O CYS A 4 4162 5573 2787 202 -21 -560 O ATOM 35 CB CYS A 4 24.440 35.634 45.905 1.00 35.65 C ANISOU 35 CB CYS A 4 4232 6271 3040 414 724 -10 C ATOM 36 SG CYS A 4 26.087 35.012 45.476 1.00 36.57 S ANISOU 36 SG CYS A 4 4536 5491 3865 -134 172 -292 S ATOM 37 N HIS A 5 25.194 36.900 48.725 1.00 37.49 N ANISOU 37 N HIS A 5 4979 5176 4089 95 93 -846 N ATOM 38 CA HIS A 5 26.136 37.437 49.682 1.00 41.85 C ANISOU 38 CA HIS A 5 6452 6092 3355 -816 -454 -1159 C ATOM 39 C HIS A 5 25.998 36.741 51.028 1.00 40.69 C ANISOU 39 C HIS A 5 4767 6478 4215 7 -569 -1451 C ATOM 40 O HIS A 5 27.002 36.376 51.657 1.00 45.98 O ANISOU 40 O HIS A 5 5604 7178 4688 158 -1067 -2206 O ATOM 41 CB HIS A 5 26.026 38.939 49.775 1.00 44.11 C ANISOU 41 CB HIS A 5 4445 5872 6442 -859 -528 -1782 C ATOM 42 CG HIS A 5 26.928 39.550 50.871 1.00 57.48 C ANISOU 42 CG HIS A 5 6701 7413 7727 -373 -2095 -1205 C ATOM 43 ND1 HIS A 5 28.234 39.827 50.664 1.00 67.20 N ANISOU 43 ND1 HIS A 5 10382 8416 6733 -653 3779 -2316 N ATOM 44 CD2 HIS A 5 26.671 39.883 52.205 1.00 90.63 C ANISOU 44 CD2 HIS A 5 15993 8861 9578 1646 -914 -2745 C ATOM 45 CE1 HIS A 5 28.776 40.320 51.783 1.00 76.90 C ANISOU 45 CE1 HIS A 5 15191 7451 6575 1811 -2888 -846 C ATOM 46 NE2 HIS A 5 27.823 40.341 52.724 1.00 97.10 N ANISOU 46 NE2 HIS A 5 19438 7906 9547 3097 -3044 -6890 N ATOM 47 N LYS A 6 24.755 36.526 51.464 1.00 46.68 N ANISOU 47 N LYS A 6 5815 6908 5010 -987 -503 -213 N ATOM 48 CA LYS A 6 24.518 35.839 52.689 1.00 39.78 C ANISOU 48 CA LYS A 6 4100 6960 4052 -714 -406 -39 C ATOM 49 C LYS A 6 25.116 34.478 52.820 1.00 45.96 C ANISOU 49 C LYS A 6 7453 6632 3378 -666 -1255 -1097 C ATOM 50 O LYS A 6 25.550 34.166 53.947 1.00 48.22 O ANISOU 50 O LYS A 6 6194 10004 2123 -54 -217 -204 O ATOM 51 CB LYS A 6 23.079 35.774 53.044 1.00 39.75 C ANISOU 51 CB LYS A 6 3769 6920 4412 -841 121 -1715 C ATOM 52 CG LYS A 6 22.520 37.020 53.717 1.00 71.12 C ANISOU 52 CG LYS A 6 9494 13997 3531 3120 -190 -4676 C ATOM 53 CD LYS A 6 20.980 36.875 53.824 1.00101.25 C ANISOU 53 CD LYS A 6 10214 17126 11127 -3208 -1625 -1690 C ATOM 54 CE LYS A 6 20.445 35.459 54.200 1.00 57.85 C ANISOU 54 CE LYS A 6 7555 12061 2365 742 86 -1620 C ATOM 55 NZ LYS A 6 20.202 35.394 55.645 1.00105.66 N ANISOU 55 NZ LYS A 6 15040 21576 3529 2381 -835 -745 N ATOM 56 N LYS A 7 25.155 33.716 51.709 1.00 43.85 N ANISOU 56 N LYS A 7 6452 6383 3825 -151 -226 -603 N ATOM 57 CA LYS A 7 25.844 32.434 51.605 1.00 41.04 C ANISOU 57 CA LYS A 7 5724 6338 3527 -119 -817 -381 C ATOM 58 C LYS A 7 27.349 32.559 51.571 1.00 35.16 C ANISOU 58 C LYS A 7 4781 5253 3323 -284 -1027 305 C ATOM 59 O LYS A 7 28.021 31.526 51.573 1.00 50.63 O ANISOU 59 O LYS A 7 6476 7405 5356 678 -1274 610 O ATOM 60 CB LYS A 7 25.436 31.670 50.329 1.00 44.44 C ANISOU 60 CB LYS A 7 6222 6378 4285 451 -194 -1700 C ATOM 61 CG LYS A 7 24.163 30.975 50.626 1.00 51.82 C ANISOU 61 CG LYS A 7 5679 6483 7525 95 87 517 C ATOM 62 CD LYS A 7 23.931 29.824 49.732 1.00 56.90 C ANISOU 62 CD LYS A 7 6939 10555 4123 -660 2015 -825 C ATOM 63 CE LYS A 7 22.866 28.970 50.368 1.00 58.37 C ANISOU 63 CE LYS A 7 8212 11305 2659 806 109 828 C ATOM 64 NZ LYS A 7 23.298 28.071 51.436 1.00 64.97 N ANISOU 64 NZ LYS A 7 11743 9019 3920 -2041 -2024 1425 N ATOM 65 N GLY A 8 27.891 33.791 51.546 1.00 40.18 N ANISOU 65 N GLY A 8 6137 6403 2726 -1156 269 103 N ATOM 66 CA GLY A 8 29.340 33.966 51.457 1.00 41.87 C ANISOU 66 CA GLY A 8 5407 7262 3238 -350 264 -1078 C ATOM 67 C GLY A 8 29.807 33.862 49.988 1.00 35.66 C ANISOU 67 C GLY A 8 4315 6029 3204 805 -76 -125 C ATOM 68 O GLY A 8 30.971 33.632 49.687 1.00 39.22 O ANISOU 68 O GLY A 8 4612 7283 3007 1034 -728 -1671 O ATOM 69 N GLY A 9 28.880 34.025 49.058 1.00 36.96 N ANISOU 69 N GLY A 9 5608 5403 3030 5 -915 -350 N ATOM 70 CA GLY A 9 29.219 33.864 47.600 1.00 34.94 C ANISOU 70 CA GLY A 9 5397 4960 2917 56 -612 168 C ATOM 71 C GLY A 9 29.298 35.198 46.859 1.00 33.03 C ANISOU 71 C GLY A 9 4610 4036 3903 -549 -78 -1257 C ATOM 72 O GLY A 9 29.119 36.303 47.455 1.00 35.49 O ANISOU 72 O GLY A 9 4989 4966 3529 -419 326 -1567 O ATOM 73 N HIS A 10 29.573 35.078 45.555 1.00 33.72 N ANISOU 73 N HIS A 10 3933 5242 3634 -96 34 -904 N ATOM 74 CA HIS A 10 29.513 36.162 44.662 1.00 35.30 C ANISOU 74 CA HIS A 10 5416 4481 3512 -1671 -389 -351 C ATOM 75 C HIS A 10 28.930 35.691 43.353 1.00 32.80 C ANISOU 75 C HIS A 10 4251 3695 4514 109 -682 -496 C ATOM 76 O HIS A 10 28.965 34.505 43.080 1.00 31.47 O ANISOU 76 O HIS A 10 4305 4039 3614 -566 36 -501 O ATOM 77 CB HIS A 10 30.920 36.687 44.430 1.00 40.09 C ANISOU 77 CB HIS A 10 4769 5543 4918 -2130 1528 -835 C ATOM 78 CG HIS A 10 30.938 38.043 43.862 1.00 79.21 C ANISOU 78 CG HIS A 10 8249 7844 14001 -2619 -1548 722 C ATOM 79 ND1 HIS A 10 31.410 38.306 42.609 1.00 98.22 N ANISOU 79 ND1 HIS A 10 4672 13315 19329 -750 -104 -2633 N ATOM 80 CD2 HIS A 10 30.508 39.255 44.396 1.00 86.29 C ANISOU 80 CD2 HIS A 10 10291 10522 11973 -4653 4378 -3111 C ATOM 81 CE1 HIS A 10 31.279 39.611 42.353 1.00113.21 C ANISOU 81 CE1 HIS A 10 24953 11844 6216 -10717 -1280 95 C ATOM 82 NE2 HIS A 10 30.731 40.200 43.457 1.00 97.62 N ANISOU 82 NE2 HIS A 10 11069 8215 17804 -2304 -4237 -3975 N ATOM 83 N CYS A 11 28.407 36.589 42.524 1.00 32.14 N ANISOU 83 N CYS A 11 5108 4435 2667 77 179 -870 N ATOM 84 CA CYS A 11 27.831 36.192 41.252 1.00 28.45 C ANISOU 84 CA CYS A 11 3097 5806 1906 217 649 -1586 C ATOM 85 C CYS A 11 28.786 36.113 40.145 1.00 27.67 C ANISOU 85 C CYS A 11 2929 3917 3667 -369 1195 -86 C ATOM 86 O CYS A 11 29.536 37.067 39.892 1.00 33.89 O ANISOU 86 O CYS A 11 4625 3845 4404 -991 1245 -800 O ATOM 87 CB CYS A 11 26.616 37.067 40.894 1.00 36.38 C ANISOU 87 CB CYS A 11 3932 4926 4965 289 992 -617 C ATOM 88 SG CYS A 11 25.267 37.101 42.146 1.00 40.25 S ANISOU 88 SG CYS A 11 5604 5513 4174 1082 590 -360 S ATOM 89 N PHE A 12 28.633 35.036 39.378 1.00 32.24 N ANISOU 89 N PHE A 12 3957 4644 3649 41 -281 -189 N ATOM 90 CA PHE A 12 29.570 34.775 38.195 1.00 32.65 C ANISOU 90 CA PHE A 12 3654 4868 3882 525 164 -175 C ATOM 91 C PHE A 12 28.715 34.319 37.052 1.00 31.75 C ANISOU 91 C PHE A 12 4425 4789 2850 -826 566 692 C ATOM 92 O PHE A 12 27.615 33.842 37.275 1.00 27.78 O ANISOU 92 O PHE A 12 3399 4103 3053 -161 135 -93 O ATOM 93 CB PHE A 12 30.663 33.679 38.504 1.00 29.06 C ANISOU 93 CB PHE A 12 3207 4561 3271 536 -823 71 C ATOM 94 CG PHE A 12 31.522 33.999 39.638 1.00 29.31 C ANISOU 94 CG PHE A 12 3592 4086 3456 -62 -365 -358 C ATOM 95 CD1 PHE A 12 32.666 34.792 39.463 1.00 37.03 C ANISOU 95 CD1 PHE A 12 4271 5571 4227 -1375 -612 -290 C ATOM 96 CD2 PHE A 12 31.209 33.529 40.955 1.00 33.56 C ANISOU 96 CD2 PHE A 12 4411 5127 3211 316 -793 -19 C ATOM 97 CE1 PHE A 12 33.473 35.117 40.543 1.00 39.65 C ANISOU 97 CE1 PHE A 12 4844 6238 3982 -507 -614 -1873 C ATOM 98 CE2 PHE A 12 32.086 33.851 42.056 1.00 28.52 C ANISOU 98 CE2 PHE A 12 3643 4135 3057 -541 -516 -282 C ATOM 99 CZ PHE A 12 33.189 34.642 41.833 1.00 42.76 C ANISOU 99 CZ PHE A 12 4539 6381 5327 -1425 -82 -226 C ATOM 100 N PRO A 13 29.226 34.432 35.819 1.00 26.59 N ANISOU 100 N PRO A 13 3436 3754 2911 -142 627 378 N ATOM 101 CA PRO A 13 28.435 33.933 34.648 1.00 27.48 C ANISOU 101 CA PRO A 13 3693 3718 3028 -193 572 106 C ATOM 102 C PRO A 13 28.022 32.464 34.862 1.00 25.85 C ANISOU 102 C PRO A 13 3138 3995 2687 57 544 103 C ATOM 103 O PRO A 13 28.815 31.683 35.520 1.00 28.16 O ANISOU 103 O PRO A 13 3760 3718 3221 173 42 -344 O ATOM 104 CB PRO A 13 29.474 34.079 33.497 1.00 25.68 C ANISOU 104 CB PRO A 13 3521 3408 2827 -786 605 -119 C ATOM 105 CG PRO A 13 30.238 35.310 33.908 1.00 25.50 C ANISOU 105 CG PRO A 13 3705 3754 2230 -681 76 -80 C ATOM 106 CD PRO A 13 30.511 35.051 35.412 1.00 26.83 C ANISOU 106 CD PRO A 13 3117 4371 2705 -480 376 494 C ATOM 107 N LYS A 14 26.854 32.055 34.347 1.00 26.33 N ANISOU 107 N LYS A 14 3293 3255 3455 -293 -86 -282 N ATOM 108 CA LYS A 14 26.279 30.739 34.482 1.00 27.75 C ANISOU 108 CA LYS A 14 3928 3248 3365 378 -658 151 C ATOM 109 C LYS A 14 27.302 29.546 34.237 1.00 23.33 C ANISOU 109 C LYS A 14 2356 3507 3001 -347 -575 402 C ATOM 110 O LYS A 14 27.215 28.529 34.923 1.00 26.09 O ANISOU 110 O LYS A 14 3426 3632 2855 -199 -40 276 O ATOM 111 CB LYS A 14 25.120 30.702 33.415 1.00 35.18 C ANISOU 111 CB LYS A 14 3478 4098 5791 399 -966 195 C ATOM 112 CG LYS A 14 24.369 29.433 33.341 1.00 32.85 C ANISOU 112 CG LYS A 14 4227 4728 3527 83 -200 387 C ATOM 113 CD LYS A 14 23.168 29.611 32.433 1.00 34.75 C ANISOU 113 CD LYS A 14 4472 4455 4275 701 -772 565 C ATOM 114 CE LYS A 14 22.754 28.197 32.200 1.00 35.26 C ANISOU 114 CE LYS A 14 4327 5660 3411 401 -671 -288 C ATOM 115 NZ LYS A 14 21.546 28.155 31.278 1.00 33.56 N ANISOU 115 NZ LYS A 14 3520 4953 4277 -74 -630 -49 N ATOM 116 N GLU A 15 28.205 29.639 33.234 1.00 25.69 N ANISOU 116 N GLU A 15 3240 3693 2826 64 491 -581 N ATOM 117 CA GLU A 15 29.101 28.568 32.854 1.00 22.99 C ANISOU 117 CA GLU A 15 2943 3714 2075 382 -117 -121 C ATOM 118 C GLU A 15 30.485 28.643 33.540 1.00 20.90 C ANISOU 118 C GLU A 15 2784 3231 1924 73 -32 -108 C ATOM 119 O GLU A 15 31.349 27.815 33.271 1.00 25.28 O ANISOU 119 O GLU A 15 3307 3526 2772 129 48 -243 O ATOM 120 CB GLU A 15 29.322 28.533 31.287 1.00 24.15 C ANISOU 120 CB GLU A 15 3529 3899 1745 -520 -408 -512 C ATOM 121 CG GLU A 15 28.034 28.205 30.567 1.00 25.42 C ANISOU 121 CG GLU A 15 3502 3291 2862 -829 -589 156 C ATOM 122 CD GLU A 15 27.316 26.985 31.106 1.00 29.32 C ANISOU 122 CD GLU A 15 3532 3551 4055 187 93 19 C ATOM 123 OE1 GLU A 15 27.977 25.944 31.319 1.00 27.54 O ANISOU 123 OE1 GLU A 15 4047 3686 2728 -27 -252 -301 O ATOM 124 OE2 GLU A 15 26.099 27.103 31.385 1.00 28.80 O ANISOU 124 OE2 GLU A 15 3652 4152 3138 66 376 -129 O ATOM 125 N LYS A 16 30.678 29.655 34.429 1.00 25.81 N ANISOU 125 N LYS A 16 3756 3276 2771 -362 -535 -160 N ATOM 126 CA LYS A 16 31.976 29.797 35.068 1.00 27.99 C ANISOU 126 CA LYS A 16 3220 3637 3777 -162 -613 -110 C ATOM 127 C LYS A 16 32.199 28.509 35.874 1.00 26.13 C ANISOU 127 C LYS A 16 3026 3764 3135 -191 -285 -181 C ATOM 128 O LYS A 16 31.270 28.098 36.665 1.00 27.73 O ANISOU 128 O LYS A 16 3871 3850 2815 -2 -127 252 O ATOM 129 CB LYS A 16 32.087 31.039 35.966 1.00 27.26 C ANISOU 129 CB LYS A 16 3502 3746 3110 -506 759 293 C ATOM 130 CG LYS A 16 33.519 31.148 36.534 1.00 30.53 C ANISOU 130 CG LYS A 16 3701 4291 3605 -323 170 -708 C ATOM 131 CD LYS A 16 33.721 31.926 37.759 1.00 36.38 C ANISOU 131 CD LYS A 16 4304 5071 4448 664 -82 -1527 C ATOM 132 CE LYS A 16 35.089 31.586 38.360 1.00 52.43 C ANISOU 132 CE LYS A 16 4691 8021 7207 -2454 -2881 -1257 C ATOM 133 NZ LYS A 16 35.923 32.646 37.688 1.00 73.14 N ANISOU 133 NZ LYS A 16 6132 9584 12074 -2200 -3950 3405 N ATOM 134 N ILE A 17 33.402 27.896 35.772 1.00 25.50 N ANISOU 134 N ILE A 17 3413 3626 2649 323 -497 137 N ATOM 135 CA ILE A 17 33.706 26.701 36.624 1.00 24.57 C ANISOU 135 CA ILE A 17 3747 3497 2090 443 -742 -277 C ATOM 136 C ILE A 17 33.942 27.163 38.045 1.00 26.08 C ANISOU 136 C ILE A 17 3675 3780 2454 -440 -152 -582 C ATOM 137 O ILE A 17 34.786 28.096 38.293 1.00 27.01 O ANISOU 137 O ILE A 17 3850 4078 2335 -350 93 -104 O ATOM 138 CB ILE A 17 34.925 25.963 36.079 1.00 26.88 C ANISOU 138 CB ILE A 17 4035 3263 2914 463 -575 117 C ATOM 139 CG1 ILE A 17 34.550 25.348 34.606 1.00 26.49 C ANISOU 139 CG1 ILE A 17 3104 3901 3058 -501 76 -52 C ATOM 140 CG2 ILE A 17 35.517 24.937 37.074 1.00 25.14 C ANISOU 140 CG2 ILE A 17 3599 3907 2043 -2 -622 523 C ATOM 141 CD1 ILE A 17 35.782 24.956 33.853 1.00 26.74 C ANISOU 141 CD1 ILE A 17 3359 4842 1956 281 -357 213 C ATOM 142 N CYS A 18 33.172 26.546 38.962 1.00 27.48 N ANISOU 142 N CYS A 18 3708 4467 2264 523 -175 -83 N ATOM 143 CA CYS A 18 33.350 26.853 40.436 1.00 26.84 C ANISOU 143 CA CYS A 18 4068 3996 2133 107 297 -375 C ATOM 144 C CYS A 18 33.710 25.551 41.117 1.00 27.06 C ANISOU 144 C CYS A 18 3608 3683 2988 -214 668 -320 C ATOM 145 O CYS A 18 32.870 24.623 41.132 1.00 27.52 O ANISOU 145 O CYS A 18 3638 4149 2668 -657 -5 46 O ATOM 146 CB CYS A 18 32.081 27.410 41.069 1.00 30.58 C ANISOU 146 CB CYS A 18 3044 4480 4092 570 463 -107 C ATOM 147 SG CYS A 18 31.611 29.009 40.348 1.00 34.75 S ANISOU 147 SG CYS A 18 4467 4710 4026 532 -224 -458 S ATOM 148 N LEU A 19 34.953 25.430 41.598 1.00 28.69 N ANISOU 148 N LEU A 19 3281 3899 3721 541 226 -126 N ATOM 149 CA LEU A 19 35.363 24.164 42.196 1.00 28.16 C ANISOU 149 CA LEU A 19 4444 4108 2148 1197 -196 -568 C ATOM 150 C LEU A 19 35.750 24.517 43.689 1.00 28.48 C ANISOU 150 C LEU A 19 4548 3577 2694 -27 -543 -737 C ATOM 151 O LEU A 19 36.330 25.565 43.951 1.00 33.45 O ANISOU 151 O LEU A 19 4324 5040 3344 -124 -1212 -823 O ATOM 152 CB LEU A 19 36.561 23.511 41.440 1.00 30.83 C ANISOU 152 CB LEU A 19 4602 4119 2989 814 -277 -816 C ATOM 153 CG LEU A 19 36.291 23.120 39.979 1.00 27.37 C ANISOU 153 CG LEU A 19 3892 3776 2729 4 -233 -481 C ATOM 154 CD1 LEU A 19 37.523 22.588 39.294 1.00 31.43 C ANISOU 154 CD1 LEU A 19 3517 4939 3486 190 -296 -28 C ATOM 155 CD2 LEU A 19 35.207 22.089 39.947 1.00 29.17 C ANISOU 155 CD2 LEU A 19 3936 4101 3045 -162 -947 -693 C ATOM 156 N PRO A 20 35.463 23.630 44.629 1.00 28.75 N ANISOU 156 N PRO A 20 4115 4449 2358 -184 -395 171 N ATOM 157 CA PRO A 20 34.756 22.376 44.430 1.00 28.91 C ANISOU 157 CA PRO A 20 4645 4067 2273 514 -1290 37 C ATOM 158 C PRO A 20 33.291 22.691 44.049 1.00 26.55 C ANISOU 158 C PRO A 20 4391 3474 2223 455 -67 267 C ATOM 159 O PRO A 20 32.817 23.799 44.328 1.00 30.48 O ANISOU 159 O PRO A 20 5135 3929 2514 472 -233 -324 O ATOM 160 CB PRO A 20 34.861 21.703 45.854 1.00 30.59 C ANISOU 160 CB PRO A 20 5377 4521 1724 430 -50 -319 C ATOM 161 CG PRO A 20 34.803 22.886 46.808 1.00 37.12 C ANISOU 161 CG PRO A 20 5769 4996 3338 136 -430 -686 C ATOM 162 CD PRO A 20 35.662 23.927 46.109 1.00 35.75 C ANISOU 162 CD PRO A 20 5481 5625 2477 90 -211 -339 C ATOM 163 N PRO A 21 32.577 21.722 43.415 1.00 25.71 N ANISOU 163 N PRO A 21 3622 3735 2410 181 -489 206 N ATOM 164 CA PRO A 21 31.212 22.033 42.961 1.00 25.19 C ANISOU 164 CA PRO A 21 2723 4032 2813 -359 316 -497 C ATOM 165 C PRO A 21 30.246 22.311 44.159 1.00 23.68 C ANISOU 165 C PRO A 21 3049 3698 2249 444 94 17 C ATOM 166 O PRO A 21 29.226 23.013 43.962 1.00 28.87 O ANISOU 166 O PRO A 21 3768 4148 3052 491 378 -234 O ATOM 167 CB PRO A 21 30.778 20.746 42.222 1.00 28.78 C ANISOU 167 CB PRO A 21 3367 3813 3752 132 122 -894 C ATOM 168 CG PRO A 21 32.090 20.090 41.793 1.00 28.36 C ANISOU 168 CG PRO A 21 3677 4369 2726 789 -941 -262 C ATOM 169 CD PRO A 21 33.022 20.376 43.010 1.00 27.23 C ANISOU 169 CD PRO A 21 4150 3424 2770 244 -1003 -258 C ATOM 170 N SER A 22 30.613 21.892 45.408 1.00 29.20 N ANISOU 170 N SER A 22 4165 4621 2308 154 595 0 N ATOM 171 CA SER A 22 29.698 22.257 46.459 1.00 32.57 C ANISOU 171 CA SER A 22 4881 4703 2791 126 1197 727 C ATOM 172 C SER A 22 29.736 23.725 46.793 1.00 33.60 C ANISOU 172 C SER A 22 4307 4695 3762 -112 166 315 C ATOM 173 O SER A 22 28.883 24.216 47.546 1.00 43.28 O ANISOU 173 O SER A 22 5314 7439 3692 -271 861 208 O ATOM 174 CB SER A 22 30.092 21.502 47.706 1.00 35.37 C ANISOU 174 CB SER A 22 4535 6243 2659 -790 489 534 C ATOM 175 OG SER A 22 31.487 21.706 47.955 1.00 34.56 O ANISOU 175 OG SER A 22 5200 5544 2387 105 -490 198 O ATOM 176 N SER A 23 30.754 24.446 46.266 1.00 29.75 N ANISOU 176 N SER A 23 4162 4914 2224 19 -91 77 N ATOM 177 CA SER A 23 30.853 25.937 46.461 1.00 32.81 C ANISOU 177 CA SER A 23 4619 4656 3189 -22 1049 863 C ATOM 178 C SER A 23 29.973 26.677 45.455 1.00 29.72 C ANISOU 178 C SER A 23 4945 3784 2563 -480 807 -420 C ATOM 179 O SER A 23 29.886 27.911 45.479 1.00 32.78 O ANISOU 179 O SER A 23 4896 4368 3189 52 334 -455 O ATOM 180 CB SER A 23 32.292 26.372 46.499 1.00 39.34 C ANISOU 180 CB SER A 23 4196 4678 6072 -246 2404 -2253 C ATOM 181 OG SER A 23 32.789 26.233 45.124 1.00 49.06 O ANISOU 181 OG SER A 23 5452 5360 7828 -38 295 356 O ATOM 182 N ASP A 24 29.331 25.932 44.548 1.00 26.87 N ANISOU 182 N ASP A 24 3773 4495 1940 -4 -443 -330 N ATOM 183 CA ASP A 24 28.407 26.581 43.520 1.00 27.91 C ANISOU 183 CA ASP A 24 3113 5004 2487 -40 -116 -1112 C ATOM 184 C ASP A 24 27.010 26.410 44.126 1.00 24.15 C ANISOU 184 C ASP A 24 3638 3481 2055 -77 670 -516 C ATOM 185 O ASP A 24 26.495 25.279 44.215 1.00 32.06 O ANISOU 185 O ASP A 24 4001 4048 4130 -324 579 -287 O ATOM 186 CB ASP A 24 28.632 25.803 42.204 1.00 28.86 C ANISOU 186 CB ASP A 24 4783 3434 2748 555 251 -454 C ATOM 187 CG ASP A 24 27.697 26.200 41.080 1.00 32.50 C ANISOU 187 CG ASP A 24 4485 4684 3176 332 445 -235 C ATOM 188 OD1 ASP A 24 26.671 26.872 41.317 1.00 32.26 O ANISOU 188 OD1 ASP A 24 4156 4055 4046 -210 252 -16 O ATOM 189 OD2 ASP A 24 27.962 25.809 39.848 1.00 31.25 O ANISOU 189 OD2 ASP A 24 4175 4312 3386 171 871 -410 O ATOM 190 N PHE A 25 26.347 27.542 44.425 1.00 28.18 N ANISOU 190 N PHE A 25 3452 4113 3142 273 554 -1067 N ATOM 191 CA PHE A 25 25.004 27.549 45.172 1.00 27.24 C ANISOU 191 CA PHE A 25 3128 4175 3047 68 300 -1136 C ATOM 192 C PHE A 25 23.919 27.741 44.194 1.00 31.22 C ANISOU 192 C PHE A 25 3185 4888 3786 856 557 -1005 C ATOM 193 O PHE A 25 22.779 27.946 44.576 1.00 31.84 O ANISOU 193 O PHE A 25 3748 4976 3372 -121 135 -1068 O ATOM 194 CB PHE A 25 25.010 28.644 46.214 1.00 30.77 C ANISOU 194 CB PHE A 25 4720 4528 2442 -215 -87 -804 C ATOM 195 CG PHE A 25 26.182 28.527 47.215 1.00 31.66 C ANISOU 195 CG PHE A 25 4747 4983 2297 -174 -19 -243 C ATOM 196 CD1 PHE A 25 26.460 27.331 47.892 1.00 39.96 C ANISOU 196 CD1 PHE A 25 6064 5536 3581 729 -701 -442 C ATOM 197 CD2 PHE A 25 26.953 29.667 47.531 1.00 35.35 C ANISOU 197 CD2 PHE A 25 4372 5282 3778 -393 -265 126 C ATOM 198 CE1 PHE A 25 27.513 27.278 48.895 1.00 42.96 C ANISOU 198 CE1 PHE A 25 6169 5879 4273 -617 -1013 -894 C ATOM 199 CE2 PHE A 25 28.017 29.628 48.451 1.00 36.05 C ANISOU 199 CE2 PHE A 25 4367 5365 3964 466 -322 95 C ATOM 200 CZ PHE A 25 28.270 28.414 49.175 1.00 35.44 C ANISOU 200 CZ PHE A 25 4707 4999 3759 368 230 -172 C ATOM 201 N GLY A 26 24.230 27.563 42.922 1.00 30.26 N ANISOU 201 N GLY A 26 4368 4131 2998 -405 279 -1047 N ATOM 202 CA GLY A 26 23.206 27.793 41.839 1.00 29.80 C ANISOU 202 CA GLY A 26 3485 5040 2797 -547 120 77 C ATOM 203 C GLY A 26 22.789 29.269 41.682 1.00 28.84 C ANISOU 203 C GLY A 26 3421 5107 2427 -210 -314 -415 C ATOM 204 O GLY A 26 23.485 30.197 42.130 1.00 30.66 O ANISOU 204 O GLY A 26 3575 4746 3328 -383 261 -325 O ATOM 205 N LYS A 27 21.660 29.527 41.022 1.00 36.73 N ANISOU 205 N LYS A 27 3749 5733 4474 827 -1058 -1978 N ATOM 206 CA LYS A 27 21.327 30.914 40.686 1.00 31.87 C ANISOU 206 CA LYS A 27 4015 5372 2719 763 -485 -859 C ATOM 207 C LYS A 27 21.191 31.846 41.944 1.00 31.66 C ANISOU 207 C LYS A 27 4214 4501 3312 167 177 -956 C ATOM 208 O LYS A 27 21.539 33.002 41.861 1.00 33.11 O ANISOU 208 O LYS A 27 4723 4832 3025 804 546 -518 O ATOM 209 CB LYS A 27 20.084 31.042 39.819 1.00 37.60 C ANISOU 209 CB LYS A 27 4243 6466 3575 1233 -1181 -1221 C ATOM 210 CG LYS A 27 19.863 32.529 39.242 1.00 50.76 C ANISOU 210 CG LYS A 27 6414 6658 6213 1868 -361 -2817 C ATOM 211 CD LYS A 27 18.581 32.755 38.355 1.00 67.15 C ANISOU 211 CD LYS A 27 5020 5673 14820 -287 -651 4825 C ATOM 212 CE LYS A 27 18.369 34.217 37.977 1.00 62.44 C ANISOU 212 CE LYS A 27 11590 5131 7002 -2070 5173 -659 C ATOM 213 NZ LYS A 27 17.834 34.922 39.228 1.00 61.86 N ANISOU 213 NZ LYS A 27 3212 9962 10329 -2170 3715 -4506 N ATOM 214 N MET A 28 20.671 31.350 43.060 1.00 34.78 N ANISOU 214 N MET A 28 4187 5786 3241 23 30 -806 N ATOM 215 CA MET A 28 20.352 32.230 44.213 1.00 32.44 C ANISOU 215 CA MET A 28 4236 4646 3441 196 87 -1299 C ATOM 216 C MET A 28 19.597 33.435 43.677 1.00 32.83 C ANISOU 216 C MET A 28 4029 5730 2714 -510 510 -753 C ATOM 217 O MET A 28 18.621 33.244 42.963 1.00 37.44 O ANISOU 217 O MET A 28 3682 6637 3906 719 -403 -1558 O ATOM 218 CB MET A 28 21.631 32.569 45.087 1.00 29.53 C ANISOU 218 CB MET A 28 3248 4892 3078 391 -219 -295 C ATOM 219 CG MET A 28 22.419 31.334 45.616 1.00 32.34 C ANISOU 219 CG MET A 28 3146 4351 4788 249 1593 667 C ATOM 220 SD MET A 28 21.348 30.424 46.741 1.00 39.94 S ANISOU 220 SD MET A 28 5202 5776 4195 -27 732 -301 S ATOM 221 CE MET A 28 21.001 31.625 48.066 1.00 39.29 C ANISOU 221 CE MET A 28 4708 5653 4564 819 1391 -1497 C ATOM 222 N ASP A 29 19.978 34.658 44.064 1.00 34.87 N ANISOU 222 N ASP A 29 4772 4868 3607 -32 1049 -138 N ATOM 223 CA ASP A 29 19.353 35.839 43.561 1.00 40.25 C ANISOU 223 CA ASP A 29 4913 5179 5201 656 1224 -611 C ATOM 224 C ASP A 29 20.299 36.631 42.655 1.00 33.84 C ANISOU 224 C ASP A 29 4839 4139 3878 680 856 -789 C ATOM 225 O ASP A 29 20.166 37.880 42.500 1.00 35.01 O ANISOU 225 O ASP A 29 4610 4257 4434 995 1102 -237 O ATOM 226 CB ASP A 29 18.862 36.695 44.699 1.00 37.25 C ANISOU 226 CB ASP A 29 3834 5219 5099 781 469 -1013 C ATOM 227 CG ASP A 29 19.936 37.051 45.713 1.00 41.30 C ANISOU 227 CG ASP A 29 4760 6420 4511 1085 182 -1037 C ATOM 228 OD1 ASP A 29 21.041 36.519 45.714 1.00 34.87 O ANISOU 228 OD1 ASP A 29 4278 4720 4249 392 934 -338 O ATOM 229 OD2 ASP A 29 19.655 37.927 46.600 1.00 41.36 O ANISOU 229 OD2 ASP A 29 6097 5134 4481 -283 1029 -296 O ATOM 230 N CYS A 30 21.253 35.925 42.058 1.00 34.07 N ANISOU 230 N CYS A 30 4340 5204 3401 516 1452 59 N ATOM 231 CA CYS A 30 22.038 36.567 40.976 1.00 32.82 C ANISOU 231 CA CYS A 30 3457 4753 4257 488 1078 588 C ATOM 232 C CYS A 30 21.148 36.832 39.770 1.00 37.97 C ANISOU 232 C CYS A 30 4911 5344 4171 -78 675 441 C ATOM 233 O CYS A 30 20.031 36.258 39.618 1.00 36.29 O ANISOU 233 O CYS A 30 4113 5087 4588 982 985 694 O ATOM 234 CB CYS A 30 23.163 35.645 40.522 1.00 34.14 C ANISOU 234 CB CYS A 30 3540 4901 4532 1144 164 104 C ATOM 235 SG CYS A 30 24.316 35.214 41.859 1.00 35.27 S ANISOU 235 SG CYS A 30 4714 4864 3823 558 705 -169 S ATOM 236 N ARG A 31 21.632 37.651 38.858 1.00 33.17 N ANISOU 236 N ARG A 31 4456 4064 4083 441 38 138 N ATOM 237 CA ARG A 31 20.859 37.915 37.629 1.00 30.62 C ANISOU 237 CA ARG A 31 3494 4862 3276 -207 -297 325 C ATOM 238 C ARG A 31 20.707 36.690 36.742 1.00 35.27 C ANISOU 238 C ARG A 31 4999 3770 4629 449 -754 1059 C ATOM 239 O ARG A 31 21.414 35.717 36.871 1.00 32.90 O ANISOU 239 O ARG A 31 4204 4115 4181 585 224 255 O ATOM 240 CB ARG A 31 21.465 39.043 36.810 1.00 35.70 C ANISOU 240 CB ARG A 31 4862 4298 4402 -609 83 59 C ATOM 241 CG ARG A 31 21.196 40.408 37.318 1.00 43.93 C ANISOU 241 CG ARG A 31 5854 5347 5490 143 -880 -898 C ATOM 242 CD ARG A 31 22.438 41.240 37.175 1.00 61.51 C ANISOU 242 CD ARG A 31 7859 7971 7541 -2079 -838 -1352 C ATOM 243 NE ARG A 31 22.813 41.426 35.807 1.00 59.75 N ANISOU 243 NE ARG A 31 7529 6426 8746 -1205 -288 2136 N ATOM 244 CZ ARG A 31 24.061 41.610 35.356 1.00 87.97 C ANISOU 244 CZ ARG A 31 5764 12438 15220 -279 -4814 -306 C ATOM 245 NH1 ARG A 31 25.092 41.636 36.192 1.00 53.60 N ANISOU 245 NH1 ARG A 31 8614 4875 6874 997 -3286 -261 N ATOM 246 NH2 ARG A 31 24.286 41.759 34.042 1.00103.81 N ANISOU 246 NH2 ARG A 31 14859 7236 17348 922 -1123 4652 N ATOM 247 N TRP A 32 19.786 36.761 35.803 1.00 29.99 N ANISOU 247 N TRP A 32 3451 4619 3323 842 150 597 N ATOM 248 CA TRP A 32 19.607 35.746 34.817 1.00 35.04 C ANISOU 248 CA TRP A 32 3939 5205 4169 703 433 -652 C ATOM 249 C TRP A 32 20.923 35.499 34.143 1.00 28.56 C ANISOU 249 C TRP A 32 3740 3204 3908 292 262 -87 C ATOM 250 O TRP A 32 21.601 36.446 33.802 1.00 32.06 O ANISOU 250 O TRP A 32 3743 3989 4447 79 323 61 O ATOM 251 CB TRP A 32 18.563 36.198 33.811 1.00 31.20 C ANISOU 251 CB TRP A 32 4077 4691 3084 350 379 -479 C ATOM 252 CG TRP A 32 18.236 35.194 32.756 1.00 34.56 C ANISOU 252 CG TRP A 32 4206 4630 4294 273 -1157 -21 C ATOM 253 CD1 TRP A 32 18.609 35.208 31.430 1.00 41.54 C ANISOU 253 CD1 TRP A 32 4625 6478 4677 286 23 84 C ATOM 254 CD2 TRP A 32 17.449 33.989 32.904 1.00 35.16 C ANISOU 254 CD2 TRP A 32 4294 4608 4455 191 86 431 C ATOM 255 NE1 TRP A 32 18.128 34.130 30.777 1.00 35.76 N ANISOU 255 NE1 TRP A 32 4514 5529 3543 -121 316 128 N ATOM 256 CE2 TRP A 32 17.430 33.356 31.599 1.00 43.39 C ANISOU 256 CE2 TRP A 32 5094 6506 4884 -787 1357 -357 C ATOM 257 CE3 TRP A 32 16.785 33.390 33.947 1.00 38.51 C ANISOU 257 CE3 TRP A 32 5133 4680 4819 -569 1150 -350 C ATOM 258 CZ2 TRP A 32 16.766 32.186 31.376 1.00 47.64 C ANISOU 258 CZ2 TRP A 32 6487 5881 5732 -412 755 -478 C ATOM 259 CZ3 TRP A 32 16.126 32.209 33.710 1.00 40.13 C ANISOU 259 CZ3 TRP A 32 4408 5920 4918 -1219 1708 -765 C ATOM 260 CH2 TRP A 32 16.117 31.619 32.454 1.00 47.20 C ANISOU 260 CH2 TRP A 32 5452 6594 5886 -370 1795 -1615 C ATOM 261 N ARG A 33 21.290 34.244 33.983 1.00 30.43 N ANISOU 261 N ARG A 33 4070 4056 3435 853 353 -46 N ATOM 262 CA ARG A 33 22.535 33.856 33.352 1.00 27.90 C ANISOU 262 CA ARG A 33 3038 4827 2734 427 -820 697 C ATOM 263 C ARG A 33 23.758 34.041 34.235 1.00 26.61 C ANISOU 263 C ARG A 33 3113 4073 2923 459 -375 -327 C ATOM 264 O ARG A 33 24.871 34.001 33.773 1.00 30.40 O ANISOU 264 O ARG A 33 4144 4414 2991 366 799 234 O ATOM 265 CB ARG A 33 22.741 34.558 32.005 1.00 30.49 C ANISOU 265 CB ARG A 33 4781 4762 2040 792 614 377 C ATOM 266 CG ARG A 33 23.371 33.668 30.979 1.00 33.24 C ANISOU 266 CG ARG A 33 4557 5530 2542 106 1069 301 C ATOM 267 CD ARG A 33 23.498 34.343 29.627 1.00 44.19 C ANISOU 267 CD ARG A 33 5497 6483 4807 373 187 1380 C ATOM 268 NE ARG A 33 22.226 34.602 28.995 1.00 38.66 N ANISOU 268 NE ARG A 33 4749 5413 4526 1137 305 541 N ATOM 269 CZ ARG A 33 21.652 35.782 28.973 1.00 34.93 C ANISOU 269 CZ ARG A 33 4922 4863 3486 1000 913 1262 C ATOM 270 NH1 ARG A 33 22.236 36.792 29.544 1.00 43.29 N ANISOU 270 NH1 ARG A 33 5053 5590 5803 173 85 1004 N ATOM 271 NH2 ARG A 33 20.490 35.938 28.392 1.00 46.67 N ANISOU 271 NH2 ARG A 33 4806 7732 5192 2065 -219 1418 N ATOM 272 N TRP A 34 23.525 34.226 35.519 1.00 32.53 N ANISOU 272 N TRP A 34 4724 4332 3301 315 162 -16 N ATOM 273 CA TRP A 34 24.573 34.253 36.496 1.00 27.58 C ANISOU 273 CA TRP A 34 3721 3123 3633 220 161 418 C ATOM 274 C TRP A 34 24.279 33.242 37.566 1.00 25.40 C ANISOU 274 C TRP A 34 2629 3273 3747 -229 291 448 C ATOM 275 O TRP A 34 23.183 32.748 37.669 1.00 28.51 O ANISOU 275 O TRP A 34 3163 4259 3408 -281 192 438 O ATOM 276 CB TRP A 34 24.724 35.642 37.108 1.00 28.74 C ANISOU 276 CB TRP A 34 3615 3047 4259 -495 102 224 C ATOM 277 CG TRP A 34 25.159 36.680 36.136 1.00 29.83 C ANISOU 277 CG TRP A 34 3320 4028 3985 125 229 -130 C ATOM 278 CD1 TRP A 34 24.446 37.197 35.092 1.00 30.48 C ANISOU 278 CD1 TRP A 34 4453 3766 3362 507 655 216 C ATOM 279 CD2 TRP A 34 26.436 37.346 36.070 1.00 30.97 C ANISOU 279 CD2 TRP A 34 3672 4560 3535 -388 283 -831 C ATOM 280 NE1 TRP A 34 25.160 38.106 34.425 1.00 32.82 N ANISOU 280 NE1 TRP A 34 4024 4401 4044 -557 533 366 N ATOM 281 CE2 TRP A 34 26.360 38.238 34.943 1.00 32.72 C ANISOU 281 CE2 TRP A 34 4094 3706 4629 -251 -206 -542 C ATOM 282 CE3 TRP A 34 27.592 37.289 36.795 1.00 29.00 C ANISOU 282 CE3 TRP A 34 3291 3466 4262 -353 188 -171 C ATOM 283 CZ2 TRP A 34 27.405 39.022 34.573 1.00 32.14 C ANISOU 283 CZ2 TRP A 34 4561 4059 3589 -5 657 -288 C ATOM 284 CZ3 TRP A 34 28.642 38.103 36.417 1.00 32.58 C ANISOU 284 CZ3 TRP A 34 4409 3718 4250 -563 764 -28 C ATOM 285 CH2 TRP A 34 28.546 38.942 35.331 1.00 32.73 C ANISOU 285 CH2 TRP A 34 5085 3759 3591 -144 371 -145 C ATOM 286 N LYS A 35 25.273 32.932 38.366 1.00 29.36 N ANISOU 286 N LYS A 35 3932 3861 3362 689 -125 495 N ATOM 287 CA LYS A 35 25.115 31.988 39.482 1.00 31.35 C ANISOU 287 CA LYS A 35 4356 3709 3846 -135 -729 294 C ATOM 288 C LYS A 35 26.046 32.393 40.608 1.00 25.86 C ANISOU 288 C LYS A 35 3940 3096 2788 -44 379 -18 C ATOM 289 O LYS A 35 27.024 33.145 40.435 1.00 30.66 O ANISOU 289 O LYS A 35 4468 3551 3628 -311 937 -381 O ATOM 290 CB LYS A 35 25.387 30.534 39.048 1.00 26.30 C ANISOU 290 CB LYS A 35 3945 3381 2667 -110 318 55 C ATOM 291 CG LYS A 35 26.871 30.297 38.601 1.00 27.24 C ANISOU 291 CG LYS A 35 3388 3653 3307 360 525 40 C ATOM 292 CD LYS A 35 27.178 28.846 38.350 1.00 29.26 C ANISOU 292 CD LYS A 35 3499 4077 3539 433 877 250 C ATOM 293 CE LYS A 35 28.609 28.696 37.826 1.00 26.92 C ANISOU 293 CE LYS A 35 3433 3775 3018 479 230 -349 C ATOM 294 NZ LYS A 35 28.947 27.245 37.651 1.00 26.80 N ANISOU 294 NZ LYS A 35 3515 3537 3130 90 109 -327 N ATOM 295 N CYS A 36 25.712 31.909 41.794 1.00 26.98 N ANISOU 295 N CYS A 36 3938 4167 2144 56 56 -124 N ATOM 296 CA CYS A 36 26.403 32.315 43.066 1.00 26.70 C ANISOU 296 CA CYS A 36 3827 4387 1930 437 766 -546 C ATOM 297 C CYS A 36 27.416 31.214 43.391 1.00 24.99 C ANISOU 297 C CYS A 36 3073 3548 2874 -166 176 -964 C ATOM 298 O CYS A 36 27.045 30.004 43.596 1.00 29.97 O ANISOU 298 O CYS A 36 4602 3845 2938 179 282 -71 O ATOM 299 CB CYS A 36 25.280 32.402 44.168 1.00 27.09 C ANISOU 299 CB CYS A 36 2989 4768 2535 -96 510 -452 C ATOM 300 SG CYS A 36 26.051 32.900 45.709 1.00 34.74 S ANISOU 300 SG CYS A 36 4724 5367 3106 44 214 -748 S ATOM 301 N CYS A 37 28.727 31.586 43.510 1.00 25.71 N ANISOU 301 N CYS A 37 3133 3960 2674 -98 214 -942 N ATOM 302 CA CYS A 37 29.757 30.613 43.926 1.00 28.33 C ANISOU 302 CA CYS A 37 3355 4489 2919 311 -205 -823 C ATOM 303 C CYS A 37 30.466 31.245 45.108 1.00 31.03 C ANISOU 303 C CYS A 37 4507 3823 3461 -286 -31 -645 C ATOM 304 O CYS A 37 30.678 32.503 45.171 1.00 32.26 O ANISOU 304 O CYS A 37 4453 4556 3246 -643 -125 -781 O ATOM 305 CB CYS A 37 30.788 30.376 42.856 1.00 27.72 C ANISOU 305 CB CYS A 37 3550 3766 3213 -248 12 -701 C ATOM 306 SG CYS A 37 30.010 29.569 41.441 1.00 31.23 S ANISOU 306 SG CYS A 37 3864 4976 3023 369 24 -855 S ATOM 307 N LYS A 38 30.877 30.368 46.042 1.00 31.84 N ANISOU 307 N LYS A 38 4065 5204 2826 56 -321 -1079 N ATOM 308 CA LYS A 38 31.503 30.837 47.245 1.00 41.75 C ANISOU 308 CA LYS A 38 5655 6294 3912 153 -1743 -977 C ATOM 309 C LYS A 38 32.777 31.539 46.860 1.00 54.07 C ANISOU 309 C LYS A 38 6533 8731 5277 -1160 -864 -1305 C ATOM 310 O LYS A 38 33.537 31.020 46.039 1.00 51.47 O ANISOU 310 O LYS A 38 5649 8768 5139 -149 -1014 -2411 O ATOM 311 CB LYS A 38 31.777 29.652 48.227 1.00 35.15 C ANISOU 311 CB LYS A 38 4870 5967 2516 -201 164 -755 C ATOM 312 CG LYS A 38 32.204 30.176 49.572 1.00 46.27 C ANISOU 312 CG LYS A 38 8966 5667 2948 -167 -1533 -606 C ATOM 313 CD LYS A 38 32.044 29.080 50.546 1.00 55.16 C ANISOU 313 CD LYS A 38 8150 10691 2117 -632 -1123 1594 C ATOM 314 CE LYS A 38 32.197 29.672 51.994 1.00 74.58 C ANISOU 314 CE LYS A 38 12603 11866 3865 -1128 198 504 C ATOM 315 NZ LYS A 38 32.194 28.546 52.930 1.00 77.08 N ANISOU 315 NZ LYS A 38 13981 9943 5360 -384 -270 1135 N ATOM 316 N LYS A 39 33.006 32.703 47.487 1.00 61.07 N ANISOU 316 N LYS A 39 7681 7341 8180 -760 -3625 165 N ATOM 317 CA LYS A 39 34.265 33.456 47.412 1.00 65.62 C ANISOU 317 CA LYS A 39 8428 9271 7231 -2047 -2598 -3239 C ATOM 318 C LYS A 39 35.498 32.512 47.522 1.00 71.53 C ANISOU 318 C LYS A 39 7199 11911 8068 -577 743 1225 C ATOM 319 O LYS A 39 35.579 31.671 48.441 1.00 75.35 O ANISOU 319 O LYS A 39 13936 10757 3937 -128 -2607 -1310 O ATOM 320 CB LYS A 39 34.272 34.525 48.495 1.00 68.88 C ANISOU 320 CB LYS A 39 10983 6184 9002 -1563 2869 -3216 C ATOM 321 CG LYS A 39 33.466 35.758 48.131 1.00102.97 C ANISOU 321 CG LYS A 39 11741 9807 17572 1346 3970 -1130 C ATOM 322 CD LYS A 39 33.905 37.046 48.852 1.00 94.23 C ANISOU 322 CD LYS A 39 11515 11033 13252 -2164 7236 -1449 C ATOM 323 CE LYS A 39 32.782 38.077 48.838 1.00 97.93 C ANISOU 323 CE LYS A 39 13910 6725 16573 -1571 4265 -4939 C ATOM 324 NZ LYS A 39 32.137 38.304 47.500 1.00120.68 N ANISOU 324 NZ LYS A 39 3043 14906 27904 -1538 464 8037 N ATOM 325 N GLY A 40 36.419 32.649 46.557 1.00 74.62 N ANISOU 325 N GLY A 40 8370 12915 7065 -368 2072 -4565 N ATOM 326 CA GLY A 40 37.575 31.740 46.370 1.00 63.68 C ANISOU 326 CA GLY A 40 7899 9215 7079 -734 -867 -894 C ATOM 327 C GLY A 40 37.343 30.554 45.399 1.00118.78 C ANISOU 327 C GLY A 40 20484 9807 14841 2762 1032 -4159 C ATOM 328 O GLY A 40 38.084 29.556 45.492 1.00 93.93 O ANISOU 328 O GLY A 40 12769 8163 14755 -3003 -5138 4627 O ATOM 329 N SER A 41 36.353 30.656 44.477 1.00113.51 N ANISOU 329 N SER A 41 16288 6097 20744 -1466 1417 -4899 N ATOM 330 CA SER A 41 35.838 29.525 43.657 1.00 84.04 C ANISOU 330 CA SER A 41 8115 11028 12786 2108 2310 -5960 C ATOM 331 C SER A 41 36.352 29.358 42.248 1.00 98.00 C ANISOU 331 C SER A 41 17099 13583 6550 -5880 1782 -3611 C ATOM 332 O SER A 41 36.486 30.378 41.554 1.00 97.25 O ANISOU 332 O SER A 41 18547 7086 11316 -1866 213 -1285 O ATOM 333 CB SER A 41 34.321 29.562 43.556 1.00 77.71 C ANISOU 333 CB SER A 41 8239 10976 10309 -4612 -3125 1382 C ATOM 334 OG SER A 41 33.805 28.617 44.426 1.00 57.24 O ANISOU 334 OG SER A 41 6830 7445 7475 -2048 -410 735 O ATOM 335 N GLY A 42 36.520 28.064 41.836 1.00 77.95 N ANISOU 335 N GLY A 42 9329 11087 9200 -5044 1875 957 N ATOM 336 CA GLY A 42 37.230 27.538 40.578 1.00 40.16 C ANISOU 336 CA GLY A 42 4993 6071 4194 -486 -1369 1192 C ATOM 337 C GLY A 42 38.752 27.782 40.768 1.00 86.71 C ANISOU 337 C GLY A 42 5684 12664 14596 701 1185 -1744 C ATOM 338 O GLY A 42 39.600 26.870 40.826 1.00 65.58 O ANISOU 338 O GLY A 42 6600 11041 7273 84 487 -1703 O TER 339 GLY A 42 HETATM 340 O HOH A 201 15.588 39.140 44.473 1.00 38.59 O ANISOU 340 O HOH A 201 3898 4857 5907 -622 271 -326 O HETATM 341 O HOH A 202 24.922 25.994 39.405 1.00 34.65 O ANISOU 341 O HOH A 202 4093 6634 2438 -455 -710 -683 O HETATM 342 O HOH A 203 21.005 33.143 51.282 1.00 45.62 O ANISOU 342 O HOH A 203 6024 6584 4723 -715 1173 -1045 O HETATM 343 O HOH A 205 24.714 37.501 30.725 1.00 39.43 O ANISOU 343 O HOH A 205 5397 5743 3840 176 924 670 O HETATM 344 O HOH A 207 19.998 31.757 34.653 1.00 41.15 O ANISOU 344 O HOH A 207 6211 4398 5024 -888 291 939 O HETATM 345 O HOH A 208 28.221 25.644 35.347 1.00 31.59 O ANISOU 345 O HOH A 208 4438 5036 2528 -709 -282 -10 O HETATM 346 O HOH A 209 20.248 28.595 43.911 1.00 43.84 O ANISOU 346 O HOH A 209 6129 5556 4971 -530 1116 -1181 O HETATM 347 O HOH A 210 22.323 30.872 35.787 1.00 43.01 O ANISOU 347 O HOH A 210 5103 5577 5660 -7 -542 -305 O HETATM 348 O HOH A 211 25.274 26.507 35.440 1.00 36.19 O ANISOU 348 O HOH A 211 4408 4924 4419 -226 567 755 O HETATM 349 O HOH A 212 23.052 28.004 36.687 1.00 45.34 O ANISOU 349 O HOH A 212 6139 5362 5725 -283 1415 -232 O HETATM 350 O HOH A 213 21.932 26.735 46.908 1.00 49.79 O ANISOU 350 O HOH A 213 6746 7339 4830 -1465 2010 689 O HETATM 351 O HOH A 214 24.316 38.617 38.881 1.00 34.93 O ANISOU 351 O HOH A 214 4527 4871 3870 531 268 233 O HETATM 352 O HOH A 215 17.238 39.118 46.800 1.00 45.64 O ANISOU 352 O HOH A 215 5530 5652 6157 564 606 -1828 O HETATM 353 O HOH A 216 31.998 19.078 45.942 1.00 42.50 O ANISOU 353 O HOH A 216 7040 5227 3878 277 1717 881 O HETATM 354 O HOH A 217 38.652 33.069 38.370 1.00 52.70 O ANISOU 354 O HOH A 217 7714 7880 4428 72 -49 -433 O HETATM 355 O HOH A 218 28.062 28.919 52.721 1.00 65.74 O ANISOU 355 O HOH A 218 10995 8863 5119 399 22 -541 O HETATM 356 O HOH A 219 27.907 39.552 43.400 1.00 47.12 O ANISOU 356 O HOH A 219 6091 6126 5686 1454 -151 -1939 O HETATM 357 O HOH A 220 26.409 38.723 45.658 1.00 39.44 O ANISOU 357 O HOH A 220 5661 4714 4607 286 286 -450 O HETATM 358 O HOH A 221 31.913 24.195 49.670 1.00 43.35 O ANISOU 358 O HOH A 221 5540 5714 5214 -123 -258 360 O CONECT 36 35 300 CONECT 88 87 235 CONECT 147 146 306 CONECT 235 88 234 CONECT 300 36 299 CONECT 306 147 305 END If you find results from this site helpful for your research, please cite one of our papers:
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