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1A0J.pdb
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HEADER SERINE PROTEASE 01-DEC-97 1A0J
TITLE CRYSTAL STRUCTURE OF A NON-PSYCHROPHILIC TRYPSIN FROM A COLD-ADAPTED
TITLE 2 FISH SPECIES.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.4.21.4;
COMPND 5 OTHER_DETAILS: BENZAMIDINE INHIBITOR IN THE ACTIVE SITE. THE AMINO
COMPND 6 ACID NUMBERING SCHEME USED IS ADOPTED FROM CHYMOTRYPSINOGEN.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMO SALAR;
SOURCE 3 ORGANISM_COMMON: ATLANTIC SALMON;
SOURCE 4 ORGANISM_TAXID: 8030;
SOURCE 5 ORGAN: PANCREAS
KEYWDS SERINE PROTEINASE, TRYPSIN, HYDROLASE, SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-K.SCHROEDER,N.P.WILLASSEN,A.O.SMALAAS
REVDAT 3 13-JUL-11 1A0J 1 VERSN
REVDAT 2 24-FEB-09 1A0J 1 VERSN
REVDAT 1 13-JAN-99 1A0J 0
JRNL AUTH H.K.SCHRODER,N.P.WILLASSEN,A.O.SMALAS
JRNL TITL STRUCTURE OF A NON-PSYCHROPHILIC TRYPSIN FROM A COLD-ADAPTED
JRNL TITL 2 FISH SPECIES.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 54 780 1998
JRNL REFN ISSN 0907-4449
JRNL PMID 9757092
JRNL DOI 10.1107/S0907444997018611
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 73.1
REMARK 3 NUMBER OF REFLECTIONS : 68062
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 SET) : 0.173
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3866
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 34.21
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2986
REMARK 3 BIN R VALUE (WORKING SET) : 0.2347
REMARK 3 BIN FREE R VALUE : 0.2121
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 163
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6640
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 87
REMARK 3 SOLVENT ATOMS : 379
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.93
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 2.70
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.35
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.09
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 4 : TOPH19X.PRO
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 NCS RESTRAINTS WERE INCLUDED IN THE FIRST REFINEMENT ROUNDS, THEN
REMARK 3 LEFT OUT. THE ELECTRON DENSITY INDICATES A
REMARK 3 CALCIUM ION FOR ONLY ONE OF THE FOUR MOLECULES (MOL A).
REMARK 3
REMARK 3 THE ELECTRON DENSITY INDICATES A CALCIUM ION FOR ONLY ONE
REMARK 3 OF THE FOUR MOLECULES (MOL A).
REMARK 4
REMARK 4 1A0J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : AUG-96
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGEPLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, XDS
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76357
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 28.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.2
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 52.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.25800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3PTB BOVINE TRYPSIN, WITH CORRECT AMINO
REMARK 200 ACID SEQUENCE SUPERIMPOSED ONTO ANIONIC SALMON TRYPSIN 2TBS.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.95350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.39350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.55350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.39350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.95350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.55350
REMARK 290 SMTRY3 4 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -162.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 32.95350
REMARK 350 BIOMT2 1 0.000000 -1.000000 0.000000 41.55350
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 154.78700
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 GLU B 77
REMARK 475 GLY D 78
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 24 CA CB CG CD CE NZ
REMARK 480 ASN A 25 CB CG OD1 ND2
REMARK 480 SER A 37 CA CB OG
REMARK 480 TYR A 39 CD1 CE1
REMARK 480 PHE A 41 CD1 CE1
REMARK 480 LYS A 60 CD CE NZ
REMARK 480 ARG A 97 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 110 CG CE NZ
REMARK 480 ARG A 135 CD NE CZ NH1 NH2
REMARK 480 ARG A 222 CG CD NE CZ NH1 NH2
REMARK 480 ARG B 23 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS B 24 O CB CG CD CE
REMARK 480 ASN B 25 CA C O CG OD1 ND2
REMARK 480 TYR B 39 CD1 CE1 CZ
REMARK 480 GLU B 70 CB CG
REMARK 480 ASN B 76 N CA CB CG OD1 ND2
REMARK 480 GLY B 78 O
REMARK 480 THR B 79 OG1 CG2
REMARK 480 GLU B 80 CG CD OE1 OE2
REMARK 480 PHE B 82 CD1 CE1
REMARK 480 ARG B 97 NE CZ NH1 NH2
REMARK 480 LYS B 110 CD CE NZ
REMARK 480 SER B 116 CA CB OG
REMARK 480 TYR B 117 CD1 CD2 CE1 CE2 CZ OH
REMARK 480 ARG B 135 CG CD NE CZ NH1 NH2
REMARK 480 GLN B 192 CD OE1 NE2
REMARK 480 ARG C 23 CG CD NE CZ NH1 NH2
REMARK 480 LYS C 24 CB CG CD NZ
REMARK 480 ASN C 25 CB CG OD1 ND2
REMARK 480 TYR C 39 CB CG CD1 CD2 OH
REMARK 480 HIS C 40 N CG ND1 CD2 CE1 NE2
REMARK 480 LYS C 60 CE NZ
REMARK 480 ARG C 62 CG CD NE NH2
REMARK 480 ALA C 74 N O CB
REMARK 480 ASN C 76 CA C O CB CG OD1 ND2
REMARK 480 GLU C 77 N CA CB CG OE2
REMARK 480 GLU C 80 CG CD OE1 OE2
REMARK 480 PHE C 82 CD1 CD2 CE1 CE2 CZ
REMARK 480 ASN C 115 C CB
REMARK 480 SER C 116 CB OG
REMARK 480 TYR C 117 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR C 117 OH
REMARK 480 ARG C 135 CG CD CZ NH1 NH2
REMARK 480 ARG C 222 CG CD CZ NH1 NH2
REMARK 480 ARG C 235 CD NH1
REMARK 480 ARG D 23 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS D 24 CB CG CD CE NZ
REMARK 480 ASN D 25 CG OD1 ND2
REMARK 480 GLU D 70 CB CG OE1 OE2
REMARK 480 VAL D 75 CB CG1 CG2
REMARK 480 ASN D 76 N CA O CB CG OD1 ND2
REMARK 480 GLU D 77 N CA C O CB CG CD
REMARK 480 GLU D 77 OE1
REMARK 480 THR D 79 CB OG1 CG2
REMARK 480 ARG D 97 CG CD NH1 NH2
REMARK 480 SER D 116 OG
REMARK 480 TYR D 117 CB CG CD2 CE2 CZ OH
REMARK 480 ARG D 135 CD NE CZ NH1 NH2
REMARK 480 GLN D 192 CG CD OE1 NE2
REMARK 480 TYR D 217 CD1 CD2 CE2 OH
REMARK 480 ARG D 222 CG CD NE CZ NH1 NH2
REMARK 480 ARG D 235 CG CD CZ NH1 NH2
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 HIS B 40 NE2 HIS B 40 CD2 -0.067
REMARK 500 HIS B 57 NE2 HIS B 57 CD2 -0.075
REMARK 500 HIS B 71 NE2 HIS B 71 CD2 -0.067
REMARK 500 HIS B 91 NE2 HIS B 91 CD2 -0.079
REMARK 500 HIS C 40 NE2 HIS C 40 CD2 -0.069
REMARK 500 HIS C 57 NE2 HIS C 57 CD2 -0.069
REMARK 500 HIS C 91 NE2 HIS C 91 CD2 -0.073
REMARK 500 HIS D 40 NE2 HIS D 40 CD2 -0.066
REMARK 500 HIS D 71 NE2 HIS D 71 CD2 -0.069
REMARK 500 HIS D 91 NE2 HIS D 91 CD2 -0.067
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 TRP A 51 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 51 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP A 51 CG - CD2 - CE3 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 66 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 TRP A 141 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 141 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 215 CD1 - CG - CD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP A 215 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES
REMARK 500 TRP A 237 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 237 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP B 51 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP B 51 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG B 66 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 VAL B 138 CB - CA - C ANGL. DEV. = -13.6 DEGREES
REMARK 500 TRP B 141 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP B 141 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP B 215 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP B 215 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP B 237 CD1 - CG - CD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 TRP B 237 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TRP C 51 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP C 51 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 HIS C 57 CA - CB - CG ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG C 97 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 TRP C 141 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP C 141 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP C 215 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP C 215 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP C 237 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TRP C 237 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 TRP D 51 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP D 51 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 VAL D 138 CB - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 TRP D 141 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP D 141 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP D 215 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP D 215 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 TYR D 217 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TRP D 237 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP D 237 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
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 115 -161.37 -162.54
REMARK 500 ASN B 76 47.18 -83.84
REMARK 500 THR B 79 -7.29 -57.63
REMARK 500 ASN B 115 -161.52 -174.20
REMARK 500 ASN C 115 -154.52 -160.10
REMARK 500 SER C 214 -64.06 -120.91
REMARK 500 SER D 37 77.22 -153.66
REMARK 500 GLU D 77 55.84 -158.03
REMARK 500 SER D 214 -61.45 -122.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 39 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 247 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 75 O
REMARK 620 2 GLU A 77 OE1 117.4
REMARK 620 3 GLU A 80 OE2 88.2 84.4
REMARK 620 4 GLU A 70 OE2 138.8 103.7 100.4
REMARK 620 5 ASN A 72 O 87.3 71.4 149.8 102.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 247
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN B 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN C 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN D 246
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AMINO ACID NUMBERING SCHEME USED IS ADOPTED FROM
REMARK 999 CHYMOTRYPSINOGEN.
DBREF 1A0J A 16 245 UNP P35033 TRY3_SALSA 16 238
DBREF 1A0J B 16 245 UNP P35033 TRY3_SALSA 16 238
DBREF 1A0J C 16 245 UNP P35033 TRY3_SALSA 16 238
DBREF 1A0J D 16 245 UNP P35033 TRY3_SALSA 16 238
SEQRES 1 A 223 ILE VAL GLY GLY TYR GLU CYS ARG LYS ASN SER ALA SER
SEQRES 2 A 223 TYR GLN ALA SER LEU GLN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE SER SER THR TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 HIS ASN ILE ALA VAL ASN GLU GLY THR GLU GLN PHE ILE
SEQRES 6 A 223 ASP SER VAL LYS VAL ILE MET HIS PRO SER TYR ASN SER
SEQRES 7 A 223 ARG ASN LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 A 223 LYS PRO ALA SER LEU ASN SER TYR VAL SER THR VAL ALA
SEQRES 9 A 223 LEU PRO SER SER CYS ALA SER SER GLY THR ARG CYS LEU
SEQRES 10 A 223 VAL SER GLY TRP GLY ASN LEU SER GLY SER SER SER ASN
SEQRES 11 A 223 TYR PRO ASP THR LEU ARG CYS LEU ASP LEU PRO ILE LEU
SEQRES 12 A 223 SER SER SER SER CYS ASN SER ALA TYR PRO GLY GLN ILE
SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY PHE MET GLU GLY GLY
SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY TYR
SEQRES 16 A 223 GLY CYS ALA GLN ARG ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR ARG SER TRP ILE SER SER THR MET SER
SEQRES 18 A 223 SER ASN
SEQRES 1 B 223 ILE VAL GLY GLY TYR GLU CYS ARG LYS ASN SER ALA SER
SEQRES 2 B 223 TYR GLN ALA SER LEU GLN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 B 223 GLY SER LEU ILE SER SER THR TRP VAL VAL SER ALA ALA
SEQRES 4 B 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 B 223 HIS ASN ILE ALA VAL ASN GLU GLY THR GLU GLN PHE ILE
SEQRES 6 B 223 ASP SER VAL LYS VAL ILE MET HIS PRO SER TYR ASN SER
SEQRES 7 B 223 ARG ASN LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 B 223 LYS PRO ALA SER LEU ASN SER TYR VAL SER THR VAL ALA
SEQRES 9 B 223 LEU PRO SER SER CYS ALA SER SER GLY THR ARG CYS LEU
SEQRES 10 B 223 VAL SER GLY TRP GLY ASN LEU SER GLY SER SER SER ASN
SEQRES 11 B 223 TYR PRO ASP THR LEU ARG CYS LEU ASP LEU PRO ILE LEU
SEQRES 12 B 223 SER SER SER SER CYS ASN SER ALA TYR PRO GLY GLN ILE
SEQRES 13 B 223 THR SER ASN MET PHE CYS ALA GLY PHE MET GLU GLY GLY
SEQRES 14 B 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 B 223 CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY TYR
SEQRES 16 B 223 GLY CYS ALA GLN ARG ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 B 223 VAL CYS ASN TYR ARG SER TRP ILE SER SER THR MET SER
SEQRES 18 B 223 SER ASN
SEQRES 1 C 223 ILE VAL GLY GLY TYR GLU CYS ARG LYS ASN SER ALA SER
SEQRES 2 C 223 TYR GLN ALA SER LEU GLN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 C 223 GLY SER LEU ILE SER SER THR TRP VAL VAL SER ALA ALA
SEQRES 4 C 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 C 223 HIS ASN ILE ALA VAL ASN GLU GLY THR GLU GLN PHE ILE
SEQRES 6 C 223 ASP SER VAL LYS VAL ILE MET HIS PRO SER TYR ASN SER
SEQRES 7 C 223 ARG ASN LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 C 223 LYS PRO ALA SER LEU ASN SER TYR VAL SER THR VAL ALA
SEQRES 9 C 223 LEU PRO SER SER CYS ALA SER SER GLY THR ARG CYS LEU
SEQRES 10 C 223 VAL SER GLY TRP GLY ASN LEU SER GLY SER SER SER ASN
SEQRES 11 C 223 TYR PRO ASP THR LEU ARG CYS LEU ASP LEU PRO ILE LEU
SEQRES 12 C 223 SER SER SER SER CYS ASN SER ALA TYR PRO GLY GLN ILE
SEQRES 13 C 223 THR SER ASN MET PHE CYS ALA GLY PHE MET GLU GLY GLY
SEQRES 14 C 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 C 223 CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY TYR
SEQRES 16 C 223 GLY CYS ALA GLN ARG ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 C 223 VAL CYS ASN TYR ARG SER TRP ILE SER SER THR MET SER
SEQRES 18 C 223 SER ASN
SEQRES 1 D 223 ILE VAL GLY GLY TYR GLU CYS ARG LYS ASN SER ALA SER
SEQRES 2 D 223 TYR GLN ALA SER LEU GLN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 D 223 GLY SER LEU ILE SER SER THR TRP VAL VAL SER ALA ALA
SEQRES 4 D 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 D 223 HIS ASN ILE ALA VAL ASN GLU GLY THR GLU GLN PHE ILE
SEQRES 6 D 223 ASP SER VAL LYS VAL ILE MET HIS PRO SER TYR ASN SER
SEQRES 7 D 223 ARG ASN LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 D 223 LYS PRO ALA SER LEU ASN SER TYR VAL SER THR VAL ALA
SEQRES 9 D 223 LEU PRO SER SER CYS ALA SER SER GLY THR ARG CYS LEU
SEQRES 10 D 223 VAL SER GLY TRP GLY ASN LEU SER GLY SER SER SER ASN
SEQRES 11 D 223 TYR PRO ASP THR LEU ARG CYS LEU ASP LEU PRO ILE LEU
SEQRES 12 D 223 SER SER SER SER CYS ASN SER ALA TYR PRO GLY GLN ILE
SEQRES 13 D 223 THR SER ASN MET PHE CYS ALA GLY PHE MET GLU GLY GLY
SEQRES 14 D 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 D 223 CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY TYR
SEQRES 16 D 223 GLY CYS ALA GLN ARG ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 D 223 VAL CYS ASN TYR ARG SER TRP ILE SER SER THR MET SER
SEQRES 18 D 223 SER ASN
HET CA A 247 1
HET SO4 A 248 5
HET SO4 A 249 5
HET SO4 B 248 5
HET SO4 B 249 5
HET SO4 C 248 5
HET SO4 C 249 5
HET SO4 D 248 5
HET SO4 D 249 5
HET SO4 D 250 5
HET SO4 D 251 5
HET BEN A 246 9
HET BEN B 246 9
HET BEN C 246 9
HET BEN D 246 9
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM BEN BENZAMIDINE
FORMUL 5 CA CA 2+
FORMUL 6 SO4 10(O4 S 2-)
FORMUL 16 BEN 4(C7 H8 N2)
FORMUL 20 HOH *379(H2 O)
HELIX 1 1 ALA A 56 CYS A 58 5 3
HELIX 2 2 SER A 165 ALA A 171 1 7
HELIX 3 3 VAL A 231 SER A 243 5 13
HELIX 4 4 ALA B 56 CYS B 58 5 3
HELIX 5 5 SER B 165 ALA B 171 1 7
HELIX 6 6 VAL B 231 SER B 243 5 13
HELIX 7 7 ALA C 56 CYS C 58 5 3
HELIX 8 8 SER C 165 ALA C 171 1 7
HELIX 9 9 VAL C 231 SER C 243 5 13
HELIX 10 10 ALA D 56 CYS D 58 5 3
HELIX 11 11 SER D 165 ALA D 171 1 7
HELIX 12 12 VAL D 231 SER D 243 5 13
SHEET 1 A 4 HIS A 40 SER A 45 0
SHEET 2 A 4 GLN A 30 SER A 37 -1 N SER A 37 O HIS A 40
SHEET 3 A 4 GLN A 64 LEU A 67 -1 N ARG A 66 O SER A 32
SHEET 4 A 4 GLN A 81 ASP A 84 -1 N ILE A 83 O VAL A 65
SHEET 1 B 3 TRP A 51 SER A 54 0
SHEET 2 B 3 MET A 104 LEU A 108 -1 N ILE A 106 O VAL A 52
SHEET 3 B 3 SER A 85 MET A 90 -1 N ILE A 89 O LEU A 105
SHEET 1 C 2 ARG A 135 GLY A 140 0
SHEET 2 C 2 ARG A 156 PRO A 161 -1 N LEU A 160 O CYS A 136
SHEET 1 D 4 MET A 180 ALA A 183 0
SHEET 2 D 4 GLY A 226 LYS A 230 -1 N TYR A 228 O PHE A 181
SHEET 3 D 4 GLN A 204 TRP A 215 -1 N TRP A 215 O VAL A 227
SHEET 4 D 4 PRO A 198 CYS A 201 -1 N CYS A 201 O GLN A 204
SHEET 1 E 7 GLN B 81 ASP B 84 0
SHEET 2 E 7 GLN B 64 LEU B 67 -1 N LEU B 67 O GLN B 81
SHEET 3 E 7 GLN B 30 SER B 37 -1 N GLN B 34 O GLN B 64
SHEET 4 E 7 TYR B 39 SER B 48 -1 N GLY B 44 O ALA B 31
SHEET 5 E 7 TRP B 51 SER B 54 -1 N VAL B 53 O SER B 45
SHEET 6 E 7 MET B 104 LEU B 108 -1 N ILE B 106 O VAL B 52
SHEET 7 E 7 SER B 85 MET B 90 -1 N ILE B 89 O LEU B 105
SHEET 1 F 2 ARG B 135 GLY B 140 0
SHEET 2 F 2 ARG B 156 PRO B 161 -1 N LEU B 160 O CYS B 136
SHEET 1 G 4 MET B 180 ALA B 183 0
SHEET 2 G 4 GLY B 226 LYS B 230 -1 N TYR B 228 O PHE B 181
SHEET 3 G 4 GLN B 204 TRP B 215 -1 N TRP B 215 O VAL B 227
SHEET 4 G 4 PRO B 198 CYS B 201 -1 N CYS B 201 O GLN B 204
SHEET 1 H 4 HIS C 40 SER C 45 0
SHEET 2 H 4 GLN C 30 SER C 37 -1 N SER C 37 O HIS C 40
SHEET 3 H 4 ILE C 63 LEU C 67 -1 N ARG C 66 O SER C 32
SHEET 4 H 4 GLN C 81 ASP C 84 -1 N ILE C 83 O VAL C 65
SHEET 1 I 3 TRP C 51 SER C 54 0
SHEET 2 I 3 MET C 104 LEU C 108 -1 N ILE C 106 O VAL C 52
SHEET 3 I 3 SER C 85 MET C 90 -1 N ILE C 89 O LEU C 105
SHEET 1 J 2 ARG C 135 GLY C 140 0
SHEET 2 J 2 ARG C 156 PRO C 161 -1 N LEU C 160 O CYS C 136
SHEET 1 K 4 MET C 180 ALA C 183 0
SHEET 2 K 4 GLY C 226 LYS C 230 -1 N TYR C 228 O PHE C 181
SHEET 3 K 4 GLN C 204 TRP C 215 -1 N TRP C 215 O VAL C 227
SHEET 4 K 4 PRO C 198 CYS C 201 -1 N CYS C 201 O GLN C 204
SHEET 1 L 7 GLN D 81 ASP D 84 0
SHEET 2 L 7 GLN D 64 LEU D 67 -1 N LEU D 67 O GLN D 81
SHEET 3 L 7 GLN D 30 SER D 37 -1 N GLN D 34 O GLN D 64
SHEET 4 L 7 TYR D 39 SER D 48 -1 N GLY D 44 O ALA D 31
SHEET 5 L 7 TRP D 51 SER D 54 -1 N VAL D 53 O SER D 45
SHEET 6 L 7 MET D 104 LEU D 108 -1 N ILE D 106 O VAL D 52
SHEET 7 L 7 SER D 85 MET D 90 -1 N ILE D 89 O LEU D 105
SHEET 1 M 2 ARG D 135 GLY D 140 0
SHEET 2 M 2 ARG D 156 PRO D 161 -1 N LEU D 160 O CYS D 136
SHEET 1 N 4 MET D 180 ALA D 183 0
SHEET 2 N 4 GLY D 226 LYS D 230 -1 N TYR D 228 O PHE D 181
SHEET 3 N 4 GLN D 204 TRP D 215 -1 N TRP D 215 O VAL D 227
SHEET 4 N 4 PRO D 198 CYS D 201 -1 N CYS D 201 O GLN D 204
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.02
SSBOND 2 CYS A 42 CYS A 58 1555 1555 1.99
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.03
SSBOND 4 CYS A 136 CYS A 201 1555 1555 1.99
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.01
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.05
SSBOND 7 CYS B 22 CYS B 157 1555 1555 1.98
SSBOND 8 CYS B 42 CYS B 58 1555 1555 2.00
SSBOND 9 CYS B 128 CYS B 232 1555 1555 2.01
SSBOND 10 CYS B 136 CYS B 201 1555 1555 2.03
SSBOND 11 CYS B 168 CYS B 182 1555 1555 2.03
SSBOND 12 CYS B 191 CYS B 220 1555 1555 2.01
SSBOND 13 CYS C 22 CYS C 157 1555 1555 2.00
SSBOND 14 CYS C 42 CYS C 58 1555 1555 2.01
SSBOND 15 CYS C 128 CYS C 232 1555 1555 2.02
SSBOND 16 CYS C 136 CYS C 201 1555 1555 2.00
SSBOND 17 CYS C 168 CYS C 182 1555 1555 2.02
SSBOND 18 CYS C 191 CYS C 220 1555 1555 2.03
SSBOND 19 CYS D 22 CYS D 157 1555 1555 2.01
SSBOND 20 CYS D 42 CYS D 58 1555 1555 1.99
SSBOND 21 CYS D 128 CYS D 232 1555 1555 2.02
SSBOND 22 CYS D 136 CYS D 201 1555 1555 2.02
SSBOND 23 CYS D 168 CYS D 182 1555 1555 2.02
SSBOND 24 CYS D 191 CYS D 220 1555 1555 2.00
LINK CA CA A 247 O VAL A 75 1555 1555 2.39
LINK CA CA A 247 OE1 GLU A 77 1555 1555 2.91
LINK CA CA A 247 OE2 GLU A 80 1555 1555 2.86
LINK CA CA A 247 OE2 GLU A 70 1555 1555 2.94
LINK CA CA A 247 O ASN A 72 1555 1555 2.44
SITE 1 AC1 5 GLU A 70 ASN A 72 VAL A 75 GLU A 77
SITE 2 AC1 5 GLU A 80
SITE 1 AC2 5 HIS A 40 HIS A 57 GLN A 192 GLY A 193
SITE 2 AC2 5 SER A 195
SITE 1 AC3 4 PRO A 152 ASP A 153 THR A 154 ARG A 156
SITE 1 AC4 6 HIS B 57 GLN B 192 GLY B 193 SER B 195
SITE 2 AC4 6 BEN B 246 HOH B 323
SITE 1 AC5 4 PRO B 152 ASP B 153 THR B 154 ARG B 156
SITE 1 AC6 6 HIS C 57 GLN C 192 GLY C 193 SER C 195
SITE 2 AC6 6 BEN C 246 HOH C 614
SITE 1 AC7 5 GLU C 21 PRO C 152 ASP C 153 THR C 154
SITE 2 AC7 5 ARG C 156
SITE 1 AC8 6 TYR A 39 HIS D 57 GLN D 192 GLY D 193
SITE 2 AC8 6 SER D 195 BEN D 246
SITE 1 AC9 6 ASN A 76 ARG B 235 PRO D 152 ASP D 153
SITE 2 AC9 6 THR D 154 ARG D 156
SITE 1 BC1 6 SER A 148 SER A 149 ASN C 95 ARG C 97
SITE 2 BC1 6 ARG D 62 HOH D 490
SITE 1 BC2 5 SER C 96 LYS D 60 SER D 61 HOH D 474
SITE 2 BC2 5 HOH D 503
SITE 1 BC3 6 ASP A 189 SER A 190 SER A 195 GLY A 219
SITE 2 BC3 6 CYS A 220 GLY A 226
SITE 1 BC4 6 ASP B 189 SER B 190 SER B 195 GLY B 219
SITE 2 BC4 6 GLY B 226 SO4 B 248
SITE 1 BC5 8 ASP C 189 SER C 190 CYS C 191 SER C 195
SITE 2 BC5 8 GLY C 219 GLY C 226 SO4 C 248 HOH C 312
SITE 1 BC6 7 ASP D 189 SER D 190 CYS D 191 SER D 195
SITE 2 BC6 7 GLY D 219 GLY D 226 SO4 D 248
CRYST1 65.907 83.107 154.787 90.00 90.00 90.00 P 21 21 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 0.015173 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012033 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006460 0.00000
MTRIX1 1 -0.573450 -0.321655 0.753454 25.56022 1
MTRIX2 1 -0.367037 -0.721359 -0.587303 120.97440 1
MTRIX3 1 0.732420 -0.613334 0.295604 41.05470 1
MTRIX1 2 -0.054285 -0.335982 -0.940303 107.68916 1
MTRIX2 2 -0.413757 -0.849473 0.327415 66.42438 1
MTRIX3 2 -0.908767 0.406831 -0.092901 85.58722 1
MTRIX1 3 -0.504313 0.863056 0.028337 -16.28458 1
MTRIX2 3 -0.835345 -0.479281 -0.269237 72.87833 1
MTRIX3 3 -0.218785 -0.159451 0.962657 48.48168 1
MTRIX1 4 -0.569275 0.814531 -0.111647 28.27138 1
MTRIX2 4 0.757198 0.572348 0.314752 -35.09442 1
MTRIX3 4 0.320276 0.094642 -0.942585 104.65495 1
MTRIX1 5 0.032942 -0.454114 -0.890334 74.37251 1
MTRIX2 5 0.430334 0.810460 -0.397452 -19.85422 1
MTRIX3 5 0.902069 -0.370048 0.222119 61.08286 1
MTRIX1 6 -0.289240 -0.515202 0.806788 -19.95494 1
MTRIX2 6 0.459541 0.664614 0.589161 -71.18546 1
MTRIX3 6 -0.839739 0.541161 0.044524 99.16763 1
ATOM 1 N ILE A 16 15.986 30.174 66.763 1.00 7.85 N
ATOM 2 CA ILE A 16 14.618 30.648 67.023 1.00 9.03 C
ATOM 3 C ILE A 16 14.283 30.040 68.385 1.00 10.98 C
ATOM 4 O ILE A 16 14.415 28.817 68.532 1.00 9.80 O
ATOM 5 CB ILE A 16 13.631 30.089 65.962 1.00 8.40 C
ATOM 6 CG1 ILE A 16 13.942 30.621 64.558 1.00 9.09 C
ATOM 7 CG2 ILE A 16 12.206 30.418 66.391 1.00 10.01 C
ATOM 8 CD1 ILE A 16 13.676 32.115 64.283 1.00 9.18 C
ATOM 9 N VAL A 17 13.874 30.827 69.363 1.00 11.94 N
ATOM 10 CA VAL A 17 13.505 30.358 70.700 1.00 11.39 C
ATOM 11 C VAL A 17 11.970 30.281 70.772 1.00 12.97 C
ATOM 12 O VAL A 17 11.315 31.266 70.402 1.00 14.43 O
ATOM 13 CB VAL A 17 14.028 31.353 71.746 1.00 11.59 C
ATOM 14 CG1 VAL A 17 13.564 30.905 73.140 1.00 13.71 C
ATOM 15 CG2 VAL A 17 15.533 31.419 71.686 1.00 10.63 C
ATOM 16 N GLY A 18 11.372 29.164 71.199 1.00 10.96 N
ATOM 17 CA GLY A 18 9.928 29.091 71.383 1.00 11.29 C
ATOM 18 C GLY A 18 9.111 28.957 70.096 1.00 15.03 C
ATOM 19 O GLY A 18 7.894 29.211 70.082 1.00 16.38 O
ATOM 20 N GLY A 19 9.732 28.534 68.986 1.00 13.97 N
ATOM 21 CA GLY A 19 9.079 28.443 67.686 1.00 14.70 C
ATOM 22 C GLY A 19 8.667 27.012 67.414 1.00 15.29 C
ATOM 23 O GLY A 19 8.570 26.220 68.348 1.00 18.32 O
ATOM 24 N TYR A 20 8.508 26.602 66.181 1.00 13.27 N
ATOM 25 CA TYR A 20 8.042 25.273 65.853 1.00 14.78 C
ATOM 26 C TYR A 20 8.775 24.874 64.593 1.00 17.00 C
ATOM 27 O TYR A 20 9.330 25.740 63.918 1.00 17.33 O
ATOM 28 CB TYR A 20 6.513 25.262 65.581 1.00 15.48 C
ATOM 29 CG TYR A 20 6.005 26.272 64.553 1.00 15.70 C
ATOM 30 CD1 TYR A 20 5.703 27.590 64.936 1.00 17.44 C
ATOM 31 CD2 TYR A 20 5.842 25.893 63.222 1.00 16.80 C
ATOM 32 CE1 TYR A 20 5.248 28.504 63.991 1.00 18.16 C
ATOM 33 CE2 TYR A 20 5.383 26.811 62.278 1.00 17.72 C
ATOM 34 CZ TYR A 20 5.088 28.109 62.667 1.00 18.43 C
ATOM 35 OH TYR A 20 4.617 28.991 61.707 1.00 23.69 O
ATOM 36 N GLU A 21 8.779 23.607 64.235 1.00 17.82 N
ATOM 37 CA GLU A 21 9.407 23.182 63.015 1.00 20.30 C
ATOM 38 C GLU A 21 8.521 23.562 61.842 1.00 18.81 C
ATOM 39 O GLU A 21 7.330 23.270 61.784 1.00 17.67 O
ATOM 40 CB GLU A 21 9.610 21.702 63.087 1.00 22.32 C
ATOM 41 CG GLU A 21 10.655 21.237 62.096 1.00 31.10 C
ATOM 42 CD GLU A 21 10.702 19.723 61.935 1.00 36.79 C
ATOM 43 OE1 GLU A 21 10.608 18.998 62.930 1.00 43.13 O
ATOM 44 OE2 GLU A 21 10.837 19.261 60.806 1.00 38.52 O
ATOM 45 N CYS A 22 9.118 24.301 60.922 1.00 18.49 N
ATOM 46 CA CYS A 22 8.440 24.787 59.733 1.00 20.87 C
ATOM 47 C CYS A 22 7.912 23.616 58.946 1.00 23.57 C
ATOM 48 O CYS A 22 8.526 22.536 58.902 1.00 22.59 O
ATOM 49 CB CYS A 22 9.349 25.535 58.755 1.00 18.13 C
ATOM 50 SG CYS A 22 10.213 26.965 59.453 1.00 15.30 S
ATOM 51 N ARG A 23 6.776 23.864 58.302 1.00 28.75 N
ATOM 52 CA ARG A 23 6.180 22.868 57.419 1.00 35.90 C
ATOM 53 C ARG A 23 7.124 22.693 56.245 1.00 39.02 C
ATOM 54 O ARG A 23 8.010 23.517 55.992 1.00 39.58 O
ATOM 55 CB ARG A 23 4.800 23.310 56.895 1.00 36.81 C
ATOM 56 CG ARG A 23 3.737 23.420 57.982 0.00 40.48 C
ATOM 57 CD ARG A 23 3.453 22.058 58.599 0.00 42.99 C
ATOM 58 NE ARG A 23 2.475 22.152 59.669 0.00 44.56 N
ATOM 59 CZ ARG A 23 2.050 21.079 60.343 0.00 45.08 C
ATOM 60 NH1 ARG A 23 2.496 19.850 60.078 0.00 44.50 N
ATOM 61 NH2 ARG A 23 1.152 21.242 61.310 0.00 46.13 N
ATOM 62 N LYS A 24 6.923 21.588 55.535 1.00 43.70 N
ATOM 63 CA LYS A 24 7.770 21.160 54.434 0.00 46.98 C
ATOM 64 C LYS A 24 7.950 22.195 53.328 1.00 48.31 C
ATOM 65 O LYS A 24 9.064 22.447 52.840 1.00 49.40 O
ATOM 66 CB LYS A 24 7.143 19.867 53.915 0.00 49.39 C
ATOM 67 CG LYS A 24 7.799 19.105 52.778 0.00 53.04 C
ATOM 68 CD LYS A 24 6.885 17.920 52.505 0.00 55.99 C
ATOM 69 CE LYS A 24 7.398 17.050 51.375 0.00 58.12 C
ATOM 70 NZ LYS A 24 6.487 15.947 51.135 0.00 58.95 N
ATOM 71 N ASN A 25 6.777 22.747 52.984 1.00 48.10 N
ATOM 72 CA ASN A 25 6.622 23.701 51.896 1.00 47.42 C
ATOM 73 C ASN A 25 6.752 25.153 52.323 1.00 45.75 C
ATOM 74 O ASN A 25 6.895 26.014 51.442 1.00 48.56 O
ATOM 75 CB ASN A 25 5.255 23.563 51.221 0.00 48.89 C
ATOM 76 CG ASN A 25 4.864 22.140 50.871 0.00 50.03 C
ATOM 77 OD1 ASN A 25 4.747 21.298 51.760 0.00 51.91 O
ATOM 78 ND2 ASN A 25 4.621 21.795 49.619 0.00 49.75 N
ATOM 79 N SER A 26 6.682 25.527 53.610 1.00 40.11 N
ATOM 80 CA SER A 26 6.832 26.930 53.954 1.00 35.49 C
ATOM 81 C SER A 26 8.312 27.315 54.054 1.00 31.35 C
ATOM 82 O SER A 26 9.251 26.491 54.102 1.00 29.92 O
ATOM 83 CB SER A 26 6.108 27.218 55.271 1.00 34.67 C
ATOM 84 OG SER A 26 6.341 26.166 56.181 1.00 38.24 O
ATOM 85 N ALA A 27 8.502 28.631 54.013 1.00 25.47 N
ATOM 86 CA ALA A 27 9.803 29.235 54.109 1.00 20.91 C
ATOM 87 C ALA A 27 10.714 28.716 53.006 1.00 18.94 C
ATOM 88 O ALA A 27 11.925 28.641 53.215 1.00 18.26 O
ATOM 89 CB ALA A 27 10.427 28.926 55.473 1.00 15.35 C
ATOM 90 N SER A 28 10.216 28.418 51.798 1.00 14.78 N
ATOM 91 CA SER A 28 11.091 27.875 50.777 1.00 16.13 C
ATOM 92 C SER A 28 11.995 28.896 50.117 1.00 12.67 C
ATOM 93 O SER A 28 12.810 28.545 49.253 1.00 11.76 O
ATOM 94 CB SER A 28 10.271 27.126 49.703 1.00 17.95 C
ATOM 95 OG SER A 28 9.118 27.820 49.259 1.00 24.01 O
ATOM 96 N TYR A 29 11.828 30.155 50.555 1.00 11.09 N
ATOM 97 CA TYR A 29 12.722 31.250 50.183 1.00 10.86 C
ATOM 98 C TYR A 29 13.961 31.336 51.085 1.00 11.66 C
ATOM 99 O TYR A 29 14.834 32.187 50.895 1.00 11.89 O
ATOM 100 CB TYR A 29 11.974 32.580 50.248 1.00 10.52 C
ATOM 101 CG TYR A 29 11.134 32.745 51.513 1.00 11.63 C
ATOM 102 CD1 TYR A 29 11.744 32.949 52.755 1.00 11.85 C
ATOM 103 CD2 TYR A 29 9.746 32.618 51.441 1.00 11.94 C
ATOM 104 CE1 TYR A 29 10.989 33.005 53.914 1.00 11.59 C
ATOM 105 CE2 TYR A 29 8.986 32.677 52.601 1.00 10.50 C
ATOM 106 CZ TYR A 29 9.618 32.861 53.828 1.00 12.11 C
ATOM 107 OH TYR A 29 8.882 32.858 54.989 1.00 15.12 O
ATOM 108 N GLN A 30 14.034 30.502 52.113 1.00 9.65 N
ATOM 109 CA GLN A 30 15.114 30.538 53.090 1.00 10.16 C
ATOM 110 C GLN A 30 16.431 30.046 52.524 1.00 11.15 C
ATOM 111 O GLN A 30 16.473 28.981 51.906 1.00 12.52 O
ATOM 112 CB GLN A 30 14.745 29.677 54.294 1.00 11.84 C
ATOM 113 CG GLN A 30 15.802 29.555 55.393 1.00 10.37 C
ATOM 114 CD GLN A 30 15.862 30.704 56.388 1.00 14.19 C
ATOM 115 OE1 GLN A 30 14.853 31.202 56.892 1.00 17.43 O
ATOM 116 NE2 GLN A 30 17.024 31.260 56.668 1.00 12.98 N
ATOM 117 N ALA A 31 17.513 30.786 52.743 1.00 9.09 N
ATOM 118 CA ALA A 31 18.832 30.370 52.314 1.00 9.69 C
ATOM 119 C ALA A 31 19.707 30.277 53.571 1.00 11.28 C
ATOM 120 O ALA A 31 19.333 30.822 54.621 1.00 12.20 O
ATOM 121 CB ALA A 31 19.362 31.424 51.353 1.00 9.34 C
ATOM 122 N SER A 32 20.807 29.536 53.550 1.00 13.18 N
ATOM 123 CA SER A 32 21.845 29.534 54.588 1.00 16.47 C
ATOM 124 C SER A 32 23.065 30.015 53.830 1.00 14.75 C
ATOM 125 O SER A 32 23.265 29.701 52.652 1.00 12.04 O
ATOM 126 CB SER A 32 22.372 28.207 55.111 1.00 15.96 C
ATOM 127 OG SER A 32 21.385 27.558 55.831 1.00 23.41 O
ATOM 128 N LEU A 33 23.917 30.736 54.537 1.00 16.73 N
ATOM 129 CA LEU A 33 25.138 31.283 53.998 1.00 18.12 C
ATOM 130 C LEU A 33 26.223 30.674 54.874 1.00 22.03 C
ATOM 131 O LEU A 33 26.164 30.748 56.114 1.00 22.14 O
ATOM 132 CB LEU A 33 25.161 32.791 54.150 1.00 18.79 C
ATOM 133 CG LEU A 33 24.013 33.691 53.697 1.00 22.06 C
ATOM 134 CD1 LEU A 33 24.510 35.108 53.917 1.00 23.77 C
ATOM 135 CD2 LEU A 33 23.607 33.473 52.259 1.00 22.55 C
ATOM 136 N GLN A 34 27.175 29.993 54.274 1.00 25.54 N
ATOM 137 CA GLN A 34 28.267 29.425 55.027 1.00 32.70 C
ATOM 138 C GLN A 34 29.351 30.415 54.625 1.00 37.04 C
ATOM 139 O GLN A 34 29.961 30.340 53.546 1.00 36.38 O
ATOM 140 CB GLN A 34 28.436 28.043 54.497 1.00 36.01 C
ATOM 141 CG GLN A 34 29.490 27.192 55.173 1.00 45.25 C
ATOM 142 CD GLN A 34 29.150 25.704 55.034 1.00 51.14 C
ATOM 143 OE1 GLN A 34 28.635 25.240 54.011 1.00 53.49 O
ATOM 144 NE2 GLN A 34 29.384 24.872 56.047 1.00 53.56 N
ATOM 145 N SER A 37 29.382 31.462 55.457 1.00 40.62 N
ATOM 146 CA SER A 37 30.263 32.594 55.295 0.00 44.92 C
ATOM 147 C SER A 37 31.463 32.275 56.174 1.00 47.98 C
ATOM 148 O SER A 37 31.637 32.757 57.314 1.00 47.67 O
ATOM 149 CB SER A 37 29.519 33.845 55.758 0.00 45.21 C
ATOM 150 OG SER A 37 28.230 33.999 55.169 0.00 45.47 O
ATOM 151 N GLY A 38 32.299 31.380 55.636 1.00 50.25 N
ATOM 152 CA GLY A 38 33.432 30.863 56.398 1.00 50.74 C
ATOM 153 C GLY A 38 32.950 29.808 57.405 1.00 48.94 C
ATOM 154 O GLY A 38 32.546 28.703 57.010 1.00 50.86 O
ATOM 155 N TYR A 39 33.074 30.124 58.708 1.00 46.35 N
ATOM 156 CA TYR A 39 32.528 29.275 59.769 1.00 43.28 C
ATOM 157 C TYR A 39 31.388 30.011 60.420 1.00 40.14 C
ATOM 158 O TYR A 39 30.774 29.519 61.358 1.00 39.49 O
ATOM 159 CB TYR A 39 33.606 28.901 60.838 1.00 43.88 C
ATOM 160 CG TYR A 39 34.490 27.905 60.115 1.00 44.99 C
ATOM 161 CD1 TYR A 39 34.019 26.623 59.808 0.00 45.09 C
ATOM 162 CD2 TYR A 39 35.714 28.338 59.607 1.00 44.92 C
ATOM 163 CE1 TYR A 39 34.758 25.783 58.975 0.00 45.91 C
ATOM 164 CE2 TYR A 39 36.452 27.508 58.770 1.00 44.91 C
ATOM 165 CZ TYR A 39 35.965 26.243 58.458 1.00 45.19 C
ATOM 166 OH TYR A 39 36.708 25.476 57.590 1.00 46.53 O
ATOM 167 N HIS A 40 31.095 31.210 59.914 1.00 37.72 N
ATOM 168 CA HIS A 40 29.974 31.990 60.382 1.00 37.50 C
ATOM 169 C HIS A 40 28.883 31.382 59.511 1.00 32.93 C
ATOM 170 O HIS A 40 29.117 30.948 58.370 1.00 32.64 O
ATOM 171 CB HIS A 40 30.142 33.509 60.070 1.00 40.04 C
ATOM 172 CG HIS A 40 29.223 34.485 60.838 1.00 46.00 C
ATOM 173 ND1 HIS A 40 29.023 35.783 60.580 1.00 49.56 N
ATOM 174 CD2 HIS A 40 28.437 34.196 61.953 1.00 47.50 C
ATOM 175 CE1 HIS A 40 28.171 36.278 61.469 1.00 47.92 C
ATOM 176 NE2 HIS A 40 27.821 35.308 62.291 1.00 47.71 N
ATOM 177 N PHE A 41 27.729 31.237 60.128 1.00 29.53 N
ATOM 178 CA PHE A 41 26.562 30.789 59.410 1.00 24.81 C
ATOM 179 C PHE A 41 25.559 31.881 59.654 1.00 22.02 C
ATOM 180 O PHE A 41 25.476 32.398 60.777 1.00 23.17 O
ATOM 181 CB PHE A 41 26.029 29.469 59.964 1.00 25.60 C
ATOM 182 CG PHE A 41 26.963 28.324 59.615 1.00 33.05 C
ATOM 183 CD1 PHE A 41 26.921 27.791 58.332 0.00 32.18 C
ATOM 184 CD2 PHE A 41 27.883 27.822 60.568 1.00 36.51 C
ATOM 185 CE1 PHE A 41 27.794 26.768 57.996 0.00 32.97 C
ATOM 186 CE2 PHE A 41 28.758 26.791 60.207 1.00 35.11 C
ATOM 187 CZ PHE A 41 28.708 26.267 58.915 1.00 34.21 C
ATOM 188 N CYS A 42 24.887 32.297 58.597 1.00 15.73 N
ATOM 189 CA CYS A 42 23.806 33.246 58.729 1.00 13.37 C
ATOM 190 C CYS A 42 22.642 32.731 57.914 1.00 13.04 C
ATOM 191 O CYS A 42 22.800 31.785 57.124 1.00 13.06 O
ATOM 192 CB CYS A 42 24.273 34.581 58.213 1.00 11.58 C
ATOM 193 SG CYS A 42 25.279 35.342 59.499 1.00 12.56 S
ATOM 194 N GLY A 43 21.467 33.294 58.116 1.00 10.24 N
ATOM 195 CA GLY A 43 20.324 33.017 57.267 1.00 9.75 C
ATOM 196 C GLY A 43 20.350 34.021 56.132 1.00 8.92 C
ATOM 197 O GLY A 43 21.198 34.917 56.085 1.00 7.70 O
ATOM 198 N GLY A 44 19.453 33.905 55.179 1.00 8.49 N
ATOM 199 CA GLY A 44 19.318 34.872 54.110 1.00 9.74 C
ATOM 200 C GLY A 44 18.011 34.559 53.393 1.00 10.33 C
ATOM 201 O GLY A 44 17.321 33.590 53.776 1.00 8.96 O
ATOM 202 N SER A 45 17.587 35.336 52.414 1.00 8.98 N
ATOM 203 CA SER A 45 16.430 34.914 51.634 1.00 12.46 C
ATOM 204 C SER A 45 16.561 35.158 50.119 1.00 12.21 C
ATOM 205 O SER A 45 17.236 36.101 49.660 1.00 12.27 O
ATOM 206 CB SER A 45 15.184 35.592 52.188 1.00 14.36 C
ATOM 207 OG SER A 45 15.320 36.972 52.376 1.00 17.94 O
ATOM 208 N LEU A 46 15.951 34.269 49.321 1.00 11.64 N
ATOM 209 CA LEU A 46 16.086 34.336 47.883 1.00 11.22 C
ATOM 210 C LEU A 46 15.116 35.348 47.330 1.00 14.06 C
ATOM 211 O LEU A 46 13.907 35.219 47.570 1.00 13.85 O
ATOM 212 CB LEU A 46 15.825 32.954 47.309 1.00 11.61 C
ATOM 213 CG LEU A 46 16.271 32.682 45.882 1.00 11.35 C
ATOM 214 CD1 LEU A 46 17.786 32.796 45.718 1.00 7.92 C
ATOM 215 CD2 LEU A 46 15.834 31.267 45.545 1.00 12.36 C