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*** HYDROLASE 18-AUG-15 5D8Z ***elNémo ID: 21031823295283691Job options:ID = 21031823295283691 JOBID = HYDROLASE 18-AUG-15 5D8Z USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER HYDROLASE 18-AUG-15 5D8Z TITLE STRUCTRUE OF A LUCIDUM PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENDOGLUCANASE; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GANODERMA LUCIDUM; SOURCE 3 ORGANISM_TAXID: 5315; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS GH5 FAMILY, GANODERMA LUCIDUM, ENDOGLUCANASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR R.GUO,Q.LI,N.SHANG,G.LIU,T.P.KO,C.C.CHEN,W.LIU REVDAT 3 29-JUL-20 5D8Z 1 COMPND REMARK HET HETNAM REVDAT 3 2 1 FORMUL LINK SITE ATOM REVDAT 2 23-MAY-18 5D8Z 1 REMARK REVDAT 1 29-JUN-16 5D8Z 0 JRNL AUTH G.LIU,Q.LI,N.SHANG,J.W.HUANG,T.P.KO,W.LIU,Y.ZHENG,X.HAN, JRNL AUTH 2 Y.CHEN,C.C.CHEN,J.JIN,R.T.GUO JRNL TITL FUNCTIONAL AND STRUCTURAL ANALYSES OF A JRNL TITL 2 1,4-BETA-ENDOGLUCANASE FROM GANODERMA LUCIDUM. JRNL REF ENZYME.MICROB.TECHNOL. V. 86 67 2016 JRNL REFN ISSN 0141-0229 JRNL PMID 26992795 JRNL DOI 10.1016/J.ENZMICTEC.2016.01.013 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0049 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0 REMARK 3 NUMBER OF REFLECTIONS : 20753 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) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.179 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200 REMARK 3 FREE R VALUE TEST SET COUNT : 1132 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) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1389 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.25 REMARK 3 BIN R VALUE (WORKING SET) : 0.3170 REMARK 3 BIN FREE R VALUE SET COUNT : 66 REMARK 3 BIN FREE R VALUE : 0.3590 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4864 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 46 REMARK 3 SOLVENT ATOMS : 73 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.03 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.86000 REMARK 3 B22 (A**2) : -4.22000 REMARK 3 B33 (A**2) : 2.36000 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): 1.261 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.325 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.240 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.887 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5043 ; 0.013 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): 4384 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6910 ; 1.598 ; 1.915 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10056 ; 0.908 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 646 ; 7.756 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 254 ;43.123 ;25.984 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 662 ;16.887 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;19.399 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 752 ; 0.095 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6058 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1232 ; 0.001 ; 0.020 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): 2590 ; 3.078 ; 4.531 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2589 ; 3.072 ; 4.529 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3234 ; 4.778 ; 6.793 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3235 ; 4.778 ; 6.795 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2453 ; 3.747 ; 4.823 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2453 ; 3.739 ; 4.823 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3677 ; 5.721 ; 7.133 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5932 ; 7.800 ;37.140 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5924 ; 7.769 ;37.124 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL 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 : 1.20 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 REMARK 4 REMARK 4 5D8Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-AUG-15. REMARK 100 THE DEPOSITION ID IS D_1000212865. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-MAY-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSRRC REMARK 200 BEAMLINE : BL13B1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97622 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21889 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4 REMARK 200 DATA REDUNDANCY : 7.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 20.4100 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: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3QR3 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM CHLORIDE HEXAHYDRATE, REMARK 280 0.1M BIS-TRIS PH 5.5, 25% W/V POLYETHYLENE GLYCOL 3350, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.79250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.79250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 42.21300 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 118.19950 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.21300 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 118.19950 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 41.79250 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.21300 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 118.19950 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 41.79250 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.21300 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 118.19950 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN A 1 REMARK 465 SER A 2 REMARK 465 THR A 3 REMARK 465 VAL A 4 REMARK 465 PRO A 5 REMARK 465 ALA A 6 REMARK 465 TRP A 7 REMARK 465 GLY A 8 REMARK 465 GLN A 9 REMARK 465 CYS A 10 REMARK 465 GLY A 11 REMARK 465 GLY A 12 REMARK 465 SER A 13 REMARK 465 VAL A 14 REMARK 465 PRO A 15 REMARK 465 ALA A 16 REMARK 465 SER A 17 REMARK 465 SER A 18 REMARK 465 ALA A 19 REMARK 465 GLY A 20 REMARK 465 LYS A 21 REMARK 465 GLN A 346 REMARK 465 LYS A 347 REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 THR B 3 REMARK 465 VAL B 4 REMARK 465 PRO B 5 REMARK 465 ALA B 6 REMARK 465 TRP B 7 REMARK 465 GLY B 8 REMARK 465 GLN B 9 REMARK 465 CYS B 10 REMARK 465 GLY B 11 REMARK 465 GLY B 12 REMARK 465 SER B 13 REMARK 465 VAL B 14 REMARK 465 PRO B 15 REMARK 465 ALA B 16 REMARK 465 SER B 17 REMARK 465 SER B 18 REMARK 465 ALA B 19 REMARK 465 GLY B 20 REMARK 465 LYS B 21 REMARK 465 GLN B 346 REMARK 465 LYS B 347 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O GLN B 53 N TYR B 55 2.05 REMARK 500 O LEU A 51 O GLN A 53 2.13 REMARK 500 O ALA A 148 O LYS A 150 2.14 REMARK 500 O HOH A 552 O HOH B 520 2.15 REMARK 500 OD1 ASP A 224 OG SER A 226 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH B 520 O HOH B 520 3555 1.78 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 43 75.95 -27.45 REMARK 500 GLN A 53 167.34 72.90 REMARK 500 TYR A 54 5.82 45.86 REMARK 500 ASN A 73 -35.05 -143.56 REMARK 500 HIS A 120 59.50 -95.11 REMARK 500 ALA A 123 16.31 59.07 REMARK 500 ASN A 126 68.03 34.44 REMARK 500 TYR A 151 -4.95 66.41 REMARK 500 ASP A 167 49.60 34.07 REMARK 500 ASN A 201 55.14 39.87 REMARK 500 THR A 203 38.77 39.39 REMARK 500 ASN A 242 23.11 47.46 REMARK 500 THR A 251 161.84 179.35 REMARK 500 ASN A 253 11.21 59.30 REMARK 500 ALA A 257 -64.54 -134.19 REMARK 500 ALA A 310 87.91 133.71 REMARK 500 ALA A 311 -149.85 -120.04 REMARK 500 CYS A 340 -52.89 -125.71 REMARK 500 ASN A 344 46.08 -74.73 REMARK 500 THR B 52 152.00 -47.95 REMARK 500 GLN B 53 179.05 83.21 REMARK 500 TYR B 54 8.33 35.63 REMARK 500 HIS B 120 61.62 -103.04 REMARK 500 ALA B 123 12.55 53.65 REMARK 500 ASN B 126 54.99 35.36 REMARK 500 HIS B 166 -47.85 -140.58 REMARK 500 ALA B 190 77.14 -101.37 REMARK 500 ASP B 224 5.20 -69.20 REMARK 500 ASN B 253 -11.74 73.65 REMARK 500 ALA B 257 -61.95 -130.70 REMARK 500 ASN B 281 56.68 -99.28 REMARK 500 SER B 300 -7.99 -59.12 REMARK 500 ALA B 310 91.00 137.66 REMARK 500 ALA B 311 -152.17 -121.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 PHE A 72 ASN A 73 -147.74 REMARK 500 TRP A 309 ALA A 310 130.47 REMARK 500 TRP B 309 ALA B 310 131.27 REMARK 500 REMARK 500 REMARK: NULL 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 A 553 DISTANCE = 6.07 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5D8W RELATED DB: PDB DBREF 5D8Z A 1 347 PDB 5D8Z 5D8Z 1 347 DBREF 5D8Z B 1 347 PDB 5D8Z 5D8Z 1 347 SEQRES 1 A 347 GLN SER THR VAL PRO ALA TRP GLY GLN CYS GLY GLY SER SEQRES 2 A 347 VAL PRO ALA SER SER ALA GLY LYS LEU GLN PHE ALA GLY SEQRES 3 A 347 VAL ASN ILE ALA GLY PHE ASP PHE GLY CYS GLY SER ASP SEQRES 4 A 347 GLY THR CYS ASN ALA SER GLY ALA TRP PRO PRO LEU THR SEQRES 5 A 347 GLN TYR TYR GLY ALA ASP GLY ALA GLY GLN MET LYS HIS SEQRES 6 A 347 PHE VAL ASP ASP ASP GLY PHE ASN VAL PHE ARG LEU PRO SEQRES 7 A 347 VAL GLY TRP GLN PHE ILE THR ASP GLY VAL ALA GLY GLY SEQRES 8 A 347 ASP ILE ASP GLU ASP ASN TRP ALA GLU TYR ASP ALA LEU SEQRES 9 A 347 VAL GLN ALA CYS LEU ASP ALA GLY ALA SER CYS ILE VAL SEQRES 10 A 347 ASP VAL HIS ASN TYR ALA ARG PHE ASN GLY GLU ILE ILE SEQRES 11 A 347 GLY GLN GLY GLY PRO THR ASN GLN ASP PHE ALA ALA LEU SEQRES 12 A 347 TRP SER SER ILE ALA ALA LYS TYR ALA ASP ASN ASP LYS SEQRES 13 A 347 ILE ILE PHE GLY VAL MET ASN GLU PRO HIS ASP VAL PRO SEQRES 14 A 347 ASP ILE ASN LEU TRP ALA ASP SER VAL GLN ALA ALA VAL SEQRES 15 A 347 THR ALA ILE ARG GLN ALA GLY ALA THR SER GLN ILE ILE SEQRES 16 A 347 LEU LEU PRO GLY ASN ASN TRP THR SER ALA GLU THR PHE SEQRES 17 A 347 VAL SER ASN GLY SER ALA ASP ALA LEU LYS LYS VAL THR SEQRES 18 A 347 ASN PRO ASP GLY SER VAL THR ASN LEU ILE PHE ASP VAL SEQRES 19 A 347 HIS LYS TYR LEU ASP SER ASP ASN SER GLY THR HIS GLU SEQRES 20 A 347 GLU CYS THR THR ASN ASN ILE ASP ASN ALA TRP ALA PRO SEQRES 21 A 347 LEU ALA GLU TRP LEU ARG CYS ASN GLY ARG GLN ALA PHE SEQRES 22 A 347 ASN THR GLU THR GLY GLY GLY ASN VAL ALA SER CYS GLU SEQRES 23 A 347 THR PHE MET CYS GLN GLN VAL ALA TYR GLN ASN ALA ASN SEQRES 24 A 347 SER ASP VAL PHE LEU GLY TYR VAL GLY TRP ALA ALA GLY SEQRES 25 A 347 ASN PHE TYR GLN GLY TYR VAL LEU GLY GLU VAL PRO THR SEQRES 26 A 347 ASP THR ASN GLY VAL TRP THR ASP THR ALA LEU VAL SER SEQRES 27 A 347 ALA CYS LEU ALA PRO ASN ALA GLN LYS SEQRES 1 B 347 GLN SER THR VAL PRO ALA TRP GLY GLN CYS GLY GLY SER SEQRES 2 B 347 VAL PRO ALA SER SER ALA GLY LYS LEU GLN PHE ALA GLY SEQRES 3 B 347 VAL ASN ILE ALA GLY PHE ASP PHE GLY CYS GLY SER ASP SEQRES 4 B 347 GLY THR CYS ASN ALA SER GLY ALA TRP PRO PRO LEU THR SEQRES 5 B 347 GLN TYR TYR GLY ALA ASP GLY ALA GLY GLN MET LYS HIS SEQRES 6 B 347 PHE VAL ASP ASP ASP GLY PHE ASN VAL PHE ARG LEU PRO SEQRES 7 B 347 VAL GLY TRP GLN PHE ILE THR ASP GLY VAL ALA GLY GLY SEQRES 8 B 347 ASP ILE ASP GLU ASP ASN TRP ALA GLU TYR ASP ALA LEU SEQRES 9 B 347 VAL GLN ALA CYS LEU ASP ALA GLY ALA SER CYS ILE VAL SEQRES 10 B 347 ASP VAL HIS ASN TYR ALA ARG PHE ASN GLY GLU ILE ILE SEQRES 11 B 347 GLY GLN GLY GLY PRO THR ASN GLN ASP PHE ALA ALA LEU SEQRES 12 B 347 TRP SER SER ILE ALA ALA LYS TYR ALA ASP ASN ASP LYS SEQRES 13 B 347 ILE ILE PHE GLY VAL MET ASN GLU PRO HIS ASP VAL PRO SEQRES 14 B 347 ASP ILE ASN LEU TRP ALA ASP SER VAL GLN ALA ALA VAL SEQRES 15 B 347 THR ALA ILE ARG GLN ALA GLY ALA THR SER GLN ILE ILE SEQRES 16 B 347 LEU LEU PRO GLY ASN ASN TRP THR SER ALA GLU THR PHE SEQRES 17 B 347 VAL SER ASN GLY SER ALA ASP ALA LEU LYS LYS VAL THR SEQRES 18 B 347 ASN PRO ASP GLY SER VAL THR ASN LEU ILE PHE ASP VAL SEQRES 19 B 347 HIS LYS TYR LEU ASP SER ASP ASN SER GLY THR HIS GLU SEQRES 20 B 347 GLU CYS THR THR ASN ASN ILE ASP ASN ALA TRP ALA PRO SEQRES 21 B 347 LEU ALA GLU TRP LEU ARG CYS ASN GLY ARG GLN ALA PHE SEQRES 22 B 347 ASN THR GLU THR GLY GLY GLY ASN VAL ALA SER CYS GLU SEQRES 23 B 347 THR PHE MET CYS GLN GLN VAL ALA TYR GLN ASN ALA ASN SEQRES 24 B 347 SER ASP VAL PHE LEU GLY TYR VAL GLY TRP ALA ALA GLY SEQRES 25 B 347 ASN PHE TYR GLN GLY TYR VAL LEU GLY GLU VAL PRO THR SEQRES 26 B 347 ASP THR ASN GLY VAL TRP THR ASP THR ALA LEU VAL SER SEQRES 27 B 347 ALA CYS LEU ALA PRO ASN ALA GLN LYS HET BGC C 1 12 HET BGC C 2 11 HET BGC D 1 12 HET BGC D 2 11 HETNAM BGC BETA-D-GLUCOPYRANOSE FORMUL 3 BGC 4(C6 H12 O6) FORMUL 5 HOH *73(H2 O) HELIX 1 AA1 ASP A 58 ASP A 69 1 12 HELIX 2 AA2 GLY A 80 ASP A 86 1 7 HELIX 3 AA3 ASP A 94 ALA A 111 1 18 HELIX 4 AA4 THR A 136 LYS A 150 1 15 HELIX 5 AA5 ASP A 170 ALA A 188 1 19 HELIX 6 AA6 GLY A 199 SER A 204 1 6 HELIX 7 AA7 GLY A 212 LYS A 219 1 8 HELIX 8 AA8 ALA A 257 ASN A 268 1 12 HELIX 9 AA9 VAL A 282 ASN A 299 1 18 HELIX 10 AB1 THR A 334 CYS A 340 1 7 HELIX 11 AB2 ALA B 44 ALA B 47 5 4 HELIX 12 AB3 ASP B 58 ASP B 69 1 12 HELIX 13 AB4 GLY B 80 ASP B 86 1 7 HELIX 14 AB5 ASP B 94 ALA B 111 1 18 HELIX 15 AB6 THR B 136 ALA B 152 1 17 HELIX 16 AB7 ASP B 170 ALA B 188 1 19 HELIX 17 AB8 GLY B 199 SER B 204 1 6 HELIX 18 AB9 GLY B 212 LYS B 218 1 7 HELIX 19 AC1 ALA B 257 ASN B 268 1 12 HELIX 20 AC2 VAL B 282 ALA B 298 1 17 HELIX 21 AC3 THR B 334 CYS B 340 1 7 SHEET 1 AA1 9 PHE A 24 ALA A 30 0 SHEET 2 AA1 9 VAL A 74 VAL A 79 1 O ARG A 76 N ILE A 29 SHEET 3 AA1 9 SER A 114 VAL A 119 1 O ILE A 116 N PHE A 75 SHEET 4 AA1 9 ILE A 157 GLY A 160 1 O ILE A 158 N VAL A 117 SHEET 5 AA1 9 ILE A 194 PRO A 198 1 O LEU A 196 N PHE A 159 SHEET 6 AA1 9 LEU A 230 HIS A 235 1 O ASP A 233 N LEU A 197 SHEET 7 AA1 9 ALA A 272 THR A 277 1 O PHE A 273 N VAL A 234 SHEET 8 AA1 9 PHE A 303 GLY A 312 1 O TRP A 309 N THR A 277 SHEET 9 AA1 9 PHE A 24 ALA A 30 1 N ASN A 28 O GLY A 308 SHEET 1 AA2 2 ARG A 124 PHE A 125 0 SHEET 2 AA2 2 GLU A 128 ILE A 129 -1 O GLU A 128 N PHE A 125 SHEET 1 AA3 2 THR A 325 THR A 327 0 SHEET 2 AA3 2 VAL A 330 THR A 332 -1 O VAL A 330 N THR A 327 SHEET 1 AA4 9 PHE B 24 ALA B 30 0 SHEET 2 AA4 9 VAL B 74 VAL B 79 1 O ARG B 76 N ILE B 29 SHEET 3 AA4 9 SER B 114 VAL B 119 1 O ILE B 116 N LEU B 77 SHEET 4 AA4 9 ILE B 157 GLY B 160 1 O ILE B 158 N VAL B 117 SHEET 5 AA4 9 ILE B 195 PRO B 198 1 O LEU B 196 N PHE B 159 SHEET 6 AA4 9 LEU B 230 HIS B 235 1 O ILE B 231 N LEU B 197 SHEET 7 AA4 9 ALA B 272 THR B 277 1 O PHE B 273 N PHE B 232 SHEET 8 AA4 9 PHE B 303 GLY B 312 1 O LEU B 304 N ALA B 272 SHEET 9 AA4 9 PHE B 24 ALA B 30 1 N PHE B 24 O LEU B 304 SHEET 1 AA5 2 CYS B 36 GLY B 37 0 SHEET 2 AA5 2 THR B 41 CYS B 42 -1 O THR B 41 N GLY B 37 SHEET 1 AA6 2 ARG B 124 PHE B 125 0 SHEET 2 AA6 2 GLU B 128 ILE B 129 -1 O GLU B 128 N PHE B 125 SHEET 1 AA7 2 THR B 325 THR B 327 0 SHEET 2 AA7 2 VAL B 330 THR B 332 -1 O THR B 332 N THR B 325 SSBOND 1 CYS A 36 CYS A 42 1555 1555 2.09 SSBOND 2 CYS A 108 CYS A 115 1555 1555 2.05 SSBOND 3 CYS A 249 CYS A 285 1555 1555 2.02 SSBOND 4 CYS A 290 CYS A 340 1555 1555 2.10 SSBOND 5 CYS B 36 CYS B 42 1555 1555 2.07 SSBOND 6 CYS B 108 CYS B 115 1555 1555 2.05 SSBOND 7 CYS B 249 CYS B 285 1555 1555 2.06 SSBOND 8 CYS B 290 CYS B 340 1555 1555 2.03 LINK O4 BGC C 1 C1 BGC C 2 1555 1555 1.44 LINK O4 BGC D 1 C1 BGC D 2 1555 1555 1.43 CRYST1 84.426 236.399 83.585 90.00 90.00 90.00 C 2 2 21 16 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 0.011845 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004230 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011964 0.00000 ATOM 4867 C2 BGC C 1 -1.822 -25.579 -8.511 1.00 90.25 C ATOM 4868 C3 BGC C 1 -2.743 -24.492 -7.921 1.00 90.59 C ATOM 4869 C4 BGC C 1 -1.990 -23.563 -6.942 1.00 89.85 C ATOM 4870 C5 BGC C 1 -0.522 -23.265 -7.372 1.00 90.03 C ATOM 4871 C6 BGC C 1 0.358 -22.869 -6.189 1.00 84.96 C ATOM 4872 C1 BGC C 1 -0.556 -24.944 -9.094 1.00 93.77 C ATOM 4873 O1 BGC C 1 0.262 -25.922 -9.750 1.00 90.66 O ATOM 4874 O2 BGC C 1 -2.513 -26.328 -9.517 1.00 79.74 O ATOM 4875 O3 BGC C 1 -3.885 -25.104 -7.276 1.00 87.32 O ATOM 4876 O4 BGC C 1 -2.690 -22.303 -6.818 1.00 85.62 O ATOM 4877 O5 BGC C 1 0.177 -24.342 -8.025 1.00 89.53 O ATOM 4878 O6 BGC C 1 1.719 -22.902 -6.625 1.00 78.67 O ATOM 4879 C2 BGC C 2 -4.012 -20.639 -5.590 1.00 80.07 C ATOM 4880 C3 BGC C 2 -5.380 -20.312 -4.951 1.00 82.25 C ATOM 4881 C4 BGC C 2 -6.522 -21.110 -5.555 1.00 76.48 C ATOM 4882 C5 BGC C 2 -6.151 -22.604 -5.655 1.00 74.28 C ATOM 4883 C6 BGC C 2 -7.169 -23.375 -6.492 1.00 72.61 C ATOM 4884 C1 BGC C 2 -3.729 -22.146 -5.828 1.00 84.47 C ATOM 4885 O2 BGC C 2 -2.996 -20.099 -4.738 1.00 64.47 O ATOM 4886 O3 BGC C 2 -5.759 -18.930 -5.118 1.00 88.65 O ATOM 4887 O4 BGC C 2 -7.703 -20.795 -4.778 1.00 68.78 O ATOM 4888 O5 BGC C 2 -4.889 -22.841 -6.302 1.00 82.82 O ATOM 4889 O6 BGC C 2 -6.585 -23.914 -7.683 1.00 64.45 O TER If you find results from this site helpful for your research, please cite one of our papers:
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