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4HOH.pdb
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HEADER HYDROLASE 14-SEP-98 4HOH
TITLE RIBONUCLEASE T1 (THR93ALA MUTANT) COMPLEXED WITH 2'GMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (RIBONUCLEASE T1);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: RNASE T1;
COMPND 5 EC: 3.1.27.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: COMPLEXED WITH GUANOSINE-2'-MONOPHOSPHATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;
SOURCE 3 ORGANISM_TAXID: 5062;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: WK6
KEYWDS HYDROLASE, ENDORIBONUCLEASE, RIBONUCLEASE, ENDONUCLEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.LANGHORST,R.LORIS,V.P.DENISOV,J.DOUMEN,P.ROOSE,D.MAES,
AUTHOR 2 B.HALLE,J.STEYAERT
REVDAT 3 24-FEB-09 4HOH 1 VERSN
REVDAT 2 22-DEC-99 4HOH 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 23-SEP-98 4HOH 0
JRNL AUTH U.LANGHORST,R.LORIS,V.P.DENISOV,J.DOUMEN,P.ROOSE,
JRNL AUTH 2 D.MAES,B.HALLE,J.STEYAERT
JRNL TITL DISSECTION OF THE STRUCTURAL AND FUNCTIONAL ROLE
JRNL TITL 2 OF A CONSERVED HYDRATION SITE IN RNASE T1.
JRNL REF PROTEIN SCI. V. 8 722 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10211818
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 21739
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) : 0.190
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1457
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2280
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141
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 : 3100
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 122
REMARK 3 SOLVENT ATOMS : 219
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 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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.45
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.82
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.07
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4HOH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-99.
REMARK 100 THE RCSB ID CODE IS RCSB008067.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 4.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : DUAL SLITS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21739
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 2.950
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.29
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1RGA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.20
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 29.66000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.51500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.15500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.51500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.66000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.15500
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, 3, 4
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
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
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 102 CG CD OE1 OE2
REMARK 470 GLU B 102 CG CD OE1 OE2
REMARK 470 GLU C 102 CG CD OE1 OE2
REMARK 470 GLU D 102 CG CD OE1 OE2
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 SER C 64 O HOH C 1218 2.08
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 OG SER D 72 O HOH B 1026 3656 1.20
REMARK 500 NZ LYS D 41 O HOH A 1099 4566 1.52
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 CYS C 2 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 GLY C 70 N - CA - C ANGL. DEV. = -32.8 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 81 -168.42 -110.12
REMARK 500 ASN B 81 -169.82 -109.32
REMARK 500 ASN C 99 -155.75 -85.48
REMARK 500 CYS D 2 77.16 71.19
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 C 105 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 47 O
REMARK 620 2 ASP C 49 OD1 92.4
REMARK 620 3 TYR D 45 O 71.5 103.0
REMARK 620 4 HOH C1218 O 88.5 177.8 79.2
REMARK 620 5 HOH C1219 O 80.2 93.7 147.6 84.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 106 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY D 47 O
REMARK 620 2 ASP D 49 OD1 78.3
REMARK 620 3 TYR C 45 O 78.3 88.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CT1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.
REMARK 800 SITE_IDENTIFIER: CT2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.
REMARK 800 SITE_IDENTIFIER: CT3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.
REMARK 800 SITE_IDENTIFIER: CT4
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.
REMARK 800 SITE_IDENTIFIER: BI1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: BINDING SITE.
REMARK 800 SITE_IDENTIFIER: BI2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: BINDING SITE.
REMARK 800 SITE_IDENTIFIER: BI3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: BINDING SITE.
REMARK 800 SITE_IDENTIFIER: BI4
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: BINDING SITE.
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: SITE.
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: SITE.
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 105
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 106
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2GP A 107
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2GP B 108
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2GP C 109
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2GP C 110
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2GP D 111
DBREF 4HOH A 1 104 UNP P00651 RNT1_ASPOR 27 130
DBREF 4HOH B 1 104 UNP P00651 RNT1_ASPOR 27 130
DBREF 4HOH C 1 104 UNP P00651 RNT1_ASPOR 27 130
DBREF 4HOH D 1 104 UNP P00651 RNT1_ASPOR 27 130
SEQADV 4HOH LYS A 25 UNP P00651 GLN 51 CONFLICT
SEQADV 4HOH ALA A 93 UNP P00651 THR 119 ENGINEERED
SEQRES 1 A 104 ALA CYS ASP TYR THR CYS GLY SER ASN CYS TYR SER SER
SEQRES 2 A 104 SER ASP VAL SER THR ALA GLN ALA ALA GLY TYR LYS LEU
SEQRES 3 A 104 HIS GLU ASP GLY GLU THR VAL GLY SER ASN SER TYR PRO
SEQRES 4 A 104 HIS LYS TYR ASN ASN TYR GLU GLY PHE ASP PHE SER VAL
SEQRES 5 A 104 SER SER PRO TYR TYR GLU TRP PRO ILE LEU SER SER GLY
SEQRES 6 A 104 ASP VAL TYR SER GLY GLY SER PRO GLY ALA ASP ARG VAL
SEQRES 7 A 104 VAL PHE ASN GLU ASN ASN GLN LEU ALA GLY VAL ILE THR
SEQRES 8 A 104 HIS ALA GLY ALA SER GLY ASN ASN PHE VAL GLU CYS THR
SEQRES 1 B 104 ALA CYS ASP TYR THR CYS GLY SER ASN CYS TYR SER SER
SEQRES 2 B 104 SER ASP VAL SER THR ALA GLN ALA ALA GLY TYR LYS LEU
SEQRES 3 B 104 HIS GLU ASP GLY GLU THR VAL GLY SER ASN SER TYR PRO
SEQRES 4 B 104 HIS LYS TYR ASN ASN TYR GLU GLY PHE ASP PHE SER VAL
SEQRES 5 B 104 SER SER PRO TYR TYR GLU TRP PRO ILE LEU SER SER GLY
SEQRES 6 B 104 ASP VAL TYR SER GLY GLY SER PRO GLY ALA ASP ARG VAL
SEQRES 7 B 104 VAL PHE ASN GLU ASN ASN GLN LEU ALA GLY VAL ILE THR
SEQRES 8 B 104 HIS ALA GLY ALA SER GLY ASN ASN PHE VAL GLU CYS THR
SEQRES 1 C 104 ALA CYS ASP TYR THR CYS GLY SER ASN CYS TYR SER SER
SEQRES 2 C 104 SER ASP VAL SER THR ALA GLN ALA ALA GLY TYR LYS LEU
SEQRES 3 C 104 HIS GLU ASP GLY GLU THR VAL GLY SER ASN SER TYR PRO
SEQRES 4 C 104 HIS LYS TYR ASN ASN TYR GLU GLY PHE ASP PHE SER VAL
SEQRES 5 C 104 SER SER PRO TYR TYR GLU TRP PRO ILE LEU SER SER GLY
SEQRES 6 C 104 ASP VAL TYR SER GLY GLY SER PRO GLY ALA ASP ARG VAL
SEQRES 7 C 104 VAL PHE ASN GLU ASN ASN GLN LEU ALA GLY VAL ILE THR
SEQRES 8 C 104 HIS ALA GLY ALA SER GLY ASN ASN PHE VAL GLU CYS THR
SEQRES 1 D 104 ALA CYS ASP TYR THR CYS GLY SER ASN CYS TYR SER SER
SEQRES 2 D 104 SER ASP VAL SER THR ALA GLN ALA ALA GLY TYR LYS LEU
SEQRES 3 D 104 HIS GLU ASP GLY GLU THR VAL GLY SER ASN SER TYR PRO
SEQRES 4 D 104 HIS LYS TYR ASN ASN TYR GLU GLY PHE ASP PHE SER VAL
SEQRES 5 D 104 SER SER PRO TYR TYR GLU TRP PRO ILE LEU SER SER GLY
SEQRES 6 D 104 ASP VAL TYR SER GLY GLY SER PRO GLY ALA ASP ARG VAL
SEQRES 7 D 104 VAL PHE ASN GLU ASN ASN GLN LEU ALA GLY VAL ILE THR
SEQRES 8 D 104 HIS ALA GLY ALA SER GLY ASN ASN PHE VAL GLU CYS THR
HET CA C 105 1
HET CA D 106 1
HET 2GP A 107 24
HET 2GP B 108 24
HET 2GP C 109 24
HET 2GP C 110 24
HET 2GP D 111 24
HETNAM CA CALCIUM ION
HETNAM 2GP GUANOSINE-2'-MONOPHOSPHATE
FORMUL 5 CA 2(CA 2+)
FORMUL 7 2GP 5(C10 H14 N5 O8 P)
FORMUL 12 HOH *219(H2 O)
HELIX 1 HA SER A 13 ASP A 29 1SEE REMARK 650 17
HELIX 2 HB SER B 13 ASP B 29 1SEE REMARK 650 17
HELIX 3 HC SER C 13 ASP C 29 1SEE REMARK 650 17
HELIX 4 HD SER D 13 ASP D 29 1SEE REMARK 650 17
SHEET 1 S1A 1 ASN A 9 SER A 12 0
SHEET 1 S1B 1 ASN B 9 SER B 12 0
SHEET 1 S1C 1 ASN C 9 SER C 12 0
SHEET 1 S1D 1 ASN D 9 SER D 12 0
SHEET 1 S2A 1 PHE A 100 CYS A 103 0
SHEET 1 S2B 1 PHE B 100 CYS B 103 0
SHEET 1 S2C 1 PHE C 100 CYS C 103 0
SHEET 1 S2D 1 PHE D 100 CYS D 103 0
SSBOND 1 CYS A 2 CYS A 10 1555 1555 2.65
SSBOND 2 CYS B 2 CYS B 10 1555 1555 2.39
SSBOND 3 CYS C 2 CYS C 10 1555 1555 2.33
SSBOND 4 CYS D 2 CYS D 10 1555 1555 2.51
SSBOND 5 CYS A 6 CYS A 103 1555 1555 2.30
SSBOND 6 CYS B 6 CYS B 103 1555 1555 2.31
SSBOND 7 CYS C 6 CYS C 103 1555 1555 2.29
SSBOND 8 CYS D 6 CYS D 103 1555 1555 2.31
LINK O GLY C 47 CA CA C 105 1555 1555 2.30
LINK OD1 ASP C 49 CA CA C 105 1555 1555 2.39
LINK O GLY D 47 CA CA D 106 1555 1555 2.30
LINK OD1 ASP D 49 CA CA D 106 1555 1555 2.44
LINK CA CA C 105 O TYR D 45 1555 4466 2.30
LINK CA CA C 105 O HOH C1218 1555 3656 2.03
LINK CA CA C 105 O HOH C1219 1555 3656 2.34
LINK CA CA D 106 O TYR C 45 1555 4566 2.40
CISPEP 1 TYR A 38 PRO A 39 0 -0.24
CISPEP 2 SER A 54 PRO A 55 0 -1.53
CISPEP 3 TYR B 38 PRO B 39 0 0.08
CISPEP 4 SER B 54 PRO B 55 0 -0.55
CISPEP 5 TYR C 38 PRO C 39 0 -0.49
CISPEP 6 SER C 54 PRO C 55 0 -1.74
CISPEP 7 TYR D 38 PRO D 39 0 -0.69
CISPEP 8 SER D 54 PRO D 55 0 -0.32
SITE 1 CT1 5 TYR A 38 HIS A 40 GLU A 58 ARG A 77
SITE 2 CT1 5 HIS A 92
SITE 1 CT2 5 TYR B 38 HIS B 40 GLU B 58 ARG B 77
SITE 2 CT2 5 HIS B 92
SITE 1 CT3 5 TYR C 38 HIS C 40 GLU C 58 ARG C 77
SITE 2 CT3 5 HIS C 92
SITE 1 CT4 5 TYR D 38 HIS D 40 GLU D 58 ARG D 77
SITE 2 CT4 5 HIS D 92
SITE 1 BI1 5 TYR A 42 ASN A 43 ASN A 44 TYR A 45
SITE 2 BI1 5 GLU A 46
SITE 1 BI2 5 TYR B 42 ASN B 43 ASN B 44 TYR B 45
SITE 2 BI2 5 GLU B 46
SITE 1 BI3 5 TYR C 42 ASN C 43 ASN C 44 TYR C 45
SITE 2 BI3 5 GLU C 46
SITE 1 BI4 5 TYR D 42 ASN D 43 ASN D 44 TYR D 45
SITE 2 BI4 5 GLU D 46
SITE 1 CA1 1 ASP C 49
SITE 1 CA2 1 ASP D 49
SITE 1 AC1 5 GLY C 47 ASP C 49 HOH C1218 HOH C1219
SITE 2 AC1 5 TYR D 45
SITE 1 AC2 3 TYR C 45 GLY D 47 ASP D 49
SITE 1 AC3 14 TYR A 38 HIS A 40 LYS A 41 TYR A 42
SITE 2 AC3 14 ASN A 43 ASN A 44 TYR A 45 GLU A 46
SITE 3 AC3 14 GLU A 58 ASN A 98 PHE A 100 HOH A1059
SITE 4 AC3 14 HOH A1138 HOH D1072
SITE 1 AC4 11 ASN B 36 TYR B 38 TYR B 42 ASN B 43
SITE 2 AC4 11 ASN B 44 TYR B 45 GLU B 46 GLU B 58
SITE 3 AC4 11 ASN B 98 PHE B 100 HOH B1209
SITE 1 AC5 11 SER A 53 HOH A1020 HIS C 40 TYR C 42
SITE 2 AC5 11 ASN C 43 ASN C 44 TYR C 45 GLU C 46
SITE 3 AC5 11 PHE C 100 HOH C1004 HOH C1212
SITE 1 AC6 22 SER A 53 SER A 54 PRO A 55 ASN A 81
SITE 2 AC6 22 GLU A 82 ASN A 83 HOH A1020 HOH A1201
SITE 3 AC6 22 ASN C 36 TYR C 38 HIS C 40 GLU C 58
SITE 4 AC6 22 PRO C 73 GLY C 74 ARG C 77 HIS C 92
SITE 5 AC6 22 ASN C 98 PHE C 100 HOH C1004 HOH C1212
SITE 6 AC6 22 HOH C1215 HOH C1217
SITE 1 AC7 13 TYR D 38 HIS D 40 LYS D 41 TYR D 42
SITE 2 AC7 13 ASN D 43 ASN D 44 TYR D 45 GLU D 46
SITE 3 AC7 13 GLU D 58 ASN D 98 PHE D 100 HOH D1110
SITE 4 AC7 13 HOH D1191
CRYST1 59.320 60.310 101.030 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 0.016858 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016581 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009898 0.00000
MTRIX1 1 -0.110694 -0.811065 -0.574387 53.41301 1
MTRIX2 1 0.869585 -0.358873 0.339164 64.77747 1
MTRIX3 1 -0.481216 -0.461935 0.745015 -10.28357 1
MTRIX1 2 0.570249 0.809786 0.138068 55.26530 1
MTRIX2 2 -0.425493 0.434937 -0.793590 -57.90049 1
MTRIX3 2 -0.702689 0.393797 0.592581 57.12147 1
MTRIX1 3 -0.035199 0.853298 0.520234 83.33276 1
MTRIX2 3 -0.887029 0.213122 -0.409582 1.90023 1
MTRIX3 3 -0.460369 -0.475880 0.749399 35.92253 1
ATOM 1 N ALA A 1 18.620 1.958 49.321 1.00 61.68 N
ATOM 2 CA ALA A 1 18.401 2.568 50.668 1.00 62.42 C
ATOM 3 C ALA A 1 18.990 3.978 50.753 1.00 61.64 C
ATOM 4 O ALA A 1 18.267 4.967 50.578 1.00 60.30 O
ATOM 5 CB ALA A 1 18.998 1.679 51.761 1.00 59.46 C
ATOM 6 N CYS A 2 20.297 4.063 51.014 1.00 59.91 N
ATOM 7 CA CYS A 2 20.984 5.353 51.124 1.00 54.17 C
ATOM 8 C CYS A 2 21.311 5.977 49.776 1.00 47.97 C
ATOM 9 O CYS A 2 22.482 6.061 49.367 1.00 40.44 O
ATOM 10 CB CYS A 2 22.266 5.243 51.948 1.00 56.69 C
ATOM 11 SG CYS A 2 22.830 6.877 52.487 1.00 54.22 S
ATOM 12 N ASP A 3 20.268 6.426 49.093 1.00 38.72 N
ATOM 13 CA ASP A 3 20.444 7.050 47.791 1.00 35.75 C
ATOM 14 C ASP A 3 21.129 8.417 47.878 1.00 33.43 C
ATOM 15 O ASP A 3 21.932 8.772 47.008 1.00 29.79 O
ATOM 16 CB ASP A 3 19.101 7.172 47.079 1.00 35.38 C
ATOM 17 CG ASP A 3 18.484 5.825 46.777 1.00 37.46 C
ATOM 18 OD1 ASP A 3 19.149 4.995 46.125 1.00 41.87 O
ATOM 19 OD2 ASP A 3 17.335 5.593 47.193 1.00 38.90 O
ATOM 20 N TYR A 4 20.792 9.188 48.912 1.00 28.90 N
ATOM 21 CA TYR A 4 21.386 10.509 49.121 1.00 25.49 C
ATOM 22 C TYR A 4 21.885 10.623 50.551 1.00 22.25 C
ATOM 23 O TYR A 4 21.154 10.359 51.504 1.00 24.57 O
ATOM 24 CB TYR A 4 20.370 11.623 48.855 1.00 21.90 C
ATOM 25 CG TYR A 4 19.879 11.667 47.432 1.00 23.80 C
ATOM 26 CD1 TYR A 4 20.585 12.364 46.452 1.00 19.30 C
ATOM 27 CD2 TYR A 4 18.713 11.002 47.060 1.00 23.42 C
ATOM 28 CE1 TYR A 4 20.140 12.394 45.139 1.00 22.66 C
ATOM 29 CE2 TYR A 4 18.260 11.029 45.746 1.00 23.26 C
ATOM 30 CZ TYR A 4 18.977 11.725 44.795 1.00 21.14 C
ATOM 31 OH TYR A 4 18.531 11.746 43.498 1.00 26.27 O
ATOM 32 N THR A 5 23.141 11.015 50.691 1.00 21.51 N
ATOM 33 CA THR A 5 23.751 11.173 52.003 1.00 25.26 C
ATOM 34 C THR A 5 24.038 12.646 52.238 1.00 23.32 C
ATOM 35 O THR A 5 24.865 13.239 51.538 1.00 19.74 O
ATOM 36 CB THR A 5 25.074 10.383 52.115 1.00 22.99 C
ATOM 37 OG1 THR A 5 24.830 8.998 51.834 1.00 26.00 O
ATOM 38 CG2 THR A 5 25.646 10.522 53.503 1.00 22.61 C
ATOM 39 N CYS A 6 23.305 13.240 53.177 1.00 21.64 N
ATOM 40 CA CYS A 6 23.484 14.645 53.523 1.00 19.29 C
ATOM 41 C CYS A 6 24.115 14.652 54.898 1.00 19.15 C
ATOM 42 O CYS A 6 23.431 14.496 55.908 1.00 20.50 O
ATOM 43 CB CYS A 6 22.137 15.363 53.565 1.00 22.39 C
ATOM 44 SG CYS A 6 21.207 15.272 52.027 1.00 18.15 S
ATOM 45 N GLY A 7 25.430 14.823 54.935 1.00 24.85 N
ATOM 46 CA GLY A 7 26.127 14.797 56.207 1.00 26.31 C
ATOM 47 C GLY A 7 25.981 13.380 56.730 1.00 27.94 C
ATOM 48 O GLY A 7 26.436 12.426 56.089 1.00 32.66 O
ATOM 49 N SER A 8 25.287 13.228 57.851 1.00 30.89 N
ATOM 50 CA SER A 8 25.073 11.907 58.442 1.00 31.72 C
ATOM 51 C SER A 8 23.655 11.403 58.196 1.00 29.41 C
ATOM 52 O SER A 8 23.269 10.341 58.688 1.00 32.12 O
ATOM 53 CB SER A 8 25.364 11.942 59.943 1.00 32.74 C
ATOM 54 OG SER A 8 24.508 12.864 60.598 1.00 44.58 O
ATOM 55 N ASN A 9 22.872 12.181 57.456 1.00 28.69 N
ATOM 56 CA ASN A 9 21.497 11.803 57.143 1.00 26.34 C
ATOM 57 C ASN A 9 21.414 11.030 55.846 1.00 25.07 C
ATOM 58 O ASN A 9 21.963 11.436 54.818 1.00 27.87 O
ATOM 59 CB ASN A 9 20.594 13.031 57.067 1.00 25.40 C
ATOM 60 CG ASN A 9 20.421 13.704 58.404 1.00 27.51 C
ATOM 61 OD1 ASN A 9 20.459 13.052 59.451 1.00 28.34 O
ATOM 62 ND2 ASN A 9 20.228 15.016 58.384 1.00 28.89 N
ATOM 63 N CYS A 10 20.704 9.917 55.904 1.00 25.01 N
ATOM 64 CA CYS A 10 20.544 9.065 54.754 1.00 26.69 C
ATOM 65 C CYS A 10 19.118 9.151 54.208 1.00 26.31 C
ATOM 66 O CYS A 10 18.152 8.964 54.947 1.00 28.96 O
ATOM 67 CB CYS A 10 20.881 7.641 55.157 1.00 28.10 C
ATOM 68 SG CYS A 10 20.588 6.500 53.847 1.00 36.90 S
ATOM 69 N TYR A 11 18.990 9.436 52.913 1.00 21.94 N
ATOM 70 CA TYR A 11 17.676 9.553 52.273 1.00 21.80 C
ATOM 71 C TYR A 11 17.497 8.604 51.097 1.00 22.63 C
ATOM 72 O TYR A 11 18.417 8.409 50.304 1.00 25.33 O
ATOM 73 CB TYR A 11 17.448 10.978 51.762 1.00 19.59 C
ATOM 74 CG TYR A 11 17.427 12.027 52.845 1.00 17.93 C
ATOM 75 CD1 TYR A 11 16.385 12.076 53.770 1.00 19.74 C
ATOM 76 CD2 TYR A 11 18.452 12.961 52.954 1.00 17.75 C
ATOM 77 CE1 TYR A 11 16.367 13.027 54.781 1.00 16.97 C
ATOM 78 CE2 TYR A 11 18.443 13.921 53.961 1.00 18.19 C
ATOM 79 CZ TYR A 11 17.397 13.949 54.870 1.00 18.21 C
ATOM 80 OH TYR A 11 17.373 14.899 55.869 1.00 13.58 O
ATOM 81 N SER A 12 16.307 8.023 50.988 1.00 23.31 N
ATOM 82 CA SER A 12 15.995 7.125 49.881 1.00 21.65 C
ATOM 83 C SER A 12 15.332 7.972 48.793 1.00 26.72 C
ATOM 84 O SER A 12 14.972 9.134 49.036 1.00 22.31 O
ATOM 85 CB SER A 12 15.026 6.027 50.330 1.00 23.17 C
ATOM 86 OG SER A 12 13.734 6.549 50.617 1.00 24.22 O
ATOM 87 N SER A 13 15.186 7.407 47.595 1.00 25.30 N
ATOM 88 CA SER A 13 14.545 8.110 46.488 1.00 26.27 C
ATOM 89 C SER A 13 13.105 8.451 46.859 1.00 25.52 C
ATOM 90 O SER A 13 12.584 9.489 46.446 1.00 22.88 O
ATOM 91 CB SER A 13 14.557 7.251 45.225 1.00 30.56 C
ATOM 92 OG SER A 13 15.869 7.140 44.707 1.00 42.46 O
ATOM 93 N SER A 14 12.481 7.577 47.647 1.00 23.74 N
ATOM 94 CA SER A 14 11.104 7.777 48.101 1.00 28.29 C
ATOM 95 C SER A 14 10.999 8.993 49.016 1.00 26.18 C
ATOM 96 O SER A 14 10.043 9.767 48.914 1.00 27.07 O
ATOM 97 CB SER A 14 10.603 6.541 48.846 1.00 29.21 C
ATOM 98 OG SER A 14 10.554 5.428 47.976 1.00 43.71 O
ATOM 99 N ASP A 15 11.969 9.138 49.920 1.00 23.74 N
ATOM 100 CA ASP A 15 12.003 10.264 50.853 1.00 22.26 C
ATOM 101 C ASP A 15 12.075 11.569 50.066 1.00 18.95 C
ATOM 102 O ASP A 15 11.324 12.510 50.325 1.00 20.80 O
ATOM 103 CB ASP A 15 13.230 10.173 51.773 1.00 23.36 C
ATOM 104 CG ASP A 15 13.186 8.971 52.707 1.00 27.75 C
ATOM 105 OD1 ASP A 15 12.076 8.491 53.042 1.00 29.33 O
ATOM 106 OD2 ASP A 15 14.274 8.520 53.122 1.00 29.61 O
ATOM 107 N VAL A 16 12.992 11.618 49.108 1.00 15.59 N
ATOM 108 CA VAL A 16 13.183 12.800 48.275 1.00 16.52 C
ATOM 109 C VAL A 16 11.929 13.099 47.456 1.00 17.66 C
ATOM 110 O VAL A 16 11.467 14.243 47.397 1.00 18.71 O
ATOM 111 CB VAL A 16 14.411 12.612 47.350 1.00 13.38 C
ATOM 112 CG1 VAL A 16 14.510 13.735 46.323 1.00 14.92 C
ATOM 113 CG2 VAL A 16 15.677 12.545 48.191 1.00 9.97 C
ATOM 114 N SER A 17 11.348 12.047 46.888 1.00 21.69 N
ATOM 115 CA SER A 17 10.148 12.146 46.066 1.00 21.11 C
ATOM 116 C SER A 17 8.949 12.679 46.856 1.00 19.80 C
ATOM 117 O SER A 17 8.175 13.492 46.348 1.00 22.02 O
ATOM 118 CB SER A 17 9.830 10.773 45.464 1.00 22.51 C
ATOM 119 OG SER A 17 8.874 10.883 44.436 1.00 32.87 O
ATOM 120 N THR A 18 8.801 12.217 48.097 1.00 17.60 N
ATOM 121 CA THR A 18 7.709 12.657 48.965 1.00 18.01 C
ATOM 122 C THR A 18 7.875 14.127 49.354 1.00 15.18 C
ATOM 123 O THR A 18 6.908 14.880 49.347 1.00 16.59 O
ATOM 124 CB THR A 18 7.647 11.816 50.255 1.00 18.55 C
ATOM 125 OG1 THR A 18 7.498 10.434 49.916 1.00 24.22 O
ATOM 126 CG2 THR A 18 6.465 12.254 51.126 1.00 19.59 C
ATOM 127 N ALA A 19 9.100 14.524 49.691 1.00 13.98 N
ATOM 128 CA ALA A 19 9.396 15.907 50.073 1.00 16.49 C
ATOM 129 C ALA A 19 9.178 16.850 48.884 1.00 15.27 C
ATOM 130 O ALA A 19 8.540 17.892 49.020 1.00 16.31 O
ATOM 131 CB ALA A 19 10.835 16.019 50.574 1.00 14.42 C
ATOM 132 N GLN A 20 9.684 16.452 47.716 1.00 17.75 N
ATOM 133 CA GLN A 20 9.546 17.249 46.498 1.00 16.08 C
ATOM 134 C GLN A 20 8.085 17.490 46.125 1.00 16.64 C
ATOM 135 O GLN A 20 7.710 18.602 45.762 1.00 20.39 O
ATOM 136 CB GLN A 20 10.269 16.566 45.335 1.00 20.50 C
ATOM 137 CG GLN A 20 10.222 17.352 44.038 1.00 20.79 C
ATOM 138 CD GLN A 20 10.771 16.575 42.862 1.00 24.62 C
ATOM 139 OE1 GLN A 20 10.426 16.847 41.706 1.00 31.64 O
ATOM 140 NE2 GLN A 20 11.623 15.597 43.143 1.00 22.39 N
ATOM 141 N ALA A 21 7.264 16.448 46.212 1.00 19.85 N
ATOM 142 CA ALA A 21 5.841 16.556 45.883 1.00 19.86 C
ATOM 143 C ALA A 21 5.138 17.570 46.789 1.00 19.07 C
ATOM 144 O ALA A 21 4.288 18.337 46.332 1.00 16.00 O
ATOM 145 CB ALA A 21 5.165 15.189 46.007 1.00 17.37 C
ATOM 146 N ALA A 22 5.497 17.565 48.072 1.00 16.45 N
ATOM 147 CA ALA A 22 4.902 18.471 49.047 1.00 15.44 C
ATOM 148 C ALA A 22 5.315 19.907 48.768 1.00 14.74 C
ATOM 149 O ALA A 22 4.475 20.808 48.795 1.00 17.29 O
ATOM 150 CB ALA A 22 5.308 18.067 50.462 1.00 14.82 C
ATOM 151 N GLY A 23 6.604 20.116 48.494 1.00 12.30 N
ATOM 152 CA GLY A 23 7.095 21.454 48.207 1.00 11.55 C
ATOM 153 C GLY A 23 6.565 22.029 46.904 1.00 14.07 C
ATOM 154 O GLY A 23 6.269 23.219 46.822 1.00 13.85 O
ATOM 155 N TYR A 24 6.462 21.183 45.881 1.00 13.54 N
ATOM 156 CA TYR A 24 5.952 21.610 44.586 1.00 14.64 C
ATOM 157 C TYR A 24 4.475 21.987 44.700 1.00 14.01 C
ATOM 158 O TYR A 24 4.036 22.964 44.095 1.00 15.81 O
ATOM 159 CB TYR A 24 6.141 20.511 43.532 1.00 16.44 C
ATOM 160 CG TYR A 24 5.758 20.974 42.146 1.00 16.35 C
ATOM 161 CD1 TYR A 24 6.620 21.773 41.402 1.00 15.99 C
ATOM 162 CD2 TYR A 24 4.508 20.663 41.605 1.00 18.59 C
ATOM 163 CE1 TYR A 24 6.254 22.259 40.154 1.00 20.13 C
ATOM 164 CE2 TYR A 24 4.128 21.150 40.350 1.00 19.45 C
ATOM 165 CZ TYR A 24 5.007 21.947 39.634 1.00 21.02 C
ATOM 166 OH TYR A 24 4.644 22.444 38.403 1.00 25.33 O
ATOM 167 N LYS A 25 3.723 21.226 45.494 1.00 18.46 N
ATOM 168 CA LYS A 25 2.303 21.489 45.697 1.00 19.60 C
ATOM 169 C LYS A 25 2.106 22.878 46.296 1.00 19.66 C
ATOM 170 O LYS A 25 1.244 23.637 45.839 1.00 17.64 O
ATOM 171 CB LYS A 25 1.668 20.424 46.595 1.00 26.58 C
ATOM 172 CG LYS A 25 0.153 20.542 46.695 1.00 37.19 C
ATOM 173 CD LYS A 25 -0.475 20.596 45.302 1.00 48.48 C
ATOM 174 CE LYS A 25 -1.925 21.062 45.347 1.00 56.45 C
ATOM 175 NZ LYS A 25 -2.480 21.368 43.993 1.00 57.89 N
ATOM 176 N LEU A 26 2.913 23.219 47.300 1.00 15.77 N
ATOM 177 CA LEU A 26 2.827 24.536 47.923 1.00 15.24 C
ATOM 178 C LEU A 26 3.213 25.638 46.941 1.00 15.81 C
ATOM 179 O LEU A 26 2.578 26.686 46.908 1.00 14.31 O
ATOM 180 CB LEU A 26 3.714 24.620 49.169 1.00 19.81 C
ATOM 181 CG LEU A 26 3.228 23.918 50.440 1.00 20.22 C
ATOM 182 CD1 LEU A 26 4.168 24.263 51.579 1.00 25.64 C
ATOM 183 CD2 LEU A 26 1.825 24.370 50.782 1.00 22.42 C
ATOM 184 N HIS A 27 4.263 25.397 46.158 1.00 14.56 N
ATOM 185 CA HIS A 27 4.720 26.363 45.172 1.00 17.76 C
ATOM 186 C HIS A 27 3.606 26.620 44.168 1.00 21.75 C
ATOM 187 O HIS A 27 3.334 27.766 43.804 1.00 24.22 O
ATOM 188 CB HIS A 27 5.955 25.845 44.427 1.00 18.27 C
ATOM 189 CG HIS A 27 6.298 26.649 43.209 1.00 19.41 C
ATOM 190 ND1 HIS A 27 6.723 27.962 43.278 1.00 18.14 N
ATOM 191 CD2 HIS A 27 6.204 26.353 41.889 1.00 17.67 C
ATOM 192 CE1 HIS A 27 6.866 28.440 42.055 1.00 21.57 C
ATOM 193 NE2 HIS A 27 6.558 27.485 41.195 1.00 15.25 N
ATOM 194 N GLU A 28 2.976 25.536 43.726 1.00 23.66 N
ATOM 195 CA GLU A 28 1.892 25.583 42.760 1.00 25.75 C
ATOM 196 C GLU A 28 0.725 26.426 43.281 1.00 28.46 C
ATOM 197 O GLU A 28 0.133 27.197 42.529 1.00 29.76 O
ATOM 198 CB GLU A 28 1.443 24.157 42.468 1.00 27.51 C
ATOM 199 CG GLU A 28 0.644 23.978 41.213 1.00 40.39 C
ATOM 200 CD GLU A 28 0.405 22.510 40.904 1.00 49.23 C
ATOM 201 OE1 GLU A 28 0.031 21.751 41.830 1.00 46.84 O
ATOM 202 OE2 GLU A 28 0.603 22.112 39.733 1.00 53.27 O
ATOM 203 N ASP A 29 0.422 26.299 44.574 1.00 28.35 N
ATOM 204 CA ASP A 29 -0.669 27.053 45.194 1.00 28.81 C
ATOM 205 C ASP A 29 -0.258 28.469 45.573 1.00 27.91 C
ATOM 206 O ASP A 29 -1.103 29.291 45.909 1.00 30.07 O
ATOM 207 CB ASP A 29 -1.181 26.344 46.451 1.00 30.39 C
ATOM 208 CG ASP A 29 -1.742 24.961 46.169 1.00 37.87 C
ATOM 209 OD1 ASP A 29 -1.975 24.611 44.990 1.00 39.39 O
ATOM 210 OD2 ASP A 29 -1.951 24.215 47.149 1.00 43.92 O
ATOM 211 N GLY A 30 1.040 28.743 45.544 1.00 27.87 N
ATOM 212 CA GLY A 30 1.532 30.065 45.892 1.00 26.77 C
ATOM 213 C GLY A 30 1.581 30.285 47.396 1.00 29.55 C
ATOM 214 O GLY A 30 1.479 31.416 47.873 1.00 27.18 O
ATOM 215 N GLU A 31 1.736 29.196 48.145 1.00 27.60 N
ATOM 216 CA GLU A 31 1.797 29.252 49.601 1.00 26.99 C
ATOM 217 C GLU A 31 3.188 28.909 50.123 1.00 25.16 C
ATOM 218 O GLU A 31 3.963 28.218 49.457 1.00 24.27 O
ATOM 219 CB GLU A 31 0.779 28.292 50.208 1.00 32.18 C
ATOM 220 CG GLU A 31 -0.662 28.619 49.858 1.00 46.96 C
ATOM 221 CD GLU A 31 -1.654 27.614 50.409 1.00 54.13 C
ATOM 222 OE1 GLU A 31 -1.261 26.458 50.674 1.00 56.84 O
ATOM 223 OE2 GLU A 31 -2.840 27.981 50.565 1.00 59.63 O
ATOM 224 N THR A 32 3.500 29.418 51.311 1.00 19.22 N
ATOM 225 CA THR A 32 4.791 29.170 51.952 1.00 19.47 C
ATOM 226 C THR A 32 4.593 28.907 53.445 1.00 21.06 C
ATOM 227 O THR A 32 3.587 29.303 54.031 1.00 23.38 O
ATOM 228 CB THR A 32 5.752 30.368 51.819 1.00 19.28 C
ATOM 229 OG1 THR A 32 5.163 31.510 52.439 1.00 19.79 O
ATOM 230 CG2 THR A 32 6.060 30.680 50.358 1.00 20.72 C
ATOM 231 N VAL A 33 5.569 28.244 54.054 1.00 16.82 N
ATOM 232 CA VAL A 33 5.527 27.925 55.479 1.00 16.61 C
ATOM 233 C VAL A 33 6.903 28.145 56.109 1.00 17.84 C
ATOM 234 O VAL A 33 7.927 28.144 55.414 1.00 14.55 O
ATOM 235 CB VAL A 33 5.086 26.448 55.726 1.00 19.43 C
ATOM 236 CG1 VAL A 33 3.641 26.250 55.299 1.00 15.85 C
ATOM 237 CG2 VAL A 33 5.993 25.477 54.968 1.00 14.75 C
ATOM 238 N GLY A 34 6.926 28.363 57.418 1.00 12.91 N
ATOM 239 CA GLY A 34 8.186 28.558 58.115 1.00 15.06 C
ATOM 240 C GLY A 34 8.669 29.990 58.135 1.00 16.31 C
ATOM 241 O GLY A 34 8.199 30.822 57.361 1.00 18.53 O
ATOM 242 N SER A 35 9.635 30.277 59.003 1.00 14.34 N
ATOM 243 CA SER A 35 10.161 31.628 59.113 1.00 18.58 C
ATOM 244 C SER A 35 10.904 32.081 57.857 1.00 18.18 C
ATOM 245 O SER A 35 11.008 33.273 57.599 1.00 16.54 O
ATOM 246 CB SER A 35 11.051 31.774 60.353 1.00 19.46 C
ATOM 247 OG SER A 35 12.304 31.144 60.180 1.00 18.66 O
ATOM 248 N ASN A 36 11.420 31.137 57.077 1.00 20.43 N
ATOM 249 CA ASN A 36 12.124 31.481 55.841 1.00 23.18 C
ATOM 250 C ASN A 36 11.279 31.369 54.586 1.00 19.94 C
ATOM 251 O ASN A 36 11.806 31.420 53.480 1.00 20.36 O
ATOM 252 CB ASN A 36 13.395 30.665 55.675 1.00 28.45 C
ATOM 253 CG ASN A 36 14.537 31.233 56.455 1.00 38.78 C
ATOM 254 OD1 ASN A 36 15.208 32.156 55.996 1.00 38.67 O
ATOM 255 ND2 ASN A 36 14.748 30.716 57.666 1.00 45.09 N
ATOM 256 N SER A 37 9.975 31.181 54.771 1.00 18.86 N
ATOM 257 CA SER A 37 9.026 31.090 53.668 1.00 18.75 C
ATOM 258 C SER A 37 9.383 30.088 52.570 1.00 16.36 C
ATOM 259 O SER A 37 9.673 30.469 51.434 1.00 17.98 O
ATOM 260 CB SER A 37 8.812 32.477 53.060 1.00 20.06 C
ATOM 261 OG SER A 37 8.276 33.362 54.023 1.00 27.10 O
ATOM 262 N TYR A 38 9.344 28.805 52.913 1.00 13.80 N
ATOM 263 CA TYR A 38 9.621 27.747 51.952 1.00 12.67 C
ATOM 264 C TYR A 38 8.310 27.316 51.291 1.00 11.25 C
ATOM 265 O TYR A 38 7.260 27.329 51.922 1.00 12.40 O
ATOM 266 CB TYR A 38 10.255 26.546 52.653 1.00 8.49 C
ATOM 267 CG TYR A 38 11.637 26.820 53.195 1.00 12.63 C
ATOM 268 CD1 TYR A 38 12.735 26.922 52.342 1.00 14.01 C
ATOM 269 CD2 TYR A 38 11.849 26.971 54.563 1.00 11.43 C
ATOM 270 CE1 TYR A 38 14.008 27.161 52.837 1.00 16.35 C
ATOM 271 CE2 TYR A 38 13.124 27.214 55.068 1.00 14.28 C
ATOM 272 CZ TYR A 38 14.195 27.308 54.199 1.00 15.82 C
ATOM 273 OH TYR A 38 15.458 27.558 54.680 1.00 18.76 O
ATOM 274 N PRO A 39 8.352 26.943 50.003 1.00 14.58 N
ATOM 275 CA PRO A 39 9.559 26.920 49.173 1.00 15.22 C
ATOM 276 C PRO A 39 9.843 28.297 48.612 1.00 14.16 C
ATOM 277 O PRO A 39 8.924 29.073 48.372 1.00 20.42 O
ATOM 278 CB PRO A 39 9.189 25.933 48.064 1.00 12.43 C
ATOM 279 CG PRO A 39 7.743 26.191 47.884 1.00 13.16 C
ATOM 280 CD PRO A 39 7.224 26.312 49.297 1.00 14.26 C
ATOM 281 N HIS A 40 11.118 28.628 48.462 1.00 12.93 N
ATOM 282 CA HIS A 40 11.480 29.921 47.898 1.00 15.58 C
ATOM 283 C HIS A 40 12.562 29.697 46.850 1.00 14.73 C
ATOM 284 O HIS A 40 13.185 28.637 46.809 1.00 12.19 O
ATOM 285 CB HIS A 40 11.922 30.924 48.989 1.00 10.89 C
ATOM 286 CG HIS A 40 13.205 30.557 49.688 1.00 14.82 C
ATOM 287 ND1 HIS A 40 14.440 30.713 49.092 1.00 16.06 N
ATOM 288 CD2 HIS A 40 13.431 30.072 50.934 1.00 14.67 C
ATOM 289 CE1 HIS A 40 15.373 30.346 49.944 1.00 21.30 C
ATOM 290 NE2 HIS A 40 14.796 29.953 51.066 1.00 16.75 N
ATOM 291 N LYS A 41 12.770 30.689 45.992 1.00 15.17 N
ATOM 292 CA LYS A 41 13.765 30.580 44.938 1.00 15.87 C
ATOM 293 C LYS A 41 15.168 30.301 45.420 1.00 14.34 C
ATOM 294 O LYS A 41 15.612 30.857 46.423 1.00 15.04 O
ATOM 295 CB LYS A 41 13.774 31.829 44.060 1.00 17.33 C
ATOM 296 CG LYS A 41 12.585 31.927 43.137 1.00 34.08 C
ATOM 297 CD LYS A 41 12.857 32.905 42.002 1.00 41.57 C
ATOM 298 CE LYS A 41 13.163 34.298 42.529 1.00 50.78 C
ATOM 299 NZ LYS A 41 11.990 34.916 43.212 1.00 57.81 N
ATOM 300 N TYR A 42 15.836 29.401 44.706 1.00 12.17 N
ATOM 301 CA TYR A 42 17.216 29.038 44.989 1.00 12.41 C
ATOM 302 C TYR A 42 17.963 29.617 43.782 1.00 16.02 C
ATOM 303 O TYR A 42 17.756 29.180 42.650 1.00 14.34 O
ATOM 304 CB TYR A 42 17.358 27.518 45.057 1.00 8.50 C
ATOM 305 CG TYR A 42 18.774 27.050 45.269 1.00 15.19 C
ATOM 306 CD1 TYR A 42 19.402 27.192 46.506 1.00 14.89 C
ATOM 307 CD2 TYR A 42 19.515 26.515 44.208 1.00 13.63 C
ATOM 308 CE1 TYR A 42 20.734 26.822 46.680 1.00 14.94 C
ATOM 309 CE2 TYR A 42 20.839 26.145 44.373 1.00 15.90 C
ATOM 310 CZ TYR A 42 21.443 26.304 45.606 1.00 18.88 C
ATOM 311 OH TYR A 42 22.767 25.974 45.753 1.00 21.37 O
ATOM 312 N ASN A 43 18.788 30.632 44.021 1.00 14.48 N
ATOM 313 CA ASN A 43 19.510 31.297 42.939 1.00 17.27 C
ATOM 314 C ASN A 43 20.754 30.596 42.402 1.00 19.05 C
ATOM 315 O ASN A 43 21.310 31.009 41.388 1.00 21.97 O
ATOM 316 CB ASN A 43 19.839 32.738 43.343 1.00 20.04 C
ATOM 317 CG ASN A 43 18.596 33.545 43.675 1.00 23.64 C
ATOM 318 OD1 ASN A 43 17.607 33.517 42.935 1.00 27.42 O
ATOM 319 ND2 ASN A 43 18.632 34.254 44.796 1.00 23.74 N
ATOM 320 N ASN A 44 21.175 29.530 43.073 1.00 18.69 N
ATOM 321 CA ASN A 44 22.354 28.764 42.686 1.00 18.45 C
ATOM 322 C ASN A 44 23.663 29.550 42.819 1.00 19.18 C
ATOM 323 O ASN A 44 24.501 29.540 41.914 1.00 19.89 O
ATOM 324 CB ASN A 44 22.192 28.197 41.262 1.00 19.83 C
ATOM 325 CG ASN A 44 23.117 27.007 40.992 1.00 21.21 C
ATOM 326 OD1 ASN A 44 23.678 26.415 41.916 1.00 23.50 O
ATOM 327 ND2 ASN A 44 23.261 26.644 39.726 1.00 17.14 N
ATOM 328 N TYR A 45 23.845 30.216 43.955 1.00 17.08 N
ATOM 329 CA TYR A 45 25.066 30.978 44.207 1.00 19.19 C
ATOM 330 C TYR A 45 26.264 30.036 44.256 1.00 18.95 C
ATOM 331 O TYR A 45 27.393 30.452 44.009 1.00 23.10 O
ATOM 332 CB TYR A 45 24.983 31.732 45.542 1.00 19.12 C
ATOM 333 CG TYR A 45 23.927 32.802 45.603 1.00 22.35 C
ATOM 334 CD1 TYR A 45 23.628 33.589 44.490 1.00 22.28 C
ATOM 335 CD2 TYR A 45 23.220 33.034 46.784 1.00 27.35 C
ATOM 336 CE1 TYR A 45 22.647 34.584 44.555 1.00 27.94 C
ATOM 337 CE2 TYR A 45 22.243 34.025 46.858 1.00 24.28 C
ATOM 338 CZ TYR A 45 21.962 34.790 45.744 1.00 27.43 C
ATOM 339 OH TYR A 45 20.997 35.768 45.824 1.00 35.41 O
ATOM 340 N GLU A 46 26.011 28.780 44.617 1.00 19.22 N
ATOM 341 CA GLU A 46 27.049 27.753 44.708 1.00 18.57 C
ATOM 342 C GLU A 46 27.523 27.304 43.328 1.00 21.57 C
ATOM 343 O GLU A 46 28.583 26.687 43.202 1.00 19.77 O
ATOM 344 CB GLU A 46 26.542 26.531 45.480 1.00 14.47 C
ATOM 345 CG GLU A 46 26.531 26.672 47.009 1.00 15.53 C
ATOM 346 CD GLU A 46 25.448 27.596 47.536 1.00 15.43 C
ATOM 347 OE1 GLU A 46 24.416 27.806 46.859 1.00 14.94 O
ATOM 348 OE2 GLU A 46 25.626 28.110 48.650 1.00 18.11 O
ATOM 349 N GLY A 47 26.719 27.586 42.304 1.00 23.63 N
ATOM 350 CA GLY A 47 27.079 27.212 40.946 1.00 21.31 C
ATOM 351 C GLY A 47 27.058 25.721 40.672 1.00 22.05 C
ATOM 352 O GLY A 47 27.971 25.199 40.030 1.00 21.20 O
ATOM 353 N PHE A 48 26.051 25.025 41.189 1.00 19.26 N
ATOM 354 CA PHE A 48 25.939 23.601 40.950 1.00 21.29 C
ATOM 355 C PHE A 48 25.586 23.382 39.491 1.00 23.87 C
ATOM 356 O PHE A 48 24.850 24.175 38.889 1.00 23.18 O
ATOM 357 CB PHE A 48 24.856 22.977 41.825 1.00 19.46 C
ATOM 358 CG PHE A 48 25.194 22.963 43.281 1.00 24.92 C
ATOM 359 CD1 PHE A 48 26.320 22.285 43.737 1.00 26.35 C
ATOM 360 CD2 PHE A 48 24.383 23.612 44.205 1.00 22.02 C
ATOM 361 CE1 PHE A 48 26.639 22.261 45.089 1.00 26.56 C
ATOM 362 CE2 PHE A 48 24.694 23.591 45.561 1.00 22.98 C
ATOM 363 CZ PHE A 48 25.821 22.911 46.004 1.00 24.36 C
ATOM 364 N ASP A 49 26.126 22.292 38.951 1.00 30.52 N
ATOM 365 CA ASP A 49 25.892 21.897 37.571 1.00 36.88 C
ATOM 366 C ASP A 49 24.608 21.070 37.493 1.00 33.44 C
ATOM 367 O ASP A 49 24.653 19.842 37.444 1.00 34.92 O
ATOM 368 CB ASP A 49 27.104 21.113 37.020 1.00 43.56 C
ATOM 369 CG ASP A 49 27.348 19.785 37.743 1.00 54.31 C
ATOM 370 OD1 ASP A 49 27.232 19.735 38.991 1.00 58.33 O
ATOM 371 OD2 ASP A 49 27.649 18.783 37.051 1.00 58.74 O
ATOM 372 N PHE A 50 23.461 21.748 37.548 1.00 28.23 N
ATOM 373 CA PHE A 50 22.184 21.043 37.461 1.00 23.61 C
ATOM 374 C PHE A 50 21.865 20.674 36.016 1.00 23.52 C
ATOM 375 O PHE A 50 22.153 21.442 35.096 1.00 21.71 O
ATOM 376 CB PHE A 50 21.054 21.890 38.041 1.00 22.61 C
ATOM 377 CG PHE A 50 21.152 22.109 39.528 1.00 22.87 C
ATOM 378 CD1 PHE A 50 21.494 21.059 40.379 1.00 21.22 C
ATOM 379 CD2 PHE A 50 20.871 23.358 40.081 1.00 21.90 C
ATOM 380 CE1 PHE A 50 21.549 21.249 41.760 1.00 22.10 C
ATOM 381 CE2 PHE A 50 20.923 23.557 41.458 1.00 20.37 C
ATOM 382 CZ PHE A 50 21.264 22.496 42.299 1.00 20.16 C
ATOM 383 N SER A 51 21.283 19.492 35.828 1.00 19.48 N
ATOM 384 CA SER A 51 20.917 19.006 34.499 1.00 24.72 C
ATOM 385 C SER A 51 19.560 19.505 34.023 1.00 23.38 C
ATOM 386 O SER A 51 19.178 19.274 32.880 1.00 26.82 O
ATOM 387 CB SER A 51 20.914 17.483 34.481 1.00 24.34 C
ATOM 388 OG SER A 51 22.225 17.011 34.676 1.00 39.22 O
ATOM 389 N VAL A 52 18.810 20.139 34.915 1.00 21.89 N
ATOM 390 CA VAL A 52 17.499 20.661 34.566 1.00 20.16 C
ATOM 391 C VAL A 52 17.557 22.184 34.609 1.00 18.59 C
ATOM 392 O VAL A 52 18.374 22.757 35.322 1.00 17.17 O
ATOM 393 CB VAL A 52 16.402 20.103 35.504 1.00 20.43 C
ATOM 394 CG1 VAL A 52 16.325 18.579 35.371 1.00 13.89 C
ATOM 395 CG2 VAL A 52 16.688 20.497 36.945 1.00 14.63 C
ATOM 396 N SER A 53 16.703 22.836 33.834 1.00 15.90 N
ATOM 397 CA SER A 53 16.717 24.289 33.778 1.00 21.84 C
ATOM 398 C SER A 53 16.036 24.996 34.949 1.00 20.56 C
ATOM 399 O SER A 53 15.195 24.412 35.641 1.00 21.68 O
ATOM 400 CB SER A 53 16.127 24.764 32.449 1.00 23.33 C
ATOM 401 OG SER A 53 14.808 24.295 32.291 1.00 30.62 O
ATOM 402 N SER A 54 16.442 26.245 35.173 1.00 17.11 N
ATOM 403 CA SER A 54 15.902 27.089 36.231 1.00 17.56 C
ATOM 404 C SER A 54 14.521 27.581 35.786 1.00 15.45 C
ATOM 405 O SER A 54 14.096 27.299 34.669 1.00 15.30 O
ATOM 406 CB SER A 54 16.854 28.261 36.481 1.00 19.54 C
ATOM 407 OG SER A 54 17.019 29.034 35.309 1.00 18.60 O
ATOM 408 N PRO A 55 13.788 28.308 36.658 1.00 16.09 N
ATOM 409 CA PRO A 55 14.145 28.673 38.032 1.00 18.10 C
ATOM 410 C PRO A 55 14.108 27.493 39.002 1.00 17.66 C
ATOM 411 O PRO A 55 13.364 26.532 38.808 1.00 15.66 O
ATOM 412 CB PRO A 55 13.095 29.736 38.378 1.00 18.90 C
ATOM 413 CG PRO A 55 11.903 29.287 37.607 1.00 17.35 C
ATOM 414 CD PRO A 55 12.498 28.901 36.277 1.00 15.50 C
ATOM 415 N TYR A 56 14.954 27.555 40.020 1.00 17.23 N
ATOM 416 CA TYR A 56 15.029 26.507 41.028 1.00 15.84 C
ATOM 417 C TYR A 56 14.369 26.989 42.316 1.00 17.20 C
ATOM 418 O TYR A 56 14.277 28.198 42.573 1.00 16.41 O
ATOM 419 CB TYR A 56 16.490 26.152 41.315 1.00 13.80 C
ATOM 420 CG TYR A 56 17.287 25.785 40.093 1.00 15.03 C
ATOM 421 CD1 TYR A 56 16.940 24.671 39.324 1.00 15.53 C
ATOM 422 CD2 TYR A 56 18.386 26.555 39.697 1.00 14.39 C
ATOM 423 CE1 TYR A 56 17.670 24.328 38.185 1.00 13.69 C
ATOM 424 CE2 TYR A 56 19.126 26.221 38.560 1.00 19.34 C
ATOM 425 CZ TYR A 56 18.759 25.108 37.812 1.00 18.09 C
ATOM 426 OH TYR A 56 19.480 24.791 36.692 1.00 20.58 O
ATOM 427 N TYR A 57 13.902 26.034 43.113 1.00 12.59 N
ATOM 428 CA TYR A 57 13.262 26.335 44.389 1.00 13.63 C
ATOM 429 C TYR A 57 13.786 25.343 45.414 1.00 13.57 C
ATOM 430 O TYR A 57 13.969 24.168 45.095 1.00 12.58 O
ATOM 431 CB TYR A 57 11.741 26.183 44.285 1.00 10.33 C
ATOM 432 CG TYR A 57 11.118 27.085 43.259 1.00 19.86 C
ATOM 433 CD1 TYR A 57 10.738 28.387 43.585 1.00 19.68 C
ATOM 434 CD2 TYR A 57 10.950 26.653 41.941 1.00 20.91 C
ATOM 435 CE1 TYR A 57 10.206 29.249 42.614 1.00 21.71 C
ATOM 436 CE2 TYR A 57 10.427 27.497 40.972 1.00 21.57 C
ATOM 437 CZ TYR A 57 10.056 28.794 41.315 1.00 23.29 C
ATOM 438 OH TYR A 57 9.530 29.631 40.360 1.00 26.51 O
ATOM 439 N GLU A 58 14.072 25.821 46.621 1.00 9.75 N
ATOM 440 CA GLU A 58 14.546 24.931 47.672 1.00 10.81 C
ATOM 441 C GLU A 58 13.429 24.669 48.684 1.00 10.86 C
ATOM 442 O GLU A 58 12.623 25.557 48.997 1.00 12.99 O
ATOM 443 CB GLU A 58 15.814 25.473 48.352 1.00 15.07 C
ATOM 444 CG GLU A 58 15.654 26.821 49.046 1.00 14.49 C
ATOM 445 CD GLU A 58 16.800 27.131 49.990 1.00 16.19 C
ATOM 446 OE1 GLU A 58 16.963 26.416 51.000 1.00 17.41 O