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HEADER ANTIBIOTIC 23-JAN-97 1AA5
TITLE VANCOMYCIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VANCOMYCIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: AMYCOLATOPSIS ORIENTALIS;
SOURCE 4 ORGANISM_TAXID: 31958
KEYWDS GLYCOPEPTIDE, ANTIBIOTIC
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.LOLL,A.E.BEVIVINO,B.D.KORTY,P.H.AXELSEN
REVDAT 4 27-JUL-11 1AA5 1 HETATM REMARK
REVDAT 3 13-JUL-11 1AA5 1 VERSN
REVDAT 2 24-FEB-09 1AA5 1 VERSN
REVDAT 1 20-AUG-97 1AA5 0
JRNL AUTH P.J.LOLL,A.E.BEVIVINO,B.D.KORTY,P.H.AXELSEN
JRNL TITL SIMULTANEOUS RECOGNITION OF A CARBOXYLATE-CONTAINING LIGAND
JRNL TITL 2 AND AN INTRAMOLECULAR SURROGATE LIGAND IN THE CRYSTAL
JRNL TITL 3 STRUCTURE OF AN ASYMMETRIC VANCOMYCIN DIMER.
JRNL REF J.AM.CHEM.SOC. V. 119 1516 1997
JRNL REFN ISSN 0002-7863
JRNL DOI 10.1021/JA963566P
REMARK 2
REMARK 2 RESOLUTION. 0.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-93
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 4.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.0
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.124
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.124
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 17899
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.112
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.112
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 17479
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 160
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 55
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 255.40
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 158.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 3
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 2553
REMARK 3 NUMBER OF RESTRAINTS : 3647
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 ANGLE DISTANCES (A) : NULL
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.019
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.008
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.011
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.025
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT WAS CARRIED OUT VS. F**2;
REMARK 3 SIMILAR 1,2 AND 1,3 DISTANCE RESTRAINTS WERE APPLIED TO THE TWO
REMARK 3 VANCOMYCIN MOLECULES. ALSO, RESTRAINTS WERE IMPOSED TO LIMIT
REMARK 3 DEVIATIONS OF RINGS AND PEPTIDE BONDS FROM PLANARITY AND
REMARK 3 DIFFERENCES IN ALONG-BOND COMPONENTS OF ADPS. ADPS FOR SOLVENT
REMARK 3 WERE RESTRAINED TO BE APPROXIMATELY ISOTROPIC, AND ANTIBUMPING
REMARK 3 RESTRAINTS WERE USED TO PREVENT SOLVENT WATER MOLECULES FROM
REMARK 3 VIOLATING MINIMUM CONTACT DISTANCES. CONJUGATE GRADIENT LEAST
REMARK 3 SQUARES WAS USED FOR MOST OF THE REFINEMENT, WITH BLOCKED LEAST
REMARK 3 SQUARES AT THE END.
REMARK 4
REMARK 4 1AA5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
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 : APR-96
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.85
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MADNES, PROCOR
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17899
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.890
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 200 DATA REDUNDANCY : 12.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 100.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.14300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 31.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT METHODS
REMARK 200 SOFTWARE USED: SHELXL-93
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 25.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY MIXING EQUAL
REMARK 280 VOLUMES OF A 25 MG/ML VANCOMYCIN SOLUTION AND 2.2 M NACL, 0.1 M
REMARK 280 SODIUM ACETATE, PH 4.6 (RESERVOIR BUFFER) AND THEN SUSPENDING
REMARK 280 THIS DROP OVER THE RESERVOIR. CRYSTALS WERE GROWN AT 293 K.,
REMARK 280 VAPOR DIFFUSION - HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 32.92000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 14.22500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 14.22500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 49.38000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 14.22500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 14.22500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 16.46000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 14.22500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 14.22500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 49.38000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 14.22500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 14.22500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 16.46000
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 32.92000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA 1.18
REMARK 350 TOTAL BURIED SURFACE AREA: 1370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 2890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.8 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 14.22500
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 14.22500
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -16.46000
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 A2015 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 VANCOMYCIN IS A TRICYCLIC GLYCOPEPTIDE. THE SCAFFOLD IS
REMARK 400 A HEPTAPEPTIDE WITH THE CONFIGURATION D-D-L-D-D-L-L. IT IS
REMARK 400 FURTHER GLYCOSYLATED BY A DISACCHARIDE MADE OF D-GLUCOSE
REMARK 400 AND VANCOSAMINE.
REMARK 400 HERE, VANCOMYCIN IS REPRESENTED BY GROUPING TOGETHER THE
REMARK 400 SEQUENCE (SEQRES) AND THE TWO LIGANDS (HET) BGC AND RER.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: VANCOMYCIN
REMARK 400 CHAIN: A, B
REMARK 400 COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 7
REMARK 400 COMPONENT_2: SUGAR RESIDUES 8, 9
REMARK 400 DESCRIPTION: VANCOMYCIN IS A TRICYCLIC GLYCOPEPTIDE,
REMARK 400 GLYCOSYLATED BY A DISACCHARIDE (RESIDUES 8
REMARK 400 AND 9) ON RESIDUE 4.
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 O2 BGC B 8 O5 RER B 9 2.01
REMARK 500 C2 BGC B 8 C1 RER B 9 2.18
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 3 -69.08 -100.65
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 A2004 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH A2007 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH A2008 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH B2004 DISTANCE = 5.28 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 21
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 21
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF VANCOMYCIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF VANCOMYCIN
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN COMPLEXED WITH 2-ACETOXY-D-
REMARK 900 PROPANOIC ACID
REMARK 900 RELATED ID: 1C0R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN WITH D-LACTIC ACID
REMARK 900 RELATED ID: 1FVM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN COMPLEXED WITH DI-ACETYL-
REMARK 900 LYS-D-ALA-D-ALA
REMARK 900 RELATED ID: 1GAC RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF A82846B COMPLEXED WITH ITS CELL WALL
REMARK 900 PENTAPEPTIDE FRAGMENT
REMARK 900 RELATED ID: 1GHG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON
REMARK 900 RELATED ID: 1PN3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TDP-EPI-VANCOSAMINYLTRANSFERASE GTFA
REMARK 900 COMPLEXD WITH TDP AND DESVANCOSAMINYL VANCOMYCIN
REMARK 900 RELATED ID: 1PNV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TDP-EPI-VANCOSAMINYLTRANSFERASE GTFA
REMARK 900 COMPLEXED WITH TDP AND VANCOMYCIN
REMARK 900 RELATED ID: 1QD8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN COMPLEXED WITH N-ACETYL
REMARK 900 GLYCIN
REMARK 900 RELATED ID: 1RRV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TDP-VANCOSAMINYLTRANSFERASE GTFD
REMARK 900 COMPLEXED WITH TDP AND DESVANCOSAMINYL VANCOMYCIN.
REMARK 900 RELATED ID: 1SHO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN
DBREF 1AA5 A 1 7 NOR NOR00681 NOR00681 1 7
DBREF 1AA5 B 1 7 NOR NOR00681 NOR00681 1 7
SEQRES 1 A 7 MLU OMZ ASN GHP GHP OMY 3FG
SEQRES 1 B 7 MLU OMZ ASN GHP GHP OMY 3FG
HET MLU A 1 31
HET OMZ A 2 21
HET GHP A 4 15
HET GHP A 5 17
HET OMY A 6 21
HET 3FG A 7 20
HET MLU B 1 24
HET OMZ B 2 21
HET GHP B 4 16
HET GHP B 5 17
HET OMY B 6 21
HET 3FG B 7 20
HET BGC A 8 21
HET RER A 9 26
HET ACY A 11 8
HET CL A 21 1
HET CL A 22 1
HET BGC B 8 42
HET RER B 9 25
HET CL B 21 1
HET CL B 22 1
HETNAM MLU N-METHYLLEUCINE
HETNAM OMZ (BETAR)-3-CHLORO-BETA-HYDROXY-D-TYROSINE
HETNAM GHP (2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC ACID
HETNAM OMY (BETAR)-3-CHLORO-BETA-HYDROXY-L-TYROSINE
HETNAM 3FG (2S)-AMINO(3,5-DIHYDROXYPHENYL)ETHANOIC ACID
HETNAM BGC BETA-D-GLUCOSE
HETNAM RER (1R,3S,4S,5S)-3-AMINO-2,3,6-TRIDEOXY-3-METHYL-ALPHA-L-
HETNAM 2 RER ARABINO-HEXOPYRANOSE
HETNAM ACY ACETIC ACID
HETNAM CL CHLORIDE ION
HETSYN RER VANCOSAMINE
FORMUL 1 MLU 2(C7 H15 N O2)
FORMUL 1 OMZ 2(C9 H10 CL N O4)
FORMUL 1 GHP 4(C8 H9 N O3)
FORMUL 1 OMY 2(C9 H10 CL N O4)
FORMUL 1 3FG 2(C8 H9 N O4)
FORMUL 3 BGC 2(C6 H12 O6)
FORMUL 3 RER 2(C7 H15 N O3)
FORMUL 4 ACY C2 H4 O2
FORMUL 5 CL 4(CL 1-)
FORMUL 10 HOH *55(H2 O)
LINK C MLU A 1 N OMZ A 2 1555 1555 1.35
LINK C OMZ A 2 N ASN A 3 1555 1555 1.33
LINK OH OMZ A 2 C5 GHP A 4 1555 1555 1.39
LINK C ASN A 3 N GHP A 4 1555 1555 1.32
LINK C GHP A 4 N GHP A 5 1555 1555 1.36
LINK C3 GHP A 4 OCZ OMY A 6 1555 1555 1.39
LINK O4 GHP A 4 C1 BGC A 8 1555 1555 1.41
LINK C GHP A 5 N OMY A 6 1555 1555 1.33
LINK C3 GHP A 5 CG1 3FG A 7 1555 1555 1.50
LINK C OMY A 6 N 3FG A 7 1555 1555 1.34
LINK O2 BGC A 8 C1 RER A 9 1555 1555 1.41
LINK C MLU B 1 N OMZ B 2 1555 1555 1.33
LINK OH OMZ B 2 C5 GHP B 4 1555 1555 1.40
LINK C OMZ B 2 N ASN B 3 1555 1555 1.32
LINK C ASN B 3 N GHP B 4 1555 1555 1.34
LINK O4 BGHP B 4 C1 BBGC B 8 1555 1555 1.45
LINK O4 AGHP B 4 C1 ABGC B 8 1555 1555 1.41
LINK C3 GHP B 4 OCZ OMY B 6 1555 1555 1.38
LINK C GHP B 4 N GHP B 5 1555 1555 1.34
LINK C3 GHP B 5 CG1 3FG B 7 1555 1555 1.51
LINK C GHP B 5 N OMY B 6 1555 1555 1.34
LINK C OMY B 6 N 3FG B 7 1555 1555 1.32
LINK O2 BBGC B 8 C1 RER B 9 1555 1555 1.10
LINK O2 ABGC B 8 C1 RER B 9 1555 1555 1.47
CISPEP 1 GHP A 5 OMY A 6 0 6.04
CISPEP 2 GHP B 5 OMY B 6 0 18.86
SITE 1 AC1 6 HOH A2033 HOH A2034 MLU B 1 OMZ B 2
SITE 2 AC1 6 ASN B 3 GHP B 4
SITE 1 AC2 4 ASN A 3 OMY A 6 3FG A 7 OMZ B 2
SITE 1 AC3 4 MLU A 1 OMZ A 2 HOH A2003 HOH A2005
SITE 1 AC4 4 OMZ A 2 RER A 9 MLU B 1 RER B 9
SITE 1 AC5 3 OMY B 6 3FG B 7 HOH B2006
SITE 1 AC6 36 CL A 21 CL A 22 HOH A2001 HOH A2002
SITE 2 AC6 36 HOH A2009 HOH A2010 HOH A2015 HOH A2016
SITE 3 AC6 36 HOH A2017 HOH A2018 HOH A2019 HOH A2021
SITE 4 AC6 36 HOH A2022 HOH A2023 HOH A2024 HOH A2025
SITE 5 AC6 36 HOH A2026 HOH A2027 HOH A2029 HOH A2030
SITE 6 AC6 36 HOH A2031 HOH A2032 MLU B 1 OMZ B 2
SITE 7 AC6 36 ASN B 3 GHP B 4 GHP B 5 OMY B 6
SITE 8 AC6 36 3FG B 7 BGC B 8 RER B 9 CL B 21
SITE 9 AC6 36 HOH B2001 HOH B2007 HOH B2017 HOH B2018
SITE 1 AC7 32 MLU A 1 OMZ A 2 ASN A 3 GHP A 4
SITE 2 AC7 32 GHP A 5 OMY A 6 3FG A 7 BGC A 8
SITE 3 AC7 32 RER A 9 ACY A 11 CL A 21 HOH A2001
SITE 4 AC7 32 HOH A2026 HOH A2030 CL B 21 CL B 22
SITE 5 AC7 32 HOH B2001 HOH B2002 HOH B2003 HOH B2006
SITE 6 AC7 32 HOH B2007 HOH B2008 HOH B2009 HOH B2010
SITE 7 AC7 32 HOH B2011 HOH B2012 HOH B2013 HOH B2015
SITE 8 AC7 32 HOH B2017 HOH B2018 HOH B2019 HOH B2020
CRYST1 28.450 28.450 65.840 90.00 90.00 90.00 P 43 21 2 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 0.035149 0.000000 0.000000 0.00000
SCALE2 0.000000 0.035149 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015188 0.00000
HETATM 1 N MLU A 1 10.127 8.826 -4.030 1.00 4.98 N
HETATM 2 CN MLU A 1 10.446 10.141 -4.639 1.00 7.32 C
HETATM 3 CA MLU A 1 8.858 8.812 -3.244 1.00 4.18 C
HETATM 4 C MLU A 1 7.715 9.246 -4.189 1.00 3.80 C
HETATM 5 O MLU A 1 7.547 8.688 -5.252 1.00 5.85 O
HETATM 6 CB MLU A 1 8.552 7.426 -2.726 1.00 4.30 C
HETATM 7 CG MLU A 1 9.587 6.788 -1.780 1.00 4.89 C
HETATM 8 CD1AMLU A 1 9.125 5.395 -1.392 0.74 5.46 C
HETATM 9 CD1BMLU A 1 10.667 6.044 -2.523 0.26 5.31 C
HETATM 10 CD2AMLU A 1 9.835 7.620 -0.583 0.74 7.84 C
HETATM 11 CD2BMLU A 1 8.866 5.876 -0.846 0.26 5.59 C
HETATM 12 H MLU A 1 10.887 8.557 -3.424 1.00 7.47 H
HETATM 13 HCN1 MLU A 1 11.271 10.077 -5.126 1.00 10.98 H
HETATM 14 HCN2 MLU A 1 10.533 10.801 -3.948 1.00 10.98 H
HETATM 15 HCN3 MLU A 1 9.740 10.396 -5.238 1.00 10.98 H
HETATM 16 HA MLU A 1 8.925 9.440 -2.494 1.00 6.27 H
HETATM 17 HB2 MLU A 1 8.440 6.837 -3.489 1.00 6.45 H
HETATM 18 HB3 MLU A 1 7.701 7.460 -2.261 1.00 6.45 H
HETATM 19 HG MLU A 1 10.432 6.702 -2.269 1.00 7.34 H
HETATM 20 HD11AMLU A 1 8.972 4.876 -2.185 0.74 8.19 H
HETATM 21 HD11BMLU A 1 8.184 6.367 -0.382 0.26 8.38 H
HETATM 22 HD12AMLU A 1 8.311 5.457 -0.888 0.74 8.19 H
HETATM 23 HD12BMLU A 1 9.487 5.511 -0.211 0.26 8.38 H
HETATM 24 HD13AMLU A 1 9.801 4.971 -0.858 0.74 8.19 H
HETATM 25 HD21AMLU A 1 10.127 8.494 -0.855 0.74 11.77 H
HETATM 26 HD21BMLU A 1 11.298 5.684 -1.895 0.26 7.97 H
HETATM 27 HD22AMLU A 1 10.515 7.210 -0.043 0.74 11.77 H
HETATM 28 HD22BMLU A 1 11.118 6.647 -3.119 0.26 7.97 H
HETATM 29 HD23AMLU A 1 9.025 7.698 -0.073 0.74 11.77 H
HETATM 30 HD23BMLU A 1 10.274 5.329 -3.028 0.26 7.97 H
HETATM 31 HN22 MLU A 1 10.062 8.136 -4.764 1.00 7.47 H
HETATM 32 N OMZ A 2 6.894 10.223 -3.742 1.00 3.44 N
HETATM 33 CA OMZ A 2 5.824 10.725 -4.588 1.00 3.72 C
HETATM 34 C OMZ A 2 4.491 9.963 -4.459 1.00 3.04 C
HETATM 35 O OMZ A 2 3.547 10.291 -5.161 1.00 3.76 O
HETATM 36 CB OMZ A 2 5.544 12.254 -4.376 1.00 3.81 C
HETATM 37 OC OMZ A 2 6.731 13.006 -4.505 1.00 4.29 O
HETATM 38 CG OMZ A 2 4.868 12.532 -3.066 1.00 3.68 C
HETATM 39 CD1 OMZ A 2 3.489 12.760 -3.038 1.00 4.01 C
HETATM 40 CD2 OMZ A 2 5.577 12.564 -1.859 1.00 3.89 C
HETATM 41 CE1 OMZ A 2 2.836 12.923 -1.830 1.00 4.46 C
HETATM 42 CL OMZ A 2 1.135 13.234 -1.833 1.00 7.25 CL
HETATM 43 CE2 OMZ A 2 4.904 12.695 -0.669 1.00 4.34 C
HETATM 44 CZ OMZ A 2 3.523 12.845 -0.655 1.00 4.40 C
HETATM 45 OH OMZ A 2 2.866 12.894 0.557 1.00 4.99 O
HETATM 46 H OMZ A 2 7.005 10.548 -2.953 1.00 5.16 H
HETATM 47 HA OMZ A 2 6.123 10.618 -5.515 1.00 5.58 H
HETATM 48 HB OMZ A 2 4.935 12.542 -5.088 1.00 5.71 H
HETATM 49 HC OMZ A 2 7.083 12.839 -5.227 1.00 6.44 H
HETATM 50 HD1 OMZ A 2 3.009 12.801 -3.834 1.00 6.01 H
HETATM 51 HD2 OMZ A 2 6.505 12.495 -1.863 1.00 5.83 H
HETATM 52 HE2 OMZ A 2 5.375 12.684 0.132 1.00 6.50 H
ATOM 53 N ASN A 3 4.449 8.963 -3.584 1.00 3.20 N
ATOM 54 CA ASN A 3 3.334 8.009 -3.566 1.00 3.32 C
ATOM 55 C ASN A 3 2.302 8.294 -2.468 1.00 2.84 C
ATOM 56 O ASN A 3 1.165 8.692 -2.806 1.00 3.32 O
ATOM 57 CB ASN A 3 3.841 6.575 -3.629 1.00 3.47 C
ATOM 58 CG ASN A 3 4.943 6.227 -2.632 1.00 3.25 C
ATOM 59 OD1 ASN A 3 5.227 6.979 -1.683 1.00 3.62 O
ATOM 60 ND2 ASN A 3 5.555 5.076 -2.861 1.00 3.99 N
ATOM 61 H ASN A 3 5.089 8.874 -3.016 1.00 4.81 H
ATOM 62 HA ASN A 3 2.859 8.152 -4.411 1.00 4.98 H
ATOM 63 HB2 ASN A 3 3.092 5.978 -3.479 1.00 5.21 H
ATOM 64 HB3 ASN A 3 4.173 6.406 -4.525 1.00 5.21 H
ATOM 65 HD21 ASN A 3 5.321 4.591 -3.531 1.00 5.99 H
ATOM 66 HD22 ASN A 3 6.186 4.813 -2.339 1.00 5.99 H
HETATM 67 N GHP A 4 2.669 8.100 -1.216 1.00 2.95 N
HETATM 68 CA GHP A 4 1.695 8.107 -0.115 1.00 3.06 C
HETATM 69 C GHP A 4 1.887 6.862 0.723 1.00 2.95 C
HETATM 70 O GHP A 4 2.988 6.455 1.041 1.00 3.19 O
HETATM 71 C1 GHP A 4 1.720 9.379 0.737 1.00 3.09 C
HETATM 72 C2 GHP A 4 1.139 9.408 1.973 1.00 3.55 C
HETATM 73 C3 GHP A 4 1.145 10.574 2.737 1.00 3.86 C
HETATM 74 C4 GHP A 4 1.693 11.737 2.232 1.00 3.66 C
HETATM 75 O4 GHP A 4 1.794 12.903 3.004 1.00 4.62 O
HETATM 76 C5 GHP A 4 2.275 11.709 0.977 1.00 3.85 C
HETATM 77 C6 GHP A 4 2.290 10.550 0.247 1.00 3.65 C
HETATM 78 H GHP A 4 3.500 7.966 -1.039 1.00 4.43 H
HETATM 79 HA GHP A 4 0.804 8.049 -0.519 1.00 4.59 H
HETATM 80 HC2 GHP A 4 0.734 8.641 2.309 1.00 5.33 H
HETATM 81 H6 GHP A 4 2.690 10.545 -0.592 1.00 5.48 H
HETATM 82 N GHP A 5 0.734 6.293 1.150 1.00 2.98 N
HETATM 83 CA GHP A 5 0.718 5.365 2.242 1.00 3.22 C
HETATM 84 C GHP A 5 -0.686 5.468 2.895 1.00 3.21 C
HETATM 85 O GHP A 5 -1.628 5.852 2.205 1.00 3.91 O
HETATM 86 C1 GHP A 5 0.930 3.872 1.977 1.00 3.30 C
HETATM 87 C2 GHP A 5 1.938 3.204 2.649 1.00 3.06 C
HETATM 88 C3 GHP A 5 2.017 1.808 2.682 1.00 3.62 C
HETATM 89 C4 GHP A 5 1.043 1.086 1.989 1.00 4.21 C
HETATM 90 O4 GHP A 5 1.089 -0.286 2.062 1.00 5.46 O
HETATM 91 C5 GHP A 5 0.080 1.751 1.263 1.00 4.79 C
HETATM 92 C6 GHP A 5 0.018 3.128 1.238 1.00 3.73 C
HETATM 93 H GHP A 5 -0.005 6.492 0.758 1.00 4.47 H
HETATM 94 HA GHP A 5 1.384 5.656 2.900 1.00 4.82 H
HETATM 95 HC2 GHP A 5 2.586 3.701 3.094 1.00 4.60 H
HETATM 96 HO4 GHP A 5 0.476 -0.604 1.619 1.00 8.19 H
HETATM 97 H5 GHP A 5 -0.543 1.260 0.779 1.00 7.18 H
HETATM 98 H6 GHP A 5 -0.631 3.558 0.730 1.00 5.59 H
HETATM 99 N OMY A 6 -0.841 5.066 4.156 1.00 3.29 N
HETATM 100 CA OMY A 6 0.153 4.642 5.068 1.00 3.77 C
HETATM 101 OCZ OMY A 6 0.644 10.625 4.037 1.00 4.40 O
HETATM 102 CE2 OMY A 6 -0.746 8.966 5.056 1.00 3.69 C
HETATM 103 CE1 OMY A 6 1.622 8.643 5.053 1.00 4.14 C
HETATM 104 CZ OMY A 6 0.519 9.416 4.702 1.00 3.74 C
HETATM 105 CG OMY A 6 0.211 6.945 5.959 1.00 3.36 C
HETATM 106 CD2 OMY A 6 -0.899 7.756 5.699 1.00 3.72 C
HETATM 107 CD1 OMY A 6 1.487 7.428 5.657 1.00 3.69 C
HETATM 108 CB OMY A 6 0.072 5.496 6.406 1.00 3.80 C
HETATM 109 CL OMY A 6 3.250 9.214 4.691 1.00 5.21 CL
HETATM 110 O OMY A 6 -0.998 2.532 5.187 1.00 4.67 O
HETATM 111 C OMY A 6 0.071 3.128 5.320 1.00 3.55 C
HETATM 112 ODE OMY A 6 -1.150 5.269 7.029 1.00 4.48 O
HETATM 113 HN1 OMY A 6 -1.648 5.066 4.453 1.00 4.94 H
HETATM 114 HA OMY A 6 1.024 4.823 4.657 1.00 5.65 H
HETATM 115 HE2 OMY A 6 -1.493 9.483 4.859 1.00 5.54 H
HETATM 116 HD2 OMY A 6 -1.747 7.477 5.961 1.00 5.59 H
HETATM 117 HD1 OMY A 6 2.240 6.923 5.867 1.00 5.54 H
HETATM 118 HB OMY A 6 0.808 5.255 7.006 1.00 5.70 H
HETATM 119 HDE OMY A 6 -1.198 4.483 7.258 1.00 6.72 H
HETATM 120 N 3FG A 7 1.230 2.520 5.592 1.00 3.81 N
HETATM 121 OD1 3FG A 7 4.706 1.291 1.808 1.00 4.00 O
HETATM 122 CD1 3FG A 7 4.329 0.915 3.056 1.00 3.61 C
HETATM 123 CG1 3FG A 7 3.042 1.139 3.548 1.00 3.76 C
HETATM 124 CZ 3FG A 7 5.301 0.282 3.852 1.00 3.74 C
HETATM 125 CD2 3FG A 7 5.003 -0.095 5.140 1.00 4.28 C
HETATM 126 OD2 3FG A 7 5.881 -0.668 5.984 1.00 4.72 O
HETATM 127 CG2 3FG A 7 3.708 0.139 5.646 1.00 4.51 C
HETATM 128 CB 3FG A 7 2.747 0.764 4.868 1.00 4.06 C
HETATM 129 CA 3FG A 7 1.363 1.079 5.448 1.00 4.59 C
HETATM 130 C 3FG A 7 1.094 0.328 6.804 1.00 5.39 C
HETATM 131 O 3FG A 7 0.845 -0.905 6.648 1.00 7.22 O
HETATM 132 OXT 3FG A 7 1.168 0.946 7.841 1.00 6.41 O
HETATM 133 HN1 3FG A 7 1.904 2.986 5.854 1.00 5.72 H
HETATM 134 HA 3FG A 7 0.691 0.779 4.801 1.00 6.88 H
HETATM 135 HD1 3FG A 7 4.075 1.650 1.428 1.00 5.99 H
HETATM 136 HZ 3FG A 7 6.148 0.117 3.505 1.00 5.61 H
HETATM 137 HD2 3FG A 7 6.605 -0.752 5.609 1.00 7.09 H
HETATM 138 HG2 3FG A 7 3.497 -0.129 6.511 1.00 6.76 H
HETATM 139 HOT 3FG A 7 1.007 0.445 8.470 1.00 9.61 H
TER 140 3FG A 7
HETATM 141 N MLU B 1 -13.037 5.891 5.853 1.00 5.04 N
HETATM 142 CN MLU B 1 -13.354 6.417 7.214 1.00 6.38 C
HETATM 143 CA MLU B 1 -11.668 6.227 5.337 1.00 5.10 C
HETATM 144 C MLU B 1 -10.680 5.657 6.376 1.00 5.09 C
HETATM 145 O MLU B 1 -10.897 4.548 6.863 1.00 6.24 O
HETATM 146 CB MLU B 1 -11.446 5.565 4.011 1.00 5.91 C
HETATM 147 CG MLU B 1 -12.393 6.014 2.858 1.00 7.23 C
HETATM 148 CD1 MLU B 1 -12.226 7.481 2.576 1.00 11.16 C
HETATM 149 CD2 MLU B 1 -12.173 5.190 1.667 1.00 8.76 C
HETATM 150 H MLU B 1 -13.719 6.252 5.204 1.00 7.56 H
HETATM 151 HCN1 MLU B 1 -14.244 6.153 7.459 1.00 9.57 H
HETATM 152 HCN2 MLU B 1 -13.294 7.375 7.209 1.00 9.57 H
HETATM 153 HCN3 MLU B 1 -12.728 6.060 7.849 1.00 9.57 H
HETATM 154 HA MLU B 1 -11.560 7.197 5.259 1.00 7.65 H
HETATM 155 HB2 MLU B 1 -11.542 4.607 4.129 1.00 8.86 H
HETATM 156 HB3 MLU B 1 -10.531 5.734 3.736 1.00 8.86 H
HETATM 157 HG MLU B 1 -13.316 5.869 3.156 1.00 10.84 H
HETATM 158 HD11 MLU B 1 -12.378 7.981 3.381 1.00 16.75 H
HETATM 159 HD12 MLU B 1 -12.857 7.752 1.906 1.00 16.75 H
HETATM 160 HD13 MLU B 1 -11.334 7.646 2.261 1.00 16.75 H
HETATM 161 HD21 MLU B 1 -12.287 4.264 1.893 1.00 13.15 H
HETATM 162 HD22 MLU B 1 -11.281 5.332 1.340 1.00 13.15 H
HETATM 163 HD23 MLU B 1 -12.805 5.434 0.988 1.00 13.15 H
HETATM 164 HN22 MLU B 1 -13.135 4.887 5.868 1.00 7.56 H
HETATM 165 N OMZ B 2 -9.595 6.386 6.606 1.00 5.26 N
HETATM 166 CA OMZ B 2 -8.669 5.974 7.643 1.00 5.29 C
HETATM 167 C OMZ B 2 -7.321 5.484 7.113 1.00 4.79 C
HETATM 168 O OMZ B 2 -6.505 5.032 7.901 1.00 5.81 O
HETATM 169 CB OMZ B 2 -8.491 7.054 8.771 1.00 5.92 C
HETATM 170 OC OMZ B 2 -9.827 7.384 9.115 1.00 8.05 O
HETATM 171 CG OMZ B 2 -7.687 8.239 8.256 1.00 4.93 C
HETATM 172 CD1 OMZ B 2 -6.305 8.231 8.391 1.00 4.58 C
HETATM 173 CD2 OMZ B 2 -8.286 9.252 7.515 1.00 5.99 C
HETATM 174 CE1 OMZ B 2 -5.540 9.185 7.786 1.00 4.14 C
HETATM 175 CL OMZ B 2 -3.792 9.156 7.959 1.00 5.10 CL
HETATM 176 CE2 OMZ B 2 -7.501 10.204 6.908 1.00 5.39 C
HETATM 177 CZ OMZ B 2 -6.125 10.166 6.999 1.00 4.63 C
HETATM 178 OH OMZ B 2 -5.357 11.066 6.297 1.00 5.00 O
HETATM 179 H OMZ B 2 -9.442 7.096 6.145 1.00 7.88 H
HETATM 180 HA OMZ B 2 -9.083 5.200 8.078 1.00 7.93 H
HETATM 181 HB OMZ B 2 -8.037 6.656 9.543 1.00 8.88 H
HETATM 182 HC OMZ B 2 -10.213 6.713 9.385 1.00 12.07 H
HETATM 183 HD1 OMZ B 2 -5.896 7.568 8.899 1.00 6.87 H
HETATM 184 HD2 OMZ B 2 -9.212 9.286 7.431 1.00 8.98 H
HETATM 185 HE2 OMZ B 2 -7.906 10.889 6.426 1.00 8.08 H
ATOM 186 N ASN B 3 -7.112 5.548 5.815 1.00 4.70 N
ATOM 187 CA ASN B 3 -5.998 4.818 5.152 1.00 4.69 C
ATOM 188 C ASN B 3 -4.911 5.737 4.594 1.00 3.75 C
ATOM 189 O ASN B 3 -3.748 5.590 4.929 1.00 5.25 O
ATOM 190 CB AASN B 3 -6.618 3.973 4.021 0.60 5.86 C
ATOM 191 CB BASN B 3 -6.439 3.686 4.239 0.40 6.85 C
ATOM 192 CG AASN B 3 -7.785 3.135 4.507 0.60 6.92 C
ATOM 193 CG BASN B 3 -7.228 2.556 4.920 0.40 7.29 C
ATOM 194 OD1AASN B 3 -8.787 2.996 3.707 0.60 11.27 O
ATOM 195 OD1BASN B 3 -8.256 2.171 4.369 0.40 9.96 O
ATOM 196 ND2AASN B 3 -7.794 2.711 5.722 0.60 9.13 N
ATOM 197 ND2BASN B 3 -6.706 2.147 6.060 0.40 9.42 N
ATOM 198 H ASN B 3 -7.638 6.029 5.334 1.00 7.05 H
ATOM 199 HA ASN B 3 -5.590 4.213 5.805 1.00 7.03 H
ATOM 200 HB2AASN B 3 -6.922 4.562 3.313 0.60 8.79 H
ATOM 201 HB2BASN B 3 -6.988 4.058 3.531 0.40 10.28 H
ATOM 202 HB3AASN B 3 -5.939 3.388 3.651 0.60 8.79 H
ATOM 203 HB3BASN B 3 -5.651 3.302 3.824 0.40 10.28 H
ATOM 204 HD21AASN B 3 -7.104 2.825 6.222 0.60 13.69 H
ATOM 205 HD21BASN B 3 -5.974 2.495 6.347 0.40 14.12 H
ATOM 206 HD22AASN B 3 -8.490 2.314 6.034 0.60 13.69 H
ATOM 207 HD22BASN B 3 -7.099 1.532 6.516 0.40 14.12 H
HETATM 208 N GHP B 4 -5.305 6.651 3.696 1.00 3.84 N
HETATM 209 CA GHP B 4 -4.357 7.502 2.979 1.00 3.48 C
HETATM 210 C GHP B 4 -4.675 7.472 1.489 1.00 3.52 C
HETATM 211 O GHP B 4 -5.801 7.694 1.080 1.00 4.85 O
HETATM 212 C1 GHP B 4 -4.356 8.956 3.449 1.00 3.69 C
HETATM 213 C2 GHP B 4 -3.777 9.919 2.663 1.00 4.55 C
HETATM 214 C3 GHP B 4 -3.797 11.247 3.031 1.00 5.64 C
HETATM 215 C4 GHP B 4 -4.341 11.623 4.272 1.00 5.87 C
HETATM 216 O4 AGHP B 4 -4.460 12.901 4.633 0.65 4.65 O
HETATM 217 O4 BGHP B 4 -3.814 12.998 4.725 0.35 4.47 O
HETATM 218 C5 GHP B 4 -4.877 10.637 5.059 1.00 4.39 C
HETATM 219 C6 GHP B 4 -4.907 9.320 4.661 1.00 4.12 C
HETATM 220 H GHP B 4 -6.145 6.741 3.537 1.00 5.76 H
HETATM 221 HA GHP B 4 -3.457 7.136 3.109 1.00 5.23 H
HETATM 222 HC2 GHP B 4 -3.363 9.671 1.868 1.00 6.82 H
HETATM 223 H6 GHP B 4 -5.297 8.677 5.207 1.00 6.17 H
HETATM 224 N GHP B 5 -3.610 7.273 0.699 1.00 3.52 N
HETATM 225 CA GHP B 5 -3.568 7.559 -0.722 1.00 3.83 C
HETATM 226 C GHP B 5 -2.155 8.154 -0.982 1.00 3.65 C
HETATM 227 O GHP B 5 -1.274 7.960 -0.146 1.00 3.88 O
HETATM 228 C1 GHP B 5 -3.685 6.352 -1.651 1.00 4.26 C
HETATM 229 C2 GHP B 5 -4.596 6.395 -2.683 1.00 4.68 C
HETATM 230 C3 GHP B 5 -4.575 5.431 -3.710 1.00 5.25 C
HETATM 231 C4 GHP B 5 -3.674 4.397 -3.602 1.00 5.55 C
HETATM 232 O4 GHP B 5 -3.656 3.446 -4.610 1.00 6.82 O
HETATM 233 C5 GHP B 5 -2.786 4.305 -2.548 1.00 5.11 C
HETATM 234 C6 GHP B 5 -2.804 5.296 -1.570 1.00 4.56 C
HETATM 235 H GHP B 5 -2.899 6.953 1.062 1.00 5.28 H
HETATM 236 HA GHP B 5 -4.254 8.220 -0.948 1.00 5.74 H
HETATM 237 HC2 GHP B 5 -5.235 7.071 -2.703 1.00 7.02 H
HETATM 238 HO4 GHP B 5 -3.085 2.881 -4.443 1.00 10.23 H
HETATM 239 H5 GHP B 5 -2.189 3.594 -2.491 1.00 7.67 H
HETATM 240 H6 GHP B 5 -2.213 5.245 -0.854 1.00 6.84 H
HETATM 241 N OMY B 6 -1.902 8.752 -2.152 1.00 3.61 N
HETATM 242 CA OMY B 6 -2.859 9.265 -3.103 1.00 4.09 C
HETATM 243 OCZ OMY B 6 -3.270 12.255 2.245 1.00 6.82 O
HETATM 244 CE2 OMY B 6 -1.886 11.848 0.322 1.00 5.30 C
HETATM 245 CE1 OMY B 6 -4.262 11.822 0.098 1.00 5.65 C
HETATM 246 CZ OMY B 6 -3.160 11.966 0.892 1.00 5.35 C
HETATM 247 CG OMY B 6 -2.897 11.345 -1.809 1.00 4.60 C
HETATM 248 CD2 OMY B 6 -1.763 11.540 -0.991 1.00 4.49 C
HETATM 249 CD1 OMY B 6 -4.142 11.521 -1.240 1.00 5.22 C
HETATM 250 CB OMY B 6 -2.749 10.819 -3.210 1.00 4.50 C
HETATM 251 CL OMY B 6 -5.874 11.966 0.776 1.00 8.09 CL
HETATM 252 O OMY B 6 -1.604 8.141 -4.814 1.00 3.95 O
HETATM 253 C OMY B 6 -2.725 8.504 -4.422 1.00 3.87 C
HETATM 254 ODE OMY B 6 -1.529 11.143 -3.827 1.00 4.63 O
HETATM 255 HN1 OMY B 6 -1.073 8.840 -2.362 1.00 5.41 H
HETATM 256 HA OMY B 6 -3.750 9.065 -2.748 1.00 6.13 H
HETATM 257 HE2 OMY B 6 -1.128 11.980 0.844 1.00 7.95 H
HETATM 258 HD2 OMY B 6 -0.914 11.456 -1.362 1.00 6.73 H
HETATM 259 HD1 OMY B 6 -4.905 11.435 -1.764 1.00 7.83 H
HETATM 260 HB OMY B 6 -3.487 11.157 -3.760 1.00 6.75 H
HETATM 261 HDE OMY B 6 -1.070 11.583 -3.309 1.00 6.94 H
HETATM 262 N 3FG B 7 -3.857 8.190 -5.027 1.00 4.82 N
HETATM 263 OD1 3FG B 7 -6.947 4.049 -3.745 1.00 9.28 O
HETATM 264 CD1 3FG B 7 -6.762 4.900 -4.778 1.00 7.28 C
HETATM 265 CG1 3FG B 7 -5.537 5.580 -4.858 1.00 6.07 C
HETATM 266 CZ 3FG B 7 -7.697 5.012 -5.788 1.00 9.18 C
HETATM 267 CD2 3FG B 7 -7.456 5.863 -6.892 1.00 8.94 C
HETATM 268 OD2 3FG B 7 -8.360 6.001 -7.860 1.00 11.87 O
HETATM 269 CG2 3FG B 7 -6.235 6.540 -6.918 1.00 7.85 C
HETATM 270 CB 3FG B 7 -5.290 6.418 -5.928 1.00 6.28 C
HETATM 271 CA 3FG B 7 -3.950 7.169 -6.078 1.00 6.39 C
HETATM 272 C 3FG B 7 -3.708 7.803 -7.496 1.00 9.14 C
HETATM 273 O 3FG B 7 -3.359 7.033 -8.352 1.00 12.46 O
HETATM 274 OXT 3FG B 7 -3.957 8.963 -7.662 1.00 13.92 O
HETATM 275 HN1 3FG B 7 -4.574 8.603 -4.794 1.00 7.23 H
HETATM 276 HA 3FG B 7 -3.231 6.521 -5.920 1.00 9.58 H
HETATM 277 HD1 3FG B 7 -7.661 3.657 -3.838 1.00 13.92 H
HETATM 278 HZ 3FG B 7 -8.488 4.525 -5.743 1.00 13.77 H
HETATM 279 HD2 3FG B 7 -9.014 5.537 -7.691 1.00 17.81 H
HETATM 280 HG2 3FG B 7 -6.054 7.100 -7.638 1.00 11.77 H
HETATM 281 HOT 3FG B 7 -3.789 9.170 -8.438 1.00 20.89 H
TER 282 3FG B 7
HETATM 283 C2 BGC A 8 0.764 14.592 4.282 1.00 7.74 C
HETATM 284 C3 BGC A 8 -0.486 15.382 4.561 1.00 9.84 C
HETATM 285 C4 BGC A 8 -0.969 15.992 3.213 1.00 9.80 C
HETATM 286 C5 BGC A 8 -1.043 14.883 2.149 1.00 9.23 C
HETATM 287 C6 BGC A 8 -1.348 15.417 0.692 1.00 11.48 C
HETATM 288 C1 BGC A 8 0.571 13.575 3.231 1.00 6.08 C
HETATM 289 O2 BGC A 8 1.176 13.981 5.521 1.00 8.35 O
HETATM 290 O3 BGC A 8 -0.274 16.407 5.506 1.00 14.77 O
HETATM 291 O4 BGC A 8 -2.284 16.523 3.362 1.00 14.63 O
HETATM 292 O5 BGC A 8 0.194 14.213 2.047 1.00 6.86 O
HETATM 293 O6 BGC A 8 -0.508 16.424 0.309 1.00 13.77 O
HETATM 294 H2 BGC A 8 1.466 15.211 3.992 1.00 11.61 H
HETATM 295 H3 BGC A 8 -1.177 14.775 4.901 1.00 14.76 H
HETATM 296 H4 BGC A 8 -0.353 16.696 2.922 1.00 14.70 H
HETATM 297 H5 BGC A 8 -1.736 14.239 2.405 1.00 13.85 H
HETATM 298 H6C1 BGC A 8 -1.267 14.682 0.063 1.00 17.22 H
HETATM 299 H6C2 BGC A 8 -2.262 15.738 0.657 1.00 17.22 H
HETATM 300 H1 BGC A 8 -0.119 12.935 3.504 1.00 9.12 H
HETATM 301 HC BGC A 8 -0.976 16.814 5.630 1.00 22.15 H
HETATM 302 HD BGC A 8 -2.797 16.130 2.856 1.00 21.95 H
HETATM 303 H6 BGC A 8 0.266 16.153 0.320 1.00 20.66 H
HETATM 304 C1 RER A 9 2.253 14.596 6.183 1.00 9.59 C
HETATM 305 C2 RER A 9 2.244 14.030 7.577 1.00 9.69 C
HETATM 306 C3 RER A 9 2.888 12.659 7.642 1.00 8.09 C
HETATM 307 N3 RER A 9 3.219 12.389 9.093 1.00 10.96 N
HETATM 308 C3A RER A 9 1.970 11.543 7.234 1.00 7.94 C
HETATM 309 C4 RER A 9 4.193 12.609 6.834 1.00 10.01 C
HETATM 310 O4 ARER A 9 5.008 13.627 7.569 0.75 9.20 O
HETATM 311 O4 BRER A 9 5.783 12.692 6.936 0.25 6.43 O
HETATM 312 C5 RER A 9 3.916 13.074 5.409 1.00 9.45 C
HETATM 313 O5 RER A 9 3.432 14.412 5.431 1.00 11.21 O
HETATM 314 C5A RER A 9 5.169 13.066 4.519 1.00 12.46 C
HETATM 315 H1 RER A 9 2.071 15.557 6.240 1.00 14.39 H
HETATM 316 H21C RER A 9 1.328 13.967 7.890 1.00 14.54 H
HETATM 317 H22C RER A 9 2.720 14.634 8.169 1.00 14.54 H
HETATM 318 H31N RER A 9 3.840 13.106 9.436 1.00 16.44 H
HETATM 319 H32N RER A 9 3.668 11.489 9.174 1.00 16.44 H
HETATM 320 H3A1 RER A 9 2.436 10.706 7.295 1.00 11.91 H
HETATM 321 H3A2 RER A 9 1.679 11.683 6.330 1.00 11.91 H
HETATM 322 H3A3 RER A 9 1.207 11.527 7.817 1.00 11.91 H
HETATM 323 H4 RER A 9 4.606 11.720 6.857 1.00 15.01 H
HETATM 324 HO4ARER A 9 5.165 14.261 7.073 0.75 13.80 H
HETATM 325 H5 RER A 9 3.236 12.493 5.009 1.00 14.17 H
HETATM 326 H5A1 RER A 9 4.938 13.366 3.637 1.00 18.69 H
HETATM 327 H5A2 RER A 9 5.522 12.174 4.471 1.00 18.69 H
HETATM 328 H5A3 RER A 9 5.831 13.652 4.893 1.00 18.69 H
HETATM 329 H33N RER A 9 2.369 12.391 9.638 1.00 16.44 H
HETATM 330 C ACY A 11 -8.682 8.170 3.803 1.00 8.68 C
HETATM 331 O ACY A 11 -9.467 8.524 4.783 1.00 8.11 O
HETATM 332 OXT ACY A 11 -8.192 7.009 3.580 1.00 8.10 O
HETATM 333 CH3 ACY A 11 -8.402 9.294 2.821 1.00 10.76 C
HETATM 334 HXT ACY A 11 -7.757 7.025 2.885 1.00 12.15 H
HETATM 335 H1 ACY A 11 -8.833 10.097 3.122 1.00 16.14 H
HETATM 336 H2 ACY A 11 -8.742 9.054 1.955 1.00 16.14 H
HETATM 337 H3 ACY A 11 -7.455 9.441 2.763 1.00 16.14 H
HETATM 338 CL CL A 21 3.772 4.414 5.678 1.00 4.90 CL
HETATM 339 CL CL A 22 9.011 11.897 -1.620 1.00 15.43 CL
HETATM 340 C2 ABGC B 8 -5.444 14.877 5.441 0.65 5.75 C
HETATM 341 C2 BBGC B 8 -4.605 15.143 5.446 0.35 4.66 C
HETATM 342 C3 ABGC B 8 -6.625 15.843 5.344 0.65 6.50 C
HETATM 343 C3 BBGC B 8 -5.634 16.259 5.314 0.35 6.06 C
HETATM 344 C4 ABGC B 8 -7.297 15.837 3.946 0.65 7.51 C
HETATM 345 C4 BBGC B 8 -5.800 16.589 3.805 0.35 6.67 C
HETATM 346 C5 ABGC B 8 -7.560 14.369 3.548 0.65 7.16 C
HETATM 347 C5 BBGC B 8 -6.014 15.272 3.038 0.35 7.02 C
HETATM 348 C6 ABGC B 8 -8.196 14.218 2.171 0.65 8.25 C
HETATM 349 C6 BBGC B 8 -6.076 15.455 1.490 0.35 8.31 C
HETATM 350 C1 ABGC B 8 -5.708 13.550 4.772 0.65 5.31 C
HETATM 351 C1 BBGC B 8 -4.899 13.949 4.629 0.35 4.64 C
HETATM 352 O2 ABGC B 8 -5.218 14.611 6.884 0.65 5.73 O
HETATM 353 O2 BBGC B 8 -4.748 14.678 6.848 0.35 6.88 O
HETATM 354 O3 ABGC B 8 -6.169 17.164 5.691 0.65 7.80 O
HETATM 355 O3 BBGC B 8 -5.194 17.453 5.972 0.35 5.44 O
HETATM 356 O4 ABGC B 8 -8.522 16.551 3.978 0.65 8.67 O
HETATM 357 O4 BBGC B 8 -6.890 17.487 3.615 0.35 8.05 O
HETATM 358 O5 ABGC B 8 -6.269 13.728 3.477 0.65 6.21 O
HETATM 359 O5 BBGC B 8 -5.014 14.325 3.286 0.35 5.89 O
HETATM 360 O6 ABGC B 8 -8.659 12.909 1.885 0.65 9.56 O
HETATM 361 O6 BBGC B 8 -7.352 15.405 0.998 0.35 11.56 O
HETATM 362 H2 ABGC B 8 -4.646 15.291 5.051 0.65 8.63 H
HETATM 363 H2 BBGC B 8 -3.699 15.475 5.275 0.35 6.99 H
HETATM 364 H3 ABGC B 8 -7.295 15.570 6.005 0.65 9.75 H
HETATM 365 H3 BBGC B 8 -6.492 15.968 5.688 0.35 9.09 H
HETATM 366 H4 ABGC B 8 -6.695 16.250 3.293 0.65 11.27 H
HETATM 367 H4 BBGC B 8 -4.978 17.014 3.481 0.35 10.01 H
HETATM 368 H5 ABGC B 8 -8.116 13.931 4.225 0.65 10.73 H
HETATM 369 H5 BBGC B 8 -6.868 14.890 3.330 0.35 10.54 H
HETATM 370 H6C1ABGC B 8 -8.942 14.834 2.104 0.65 12.37 H
HETATM 371 H6C1BBGC B 8 -5.681 16.310 1.257 0.35 12.47 H
HETATM 372 H6C2ABGC B 8 -7.544 14.471 1.498 0.65 12.37 H
HETATM 373 H6C2BBGC B 8 -5.547 14.760 1.068 0.35 12.47 H
HETATM 374 H1 ABGC B 8 -6.308 13.008 5.326 0.65 7.97 H
HETATM 375 H1 BBGC B 8 -5.734 13.535 4.932 0.35 6.96 H
HETATM 376 HC ABGC B 8 -5.369 17.139 5.870 0.65 11.69 H
HETATM 377 HC BBGC B 8 -4.456 17.324 6.307 0.35 8.17 H
HETATM 378 HD ABGC B 8 -8.379 17.329 4.192 0.65 13.01 H
HETATM 379 HD BBGC B 8 -7.449 17.140 3.126 0.35 12.07 H
HETATM 380 H6 ABGC B 8 -9.223 12.692 2.439 0.65 14.33 H
HETATM 381 H6 BBGC B 8 -7.687 14.678 1.180 0.35 17.35 H
HETATM 382 C1 RER B 9 -3.993 15.083 7.536 1.00 6.39 C
HETATM 383 C2 RER B 9 -4.225 14.998 9.051 1.00 5.32 C
HETATM 384 C3 RER B 9 -4.202 13.554 9.555 1.00 3.95 C
HETATM 385 N3 RER B 9 -4.131 13.585 11.068 1.00 3.87 N
HETATM 386 C3A RER B 9 -5.455 12.798 9.212 1.00 4.08 C
HETATM 387 C4 RER B 9 -2.921 12.865 9.057 1.00 4.45 C
HETATM 388 O4 RER B 9 -1.811 13.523 9.711 1.00 6.16 O
HETATM 389 C5 RER B 9 -2.851 12.990 7.558 1.00 5.60 C
HETATM 390 O5 RER B 9 -2.788 14.378 7.184 1.00 7.05 O
HETATM 391 C5A RER B 9 -1.609 12.318 6.948 1.00 7.02 C
HETATM 392 H1 RER B 9 -3.870 16.027 7.302 1.00 9.59 H
HETATM 393 H21C RER B 9 -3.537 15.506 9.509 1.00 7.97 H
HETATM 394 H22C RER B 9 -5.083 15.397 9.265 1.00 7.97 H
HETATM 395 H31N RER B 9 -3.303 14.085 11.355 1.00 5.80 H
HETATM 396 H32N RER B 9 -4.094 12.641 11.422 1.00 5.80 H
HETATM 397 H3A1 RER B 9 -5.390 11.901 9.548 1.00 6.12 H
HETATM 398 H3A2 RER B 9 -5.563 12.775 8.258 1.00 6.12 H
HETATM 399 H3A3 RER B 9 -6.211 13.235 9.609 1.00 6.12 H
HETATM 400 H4 RER B 9 -2.937 11.918 9.309 1.00 6.68 H
HETATM 401 HO4 RER B 9 -1.322 13.860 9.145 1.00 9.23 H
HETATM 402 H5 RER B 9 -3.655 12.589 7.166 1.00 8.40 H
HETATM 403 H5A1 RER B 9 -1.620 12.432 5.995 1.00 10.53 H
HETATM 404 H5A2 RER B 9 -1.615 11.382 7.159 1.00 10.53 H
HETATM 405 H5A3 RER B 9 -0.817 12.722 7.309 1.00 10.53 H
HETATM 406 H33N RER B 9 -4.948 14.050 11.434 1.00 5.80 H
HETATM 407 CL CL B 21 0.233 11.355 10.432 1.00 8.59 CL
HETATM 408 CL CL B 22 -6.403 9.546 -3.590 1.00 10.91 CL
HETATM 409 O HOH A2001 10.417 7.090 -6.145 1.00 6.93 O
HETATM 410 O HOH A2002 12.665 8.554 -2.847 1.00 15.18 O
HETATM 411 O HOH A2003 11.451 10.734 -0.616 0.50 16.23 O
HETATM 412 O AHOH A2004 13.830 7.936 -0.582 0.60 14.38 O
HETATM 413 O HOH A2005 10.346 13.790 -3.403 1.00 17.62 O
HETATM 414 O BHOH A2006 6.635 14.659 1.643 0.40 14.41 O
HETATM 415 O HOH A2007 16.555 8.475 -0.761 1.00 19.31 O
HETATM 416 O AHOH A2008 15.524 10.561 -0.050 0.75 36.40 O
HETATM 417 O AHOH A2009 3.712 15.326 1.972 0.50 11.19 O
HETATM 418 O HOH A2010 8.212 12.107 -6.577 1.00 11.27 O
HETATM 419 O HOH A2011 9.456 14.922 -5.741 1.00 15.32 O
HETATM 420 O HOH A2012 8.938 14.484 4.905 1.00 28.63 O
HETATM 421 O HOH A2013 1.473 13.449 12.511 1.00 27.55 O
HETATM 422 O HOH A2014 -9.637 6.869 -0.805 1.00 22.19 O
HETATM 423 O HOH A2015 3.654 3.654 0.000 0.50 5.50 O
HETATM 424 O HOH A2016 -0.877 -1.750 1.076 1.00 20.10 O
HETATM 425 O HOH A2017 -3.773 3.945 1.813 1.00 9.48 O
HETATM 426 O HOH A2018 -3.207 2.082 3.544 1.00 16.72 O
HETATM 427 O HOH A2019 -0.494 3.106 8.613 1.00 11.64 O
HETATM 428 O HOH A2020 -3.373 2.289 7.656 1.00 34.34 O
HETATM 429 O HOH A2021 3.491 2.594 8.358 1.00 8.13 O
HETATM 430 O HOH A2022 0.549 -0.228 10.244 1.00 29.25 O
HETATM 431 O HOH A2023 1.540 -2.438 8.544 1.00 32.06 O
HETATM 432 O HOH A2024 5.429 0.496 8.809 1.00 14.56 O
HETATM 433 O BHOH A2025 2.241 15.953 0.508 0.50 18.35 O
HETATM 434 O HOH A2026 -0.593 15.929 8.212 1.00 16.34 O
HETATM 435 O HOH A2027 1.341 18.561 5.356 1.00 39.60 O
HETATM 436 O BHOH A2028 -1.312 18.356 8.327 0.35 11.09 O
HETATM 437 O HOH A2029 4.268 16.936 4.102 1.00 28.28 O
HETATM 438 O HOH A2030 4.416 14.384 10.863 1.00 21.72 O
HETATM 439 O BHOH A2031 5.300 16.353 7.013 0.25 12.05 O
HETATM 440 O HOH A2032 7.573 12.947 7.195 0.75 20.91 O
HETATM 441 O HOH A2033 -8.440 5.488 1.203 1.00 16.16 O
HETATM 442 O HOH A2034 -10.841 10.620 5.415 1.00 15.08 O
HETATM 443 O HOH B2001 -3.773 5.132 7.999 1.00 9.00 O
HETATM 444 O HOH B2002 -5.562 1.335 6.774 0.60 17.55 O
HETATM 445 O HOH B2003 -9.246 2.967 1.683 0.40 11.71 O
HETATM 446 O BHOH B2004 -12.697 10.706 1.222 0.25 16.11 O
HETATM 447 O HOH B2005 -6.082 4.128 0.565 1.00 19.13 O
HETATM 448 O HOH B2006 -7.462 8.745 -0.866 1.00 16.52 O
HETATM 449 O HOH B2007 -2.114 1.285 -4.249 1.00 7.58 O
HETATM 450 O HOH B2008 -3.640 3.703 -7.448 1.00 28.59 O
HETATM 451 O HOH B2009 -1.773 13.861 -4.043 1.00 14.47 O
HETATM 452 O HOH B2010 -9.348 2.814 -3.507 1.00 19.01 O
HETATM 453 O AHOH B2011 -10.688 4.334 -7.397 0.75 23.81 O
HETATM 454 O HOH B2012 -11.073 12.344 3.332 1.00 29.98 O
HETATM 455 O HOH B2013 -9.082 11.051 -0.323 1.00 23.36 O
HETATM 456 O HOH B2014 -4.975 15.780 -1.438 1.00 38.29 O
HETATM 457 O HOH B2015 -10.095 15.431 5.979 1.00 26.81 O
HETATM 458 O AHOH B2016 -2.459 18.355 7.301 0.65 19.38 O
HETATM 459 O AHOH B2017 -3.303 18.288 4.860 0.65 18.57 O
HETATM 460 O BHOH B2018 -2.515 18.448 5.944 0.35 10.01 O
HETATM 461 O AHOH B2019 -4.626 15.170 1.593 0.32 6.41 O
HETATM 462 O BHOH B2020 -5.007 15.890 1.094 0.32 13.09 O
HETATM 463 O HOH B2021 1.175 15.465 10.408 1.00 30.89 O
CONECT 1 2 3 12
CONECT 2 1 13 14 15
CONECT 3 1 4 6 16
CONECT 4 3 5 32
CONECT 5 4
CONECT 6 3 7 17 18
CONECT 7 6 8 9 10
CONECT 7 11 19
CONECT 8 7 20 22 24
CONECT 9 7 21 23
CONECT 10 7 25 27 29
CONECT 11 7 26 28 30
CONECT 12 1
CONECT 13 2
CONECT 14 2
CONECT 15 2
CONECT 16 3
CONECT 17 6
CONECT 18 6
CONECT 19 7
CONECT 20 8
CONECT 21 9
CONECT 22 8
CONECT 23 9
CONECT 24 8
CONECT 25 10
CONECT 26 11
CONECT 27 10
CONECT 28 11
CONECT 29 10
CONECT 30 11
CONECT 32 4 33 46
CONECT 33 32 34 36 47
CONECT 34 33 35 53
CONECT 35 34
CONECT 36 33 37 38 48
CONECT 37 36 49
CONECT 38 36 39 40
CONECT 39 38 41 50
CONECT 40 38 43 51
CONECT 41 39 42 44
CONECT 42 41
CONECT 43 40 44 52
CONECT 44 41 43 45
CONECT 45 44 76
CONECT 46 32
CONECT 47 33
CONECT 48 36
CONECT 49 37
CONECT 50 39
CONECT 51 40
CONECT 52 43
CONECT 53 34
CONECT 55 67
CONECT 67 55 68 78
CONECT 68 67 69 71 79
CONECT 69 68 70 82
CONECT 70 69
CONECT 71 68 72 77
CONECT 72 71 73 80
CONECT 73 72 74 101
CONECT 74 73 75 76
CONECT 75 74 288
CONECT 76 45 74 77
CONECT 77 71 76 81
CONECT 78 67
CONECT 79 68
CONECT 80 72
CONECT 81 77
CONECT 82 69 83 93
CONECT 83 82 84 86 94
CONECT 84 83 85 99
CONECT 85 84