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HEADER HYDROLASE 02-MAY-14 4QA9
TITLE ENSEMBLE REFINEMENT OF AN EPOXIDE HYDROLASE FROM STREPTOMYCES
TITLE 2 CARZINOSTATICUS SUBSP. NEOCARZINOSTATICUS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES CARZINOSTATICUS SUBSP.
SOURCE 3 NEOCARZINOSTATICUS;
SOURCE 4 ORGANISM_TAXID: 167636;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS, MCSG, ENZYME DISCOVERY FOR NATURAL PRODUCT
KEYWDS 3 BIOSYNTHESIS, NATPRO, EPOXIDE HYDROLASE, PSI-BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
NUMMDL 20
AUTHOR F.WANG,K.TAN,L.BIGELOW,S.CLANCY,G.BABNIGG,C.A.BINGMAN,R.YENNAMALLI,
AUTHOR 2 J.LOHMAN,M.MA,B.SHEN,A.JOACHIMIAK,G.N.PHILLIPS JR.,MIDWEST CENTER
AUTHOR 3 FOR STRUCTURAL GENOMICS (MCSG),ENZYME DISCOVERY FOR NATURAL PRODUCT
AUTHOR 4 BIOSYNTHESIS (NATPRO)
REVDAT 1 21-MAY-14 4QA9 0
JRNL AUTH F.WANG,K.TAN,L.BIGELOW,S.CLANCY,G.BABNIGG,C.A.BINGMAN,
JRNL AUTH 2 R.YENNAMALLI,J.LOHMAN,M.MA,B.SHEN,A.JOACHIMIAK,
JRNL AUTH 3 G.N.PHILLIPS JR.
JRNL TITL ENSEMBLE REFINEMENT OF AN EPOXIDE HYDROLASE FROM
JRNL TITL 2 STREPTOMYCES CARZINOSTATICUS SUBSP. NEOCARZINOSTATICUS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.ENSEMBLE_REFINEMENT: DEV_1420)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 65942
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.123
REMARK 3 R VALUE (WORKING SET) : 0.122
REMARK 3 FREE R VALUE : 0.151
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3343
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 27.8208 - 4.4933 0.99 2943 148 0.1404 0.1322
REMARK 3 2 4.4933 - 3.5689 1.00 2788 152 0.1210 0.1571
REMARK 3 3 3.5689 - 3.1184 0.99 2758 148 0.1378 0.1744
REMARK 3 4 3.1184 - 2.8336 0.99 2736 145 0.1253 0.1520
REMARK 3 5 2.8336 - 2.6307 0.97 2632 160 0.1080 0.1407
REMARK 3 6 2.6307 - 2.4757 0.96 2604 158 0.0977 0.1458
REMARK 3 7 2.4757 - 2.3518 0.97 2620 154 0.0906 0.1059
REMARK 3 8 2.3518 - 2.2494 0.95 2567 148 0.0963 0.1276
REMARK 3 9 2.2494 - 2.1629 0.96 2585 129 0.0950 0.1369
REMARK 3 10 2.1629 - 2.0883 0.96 2568 135 0.0989 0.1316
REMARK 3 11 2.0883 - 2.0230 0.96 2648 131 0.1035 0.1355
REMARK 3 12 2.0230 - 1.9652 0.97 2574 140 0.1030 0.1362
REMARK 3 13 1.9652 - 1.9135 0.96 2591 129 0.1081 0.1564
REMARK 3 14 1.9135 - 1.8668 0.97 2602 139 0.1085 0.1414
REMARK 3 15 1.8668 - 1.8243 0.97 2616 122 0.1115 0.1516
REMARK 3 16 1.8243 - 1.7855 0.97 2590 126 0.1151 0.1579
REMARK 3 17 1.7855 - 1.7498 0.98 2580 158 0.1209 0.1564
REMARK 3 18 1.7498 - 1.7168 0.98 2615 132 0.1326 0.1848
REMARK 3 19 1.7168 - 1.6861 0.98 2648 127 0.1505 0.2017
REMARK 3 20 1.6861 - 1.6576 0.98 2634 139 0.1671 0.1940
REMARK 3 21 1.6576 - 1.6308 0.98 2590 144 0.1739 0.2219
REMARK 3 22 1.6308 - 1.6057 0.96 2533 141 0.1846 0.2285
REMARK 3 23 1.6057 - 1.5821 0.90 2415 118 0.2020 0.2200
REMARK 3 24 1.5821 - 1.5599 0.82 2162 120 0.2160 0.2274
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 NULL
REMARK 3 ANGLE : 1.216 NULL
REMARK 3 CHIRALITY : 0.069 NULL
REMARK 3 PLANARITY : 0.009 NULL
REMARK 3 DIHEDRAL : 9.950 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4QA9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-14.
REMARK 100 THE RCSB ID CODE IS RCSB085800.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65946
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 27.816
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
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) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: PHENIX: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4I19
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULFATE AND 0.1M TRIS:
REMARK 280 HCL, PH 8.5. CYRO WAS ETHYLENE GLYCOL., VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.51300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.66500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.66500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.25650
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.66500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.66500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 123.76950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.66500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.66500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 41.25650
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.66500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.66500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 123.76950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 82.51300
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: 9250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 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 A 512 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 44 CB GLU A 44 CG 0.124
REMARK 500 2 GLU A 44 CB GLU A 44 CG 0.141
REMARK 500 2 VAL A 103 CB VAL A 103 CG2 -0.135
REMARK 500 2 ASP A 174 CB ASP A 174 CG -0.165
REMARK 500 3 SER A 298 CB SER A 298 OG -0.107
REMARK 500 5 MET A 237 CB MET A 237 CG 0.339
REMARK 500 5 ASP A 323 CA ASP A 323 CB 0.147
REMARK 500 7 MET A 237 CB MET A 237 CG -0.197
REMARK 500 8 GLU A 344 CB GLU A 344 CG 0.146
REMARK 500 8 GLU A 367 CB GLU A 367 CG -0.226
REMARK 500 8 GLU A 367 CG GLU A 367 CD -0.098
REMARK 500 9 LYS A 307 CE LYS A 307 NZ 0.196
REMARK 500 14 GLU A 225 CG GLU A 225 CD 0.092
REMARK 500 15 MET A 326 CB MET A 326 CG 0.204
REMARK 500 15 GLU A 344 CB GLU A 344 CG 0.197
REMARK 500 16 MET A 237 CB MET A 237 CG 0.331
REMARK 500 17 SER A 298 CB SER A 298 OG -0.107
REMARK 500 18 GLU A 225 CB GLU A 225 CG 0.118
REMARK 500 20 GLU A 27 CB GLU A 27 CG 0.119
REMARK 500 20 GLU A 344 CB GLU A 344 CG 0.168
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ASP A 174 CB - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500 2 ARG A 226 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 167 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 ARG A 167 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 5 GLU A 211 N - CA - C ANGL. DEV. = -18.6 DEGREES
REMARK 500 5 MET A 326 CG - SD - CE ANGL. DEV. = -14.4 DEGREES
REMARK 500 6 ASP A 217 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 6 ARG A 226 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 ARG A 226 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 6 ASP A 276 CB - CA - C ANGL. DEV. = 17.3 DEGREES
REMARK 500 6 LEU A 356 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 7 MET A 237 CG - SD - CE ANGL. DEV. = 17.2 DEGREES
REMARK 500 7 ARG A 358 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 9 ASP A 187 CB - CG - OD1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 9 LYS A 307 CD - CE - NZ ANGL. DEV. = 18.3 DEGREES
REMARK 500 9 ARG A 340 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 9 ARG A 340 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 10 ARG A 61 CG - CD - NE ANGL. DEV. = 14.7 DEGREES
REMARK 500 10 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 10 ARG A 61 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 10 LEU A 210 CA - CB - CG ANGL. DEV. = 19.4 DEGREES
REMARK 500 10 ARG A 226 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 11 ARG A 50 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 11 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 11 ASP A 323 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 11 MET A 326 CB - CG - SD ANGL. DEV. = -21.7 DEGREES
REMARK 500 13 ARG A 226 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 13 ARG A 358 CG - CD - NE ANGL. DEV. = 13.1 DEGREES
REMARK 500 13 ARG A 358 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 13 ARG A 358 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 14 ARG A 226 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 14 MET A 237 CG - SD - CE ANGL. DEV. = 16.9 DEGREES
REMARK 500 15 ARG A 226 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 15 MET A 237 CB - CG - SD ANGL. DEV. = -30.4 DEGREES
REMARK 500 15 MET A 326 CG - SD - CE ANGL. DEV. = -10.0 DEGREES
REMARK 500 16 ASP A 88 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 16 ASP A 88 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 16 ASP A 229 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 16 MET A 237 CB - CG - SD ANGL. DEV. = -22.4 DEGREES
REMARK 500 16 MET A 237 CG - SD - CE ANGL. DEV. = -22.8 DEGREES
REMARK 500 17 ARG A 220 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 18 ARG A 50 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 18 ARG A 61 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 18 LEU A 210 CB - CG - CD1 ANGL. DEV. = 11.1 DEGREES
REMARK 500 18 GLU A 211 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 18 MET A 237 CB - CG - SD ANGL. DEV. = 22.6 DEGREES
REMARK 500 18 MET A 237 CG - SD - CE ANGL. DEV. = 11.0 DEGREES
REMARK 500 18 ASP A 373 CB - CG - OD1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 19 ASP A 174 CB - CG - OD1 ANGL. DEV. = -8.1 DEGREES
REMARK 500 19 ASP A 174 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 59 ANGLE DEVIATIONS.
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 1 ASP A 73 28.79 43.89
REMARK 500 1 PRO A 99 76.25 -104.50
REMARK 500 1 ALA A 145 -168.34 -123.15
REMARK 500 1 ASP A 174 -133.22 55.88
REMARK 500 1 GLU A 209 -83.53 -121.42
REMARK 500 1 LEU A 210 61.90 -55.05
REMARK 500 1 GLU A 211 -49.05 -160.28
REMARK 500 1 SER A 214 163.66 -49.52
REMARK 500 1 SER A 224 -25.99 -34.95
REMARK 500 1 GLU A 271 -80.11 -104.78
REMARK 500 1 GLN A 349 54.55 -143.02
REMARK 500 2 PRO A 99 77.63 -100.07
REMARK 500 2 HIS A 118 27.01 -143.96
REMARK 500 2 ASP A 174 -135.00 65.87
REMARK 500 2 GLU A 209 -57.33 -123.25
REMARK 500 2 GLU A 271 -95.17 -98.22
REMARK 500 3 ASN A -1 -119.07 -116.19
REMARK 500 3 ASP A 51 -96.62 -80.68
REMARK 500 3 ASP A 174 -133.82 57.45
REMARK 500 3 PRO A 207 49.70 -65.08
REMARK 500 3 ASN A 272 -46.89 -142.87
REMARK 500 3 PHE A 362 66.35 -106.19
REMARK 500 4 ALA A 0 140.23 -31.01
REMARK 500 4 ASP A 30 52.44 -95.68
REMARK 500 4 ASP A 73 61.27 34.81
REMARK 500 4 ALA A 145 -161.52 -100.40
REMARK 500 4 ASP A 174 -121.50 68.46
REMARK 500 4 SER A 252 112.62 -161.69
REMARK 500 4 ASN A 272 -32.23 -141.76
REMARK 500 4 SER A 314 144.29 -171.78
REMARK 500 4 ASP A 357 -23.72 -171.51
REMARK 500 5 ALA A 145 -166.26 -112.67
REMARK 500 5 ASP A 174 -128.26 59.73
REMARK 500 5 LEU A 210 57.56 -115.86
REMARK 500 5 GLU A 211 46.57 -145.83
REMARK 500 5 THR A 212 4.51 -157.03
REMARK 500 5 ASN A 272 -49.32 -146.64
REMARK 500 5 GLU A 275 2.38 -63.26
REMARK 500 5 GLN A 349 58.00 -141.14
REMARK 500 5 GLU A 355 72.86 -117.90
REMARK 500 5 LEU A 356 150.51 -43.39
REMARK 500 6 ASP A 174 -132.66 61.04
REMARK 500 6 GLU A 271 -69.86 -98.29
REMARK 500 6 SER A 314 140.99 -173.43
REMARK 500 6 GLN A 349 57.25 -143.42
REMARK 500 6 GLU A 367 64.35 -119.62
REMARK 500 6 ASP A 373 -67.43 -26.78
REMARK 500 7 HIS A 118 46.75 -140.35
REMARK 500 7 ALA A 145 -154.13 -114.16
REMARK 500 7 ASP A 174 -122.41 51.06
REMARK 500
REMARK 500 THIS ENTRY HAS 165 RAMACHANDRAN OUTLIERS.
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 ASN A -1 ALA A 0 2 -146.40
REMARK 500 LEU A 356 ASP A 357 4 -143.55
REMARK 500 ASN A -1 ALA A 0 7 -149.26
REMARK 500 LEU A 356 ASP A 357 12 -133.00
REMARK 500 SER A 232 GLY A 233 16 144.58
REMARK 500 ALA A 0 MET A 1 17 -125.09
REMARK 500 ALA A 222 VAL A 223 18 144.28
REMARK 500 VAL A 223 SER A 224 19 138.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 2 ASN A -1 24.4 L L OUTSIDE RANGE
REMARK 500 3 ASP A 346 17.0 L L OUTSIDE RANGE
REMARK 500 3 ASP A 357 21.2 L L OUTSIDE RANGE
REMARK 500 4 ASP A 30 23.6 L L OUTSIDE RANGE
REMARK 500 7 ASN A -1 24.0 L L OUTSIDE RANGE
REMARK 500 9 ASP A 229 23.7 L L OUTSIDE RANGE
REMARK 500 18 GLU A 211 46.5 L L OUTSIDE RANGE
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 609 DISTANCE = 5.25 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 416
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4I19 RELATED DB: PDB
REMARK 900 RELATED ID: MCSG-APC109144 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: NATPRO-GO.119835 RELATED DB: TARGETTRACK
DBREF 4QA9 A 1 385 UNP Q84HB8 Q84HB8_STRCZ 1 385
SEQADV 4QA9 SER A -2 UNP Q84HB8 EXPRESSION TAG
SEQADV 4QA9 ASN A -1 UNP Q84HB8 EXPRESSION TAG
SEQADV 4QA9 ALA A 0 UNP Q84HB8 EXPRESSION TAG
SEQRES 1 A 388 SER ASN ALA MET ARG PRO PHE GLN VAL GLN ILE PRO GLN
SEQRES 2 A 388 ALA ASP ILE ASP ASP LEU LYS ARG ARG LEU SER GLU THR
SEQRES 3 A 388 ARG TRP PRO GLU LEU VAL ASP VAL GLY TRP SER ARG GLY
SEQRES 4 A 388 ALA PRO LEU SER TYR ILE LYS GLU LEU ALA GLU TYR TRP
SEQRES 5 A 388 ARG ASP GLY PHE ASP TRP ARG ALA ALA GLU ARG ARG ILE
SEQRES 6 A 388 ASN GLN TYR PRO GLN PHE THR THR GLU ILE ASP GLY ALA
SEQRES 7 A 388 THR ILE HIS PHE LEU HIS VAL ARG SER PRO GLU PRO ASP
SEQRES 8 A 388 ALA THR PRO MET VAL ILE THR HIS GLY TRP PRO GLY THR
SEQRES 9 A 388 PRO VAL GLU PHE LEU ASP ILE ILE GLY PRO LEU THR ASP
SEQRES 10 A 388 PRO ARG ALA HIS GLY GLY ASP PRO ALA ASP ALA PHE HIS
SEQRES 11 A 388 LEU VAL ILE PRO SER LEU PRO GLY PHE GLY LEU SER GLY
SEQRES 12 A 388 PRO LEU LYS SER ALA GLY TRP GLU LEU GLY ARG ILE ALA
SEQRES 13 A 388 MET ALA TRP SER LYS LEU MET ALA SER LEU GLY TYR GLU
SEQRES 14 A 388 ARG TYR ILE ALA GLN GLY GLY ASP ILE GLY ALA PHE THR
SEQRES 15 A 388 SER LEU LEU LEU GLY ALA ILE ASP PRO SER HIS LEU ALA
SEQRES 16 A 388 GLY ILE HIS VAL ASN LEU LEU GLN THR ASN LEU SER GLY
SEQRES 17 A 388 GLU PRO GLY GLU LEU GLU THR LEU SER ASP ALA ASP LYS
SEQRES 18 A 388 ALA ARG LEU ALA VAL SER GLU ARG PHE LEU ASP ASP LEU
SEQRES 19 A 388 SER GLY PRO MET LYS MET GLN SER THR ARG PRO HIS THR
SEQRES 20 A 388 ILE GLY TYR MET LEU ASN ASP SER PRO VAL ALA GLN LEU
SEQRES 21 A 388 ALA TYR LEU LEU GLU MET PHE LYS HIS TRP ALA GLN THR
SEQRES 22 A 388 GLU ASN VAL PRO GLU ASP ALA VAL ASP ARG ASP LEU MET
SEQRES 23 A 388 LEU THR HIS ILE SER LEU PHE TRP PHE THR ALA THR GLY
SEQRES 24 A 388 GLY SER ALA ALA GLN ALA HIS TYR GLU LEU LYS PRO PHE
SEQRES 25 A 388 LEU PRO ILE THR SER LEU ILE GLY ARG SER PRO THR LEU
SEQRES 26 A 388 ASP VAL PRO MET GLY VAL ALA VAL TYR PRO GLY ALA LEU
SEQRES 27 A 388 PHE GLN PRO VAL ARG SER LEU ALA GLU ARG ASP PHE LYS
SEQRES 28 A 388 GLN ILE VAL HIS TRP ALA GLU LEU ASP ARG GLY GLY HIS
SEQRES 29 A 388 PHE SER ALA MET GLU GLU PRO ASP LEU PHE VAL ASP ASP
SEQRES 30 A 388 LEU ARG THR PHE ASN ARG THR LEU LYS LYS LEU
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET EDO A 405 10
HET EDO A 406 10
HET EDO A 407 10
HET EDO A 408 10
HET EDO A 409 10
HET EDO A 410 10
HET EDO A 411 10
HET EDO A 412 10
HET EDO A 413 10
HET EDO A 414 10
HET EDO A 415 10
HET EDO A 416 10
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 EDO 12(C2 H6 O2)
FORMUL 18 HOH *271(H2 O)
HELIX 1 1 PRO A 9 GLU A 22 1 14
HELIX 2 2 PRO A 38 GLY A 52 1 15
HELIX 3 3 ASP A 54 GLN A 64 1 11
HELIX 4 4 THR A 101 GLU A 104 5 4
HELIX 5 5 PHE A 105 ASP A 114 1 10
HELIX 6 6 ASP A 121 ASP A 124 5 4
HELIX 7 7 PHE A 136 GLY A 140 5 5
HELIX 8 8 GLU A 148 GLY A 164 1 17
HELIX 9 9 ASP A 174 ASP A 187 1 14
HELIX 10 10 SER A 214 SER A 224 1 11
HELIX 11 11 SER A 224 LEU A 231 1 8
HELIX 12 12 SER A 232 ARG A 241 1 10
HELIX 13 13 ARG A 241 ASP A 251 1 11
HELIX 14 14 SER A 252 TRP A 267 1 16
HELIX 15 15 VAL A 273 ALA A 277 5 5
HELIX 16 16 ASP A 279 ALA A 294 1 16
HELIX 17 17 THR A 295 LEU A 306 1 12
HELIX 18 18 LYS A 307 LEU A 310 5 4
HELIX 19 19 VAL A 339 PHE A 347 1 9
HELIX 20 20 PHE A 362 GLU A 367 1 6
HELIX 21 21 GLU A 367 LYS A 384 1 18
SHEET 1 A 9 ARG A 2 PHE A 4 0
SHEET 2 A 9 GLN A 67 ILE A 72 -1 O THR A 69 N ARG A 2
SHEET 3 A 9 ALA A 75 VAL A 82 -1 O PHE A 79 N PHE A 68
SHEET 4 A 9 PHE A 126 PRO A 131 -1 O LEU A 128 N VAL A 82
SHEET 5 A 9 THR A 90 THR A 95 1 N MET A 92 O VAL A 129
SHEET 6 A 9 TYR A 168 GLY A 172 1 O GLN A 171 N VAL A 93
SHEET 7 A 9 LEU A 191 VAL A 196 1 O HIS A 195 N ALA A 170
SHEET 8 A 9 MET A 326 VAL A 330 1 O GLY A 327 N ILE A 194
SHEET 9 A 9 ILE A 350 GLU A 355 1 O ALA A 354 N VAL A 330
CISPEP 1 TRP A 98 PRO A 99 1 6.65
CISPEP 2 TRP A 98 PRO A 99 2 1.76
CISPEP 3 TRP A 98 PRO A 99 3 8.18
CISPEP 4 TRP A 98 PRO A 99 4 -6.01
CISPEP 5 TRP A 98 PRO A 99 5 -2.82
CISPEP 6 TRP A 98 PRO A 99 6 3.05
CISPEP 7 TRP A 98 PRO A 99 7 -10.72
CISPEP 8 TRP A 98 PRO A 99 8 1.59
CISPEP 9 TRP A 98 PRO A 99 9 -5.52
CISPEP 10 TRP A 98 PRO A 99 10 -3.46
CISPEP 11 TRP A 98 PRO A 99 11 -4.24
CISPEP 12 TRP A 98 PRO A 99 12 7.39
CISPEP 13 TRP A 98 PRO A 99 13 -0.92
CISPEP 14 TRP A 98 PRO A 99 14 -4.66
CISPEP 15 TRP A 98 PRO A 99 15 3.62
CISPEP 16 TRP A 98 PRO A 99 16 -1.87
CISPEP 17 TRP A 98 PRO A 99 17 3.69
CISPEP 18 TRP A 98 PRO A 99 18 5.71
CISPEP 19 TRP A 98 PRO A 99 19 0.76
CISPEP 20 TRP A 98 PRO A 99 20 -6.71
SITE 1 AC1 4 LEU A 213 SER A 214 ASP A 215 LYS A 218
SITE 1 AC2 4 SER A -2 ILE A 72 ASP A 73 LYS A 158
SITE 1 AC3 2 PRO A 9 HOH A 682
SITE 1 AC4 4 ARG A 61 GLN A 64 TYR A 65 HOH A 723
SITE 1 AC5 8 GLN A 200 THR A 201 ASN A 202 LEU A 342
SITE 2 AC5 8 ALA A 343 ASP A 346 PHE A 347 EDO A 408
SITE 1 AC6 7 ASP A 174 PHE A 227 MET A 235 TRP A 267
SITE 2 AC6 7 LEU A 335 HOH A 621 HOH A 669
SITE 1 AC7 5 PHE A 178 PHE A 309 SER A 319 EDO A 408
SITE 2 AC7 5 HOH A 574
SITE 1 AC8 7 LEU A 181 LEU A 199 GLN A 200 SER A 319
SITE 2 AC8 7 EDO A 405 EDO A 407 EDO A 410
SITE 1 AC9 6 PRO A 85 ASP A 114 ARG A 116 ALA A 117
SITE 2 AC9 6 ALA A 185 HOH A 720
SITE 1 BC1 6 PHE A 178 LEU A 181 LEU A 199 GLN A 200
SITE 2 BC1 6 EDO A 408 HOH A 632
SITE 1 BC2 6 ASP A 174 ILE A 175 PHE A 178 HOH A 621
SITE 2 BC2 6 HOH A 669 HOH A 698
SITE 1 BC3 5 ILE A 13 LEU A 16 LYS A 17 TRP A 49
SITE 2 BC3 5 PHE A 292
SITE 1 BC4 2 ARG A 61 LEU A 282
SITE 1 BC5 8 PRO A 134 PHE A 136 TRP A 147 ALA A 302
SITE 2 BC5 8 GLU A 305 LEU A 306 HOH A 515 HOH A 715
SITE 1 BC6 3 PRO A 308 THR A 313 HOH A 637
SITE 1 BC7 4 GLY A 164 ILE A 316 HOH A 704 HOH A 712
CRYST1 75.330 75.330 165.026 90.00 90.00 90.00 P 41 21 2 8
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 0.013275 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013275 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006060 0.00000
MODEL 1
TER 6047 LEU A 385
ENDMDL
MODEL 2
TER 6047 LEU A 385
ENDMDL
MODEL 3
TER 6047 LEU A 385
ENDMDL
MODEL 4
TER 6047 LEU A 385
ENDMDL
MODEL 5
TER 6047 LEU A 385
ENDMDL
MODEL 6
TER 6047 LEU A 385
ENDMDL
MODEL 7
TER 6047 LEU A 385
ENDMDL
MODEL 8
TER 6047 LEU A 385
ENDMDL
MODEL 9
TER 6047 LEU A 385
ENDMDL
MODEL 10
TER 6047 LEU A 385
ENDMDL
MODEL 11
TER 6047 LEU A 385
ENDMDL
MODEL 12
TER 6047 LEU A 385
ENDMDL
MODEL 13
TER 6047 LEU A 385
ENDMDL
MODEL 14
TER 6047 LEU A 385
ENDMDL
MODEL 15
TER 6047 LEU A 385
ENDMDL
MODEL 16
TER 6047 LEU A 385
ENDMDL
MODEL 17
TER 6047 LEU A 385
ENDMDL
MODEL 18
TER 6047 LEU A 385
ENDMDL
MODEL 19
TER 6047 LEU A 385
ENDMDL
MODEL 20
TER 6047 LEU A 385
ENDMDL
MASTER 547 0 16 21 9 0 25 6 3390 1 140 30
END |