HEADER HYDROLASE/ANTIBIOTIC 08-JUN-04 1TK2
TITLE CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN ALKALINE PROTEINASE
TITLE 2 SAVINASE AND GRAMICIDIN S AT 1.5A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN SAVINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALKALINE PROTEASE;
COMPND 5 EC: 3.4.21.62;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: GRAMICIDIN S;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: GRAMICIDIN SOVIET;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LENTUS;
SOURCE 3 ORGANISM_TAXID: 1467;
SOURCE 4 MOL_ID: 2;
SOURCE 5 SYNTHETIC: YES;
SOURCE 6 ORGANISM_SCIENTIFIC: BREVIBACILLUS BREVIS;
SOURCE 7 ORGANISM_TAXID: 1393
KEYWDS GRAMICIDIN, ANTIBIOTIC, ANTIFUNGAL, ANTIBACTERIAL, CYCLIC GRAMICIDIN,
KEYWDS 2 MEMBRANE ION CHANNEL, HYDROLASE-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR V.S.BHATT,P.KAUR,S.KLUPSCH,C.BETZEL,S.BRENNER,T.P.SINGH
REVDAT 5 23-AUG-23 1TK2 1 REMARK LINK
REVDAT 4 27-JUL-11 1TK2 1 REMARK
REVDAT 3 13-JUL-11 1TK2 1 VERSN
REVDAT 2 24-FEB-09 1TK2 1 VERSN
REVDAT 1 22-JUN-04 1TK2 0
JRNL AUTH V.S.BHATT,P.KAUR,S.KLUPSCH,C.BETZEL,S.BRENNER,T.P.SINGH
JRNL TITL CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN ALKALINE
JRNL TITL 2 PROTEINASE SAVINASE AND GRAMICIDIN S AT 1.5A RESOLUTION.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 31702
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1038
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.58
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2163
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1770
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.2190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1961
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.60000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : -0.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.081
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.679
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1994 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1774 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2717 ; 1.821 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4128 ; 0.973 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 5.594 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 305 ;18.589 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 318 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2290 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 367 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 445 ; 0.368 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1644 ; 0.220 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2 ; 0.102 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 143 ; 0.146 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 14 ; 0.267 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 22 ; 0.327 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.200 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1369 ; 1.010 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2167 ; 1.922 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 625 ; 3.107 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 550 ; 4.805 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1TK2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022707.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-91
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.009
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : OSCILLATION CAMERA
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31702
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1SVN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.33M NACL, 10% PEG 4000, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 38.12500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 20.44500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.67000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 20.44500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.12500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.67000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: THE BIOLOGICAL UNIT IS MONOMER
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400
REMARK 400 COMPOUND
REMARK 400 GRAMICIDIN S IS A CYCLODECAPEPTIDE, CONSTRUCTED AS TWO
REMARK 400 IDENTICAL PENTAPEPTIDES JOINED HEAD TO TAIL, PRODUCED BY
REMARK 400 THE GRAM POSITIVE BACTERIUM BACILLUS BREVIS
REMARK 400 HERE, GRAMICIDIN S IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400 THE GRAMICIDIN S IS CYCLIC PEPTIDE, A MEMBER OF ANTIBIOTIC CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: GRAMICIDIN S
REMARK 400 CHAIN: B
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: GRAMICIDIN S IS A DECAPEPTIDE, RESIDUES 1 AND 10
REMARK 400 FORM A PEPTIDE BOND RESULTING IN CYCLIZATION.
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 DPN B 9 CB DPN B 9 CG -0.118
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 LEU B 3 CB - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 LEU B 3 CA - CB - CG ANGL. DEV. = -14.5 DEGREES
REMARK 500 DPN B 9 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 PRO B 10 C - N - CA ANGL. DEV. = -9.6 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 ASP A 32 -150.42 -163.08
REMARK 500 ALA A 73 24.73 -146.48
REMARK 500 ASN A 77 -150.98 -157.12
REMARK 500 VAL A 81 -161.49 -119.79
REMARK 500 THR A 213 -164.26 -128.83
REMARK 500 PRO B 5 9.86 -64.12
REMARK 500 LEU B 8 110.11 160.86
REMARK 500 DPN B 9 -178.36 58.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL B 1 ORN B 2 -148.15
REMARK 500 ORN B 7 LEU B 8 -146.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 DPN B 9 15.73
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 A1277 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 2 OE1
REMARK 620 2 ASP A 41 OD1 150.6
REMARK 620 3 ASP A 41 OD2 156.1 50.0
REMARK 620 4 LEU A 75 O 77.5 82.7 102.3
REMARK 620 5 ILE A 79 O 92.5 101.0 92.3 163.2
REMARK 620 6 VAL A 81 O 80.9 119.4 75.2 86.4 105.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1276 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 169 O
REMARK 620 2 TYR A 171 O 97.2
REMARK 620 3 ALA A 174 O 104.6 91.1
REMARK 620 4 HOH A2114 O 94.1 96.5 158.9
REMARK 620 5 HOH A2137 O 123.1 138.1 89.3 72.0
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 1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF GRAMICIDIN S
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XDC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A FROM CRYSTALS GROWN IN A LIPID
REMARK 900 CUBIC PHASE. RELATED ENTRIES
REMARK 900 RELATED ID: 1AV2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A COMPLEXED WITH CESIUM CHLORIDE
REMARK 900 RELATED ID: 1BDW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A FROM BACILLUS BREVIS
REMARK 900 RELATED ID: 1C4D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A COMPLEXED WITH CESIUM CHLORIDE
REMARK 900 RELATED ID: 1GMK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN A COMPLRXED WITH POTASSIUM
REMARK 900 THIOCYANATE
REMARK 900 RELATED ID: 1GRM RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE GRAMICIDIN A
REMARK 900 RELATED ID: 1JNO RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A IN SODIUM DODECYL SULFATE
REMARK 900 MICELLES
REMARK 900 RELATED ID: 1KQE RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF A LINKED SHORTENED GRAMICIDIN A IN BENZENE/
REMARK 900 ACETONE 10:1
REMARK 900 RELATED ID: 1MAG RELATED DB: PDB
REMARK 900 SOLID STATE NMR STRUCTURE OF GRAMICIDIN A IN HYDRATED DMPC BILAYERS,
REMARK 900 RELATED ID: 1MIC RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A IN METHANOL IN THE PRESENCE OF
REMARK 900 CACL
REMARK 900 RELATED ID: 1NG8 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A (W15G) IN SODIUM DODECYL SULFATE
REMARK 900 MICELLES
REMARK 900 RELATED ID: 1NRM RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A IN DODECYL PHOSPHOCHOLINE
REMARK 900 MICELLES
REMARK 900 RELATED ID: 1NRU RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A IN DODECYL PHOSPHOCHOLINE
REMARK 900 MICELLES IN THE PRESENCE OF EXCESS NA+
REMARK 900 RELATED ID: 1NT5 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN A (V1F) IN SODIUM DODECYL SULFATE
REMARK 900 MICELLES
REMARK 900 RELATED ID: 1JO3 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN B IN SODIUM DODECYL SULFATE
REMARK 900 MICELLES
REMARK 900 RELATED ID: 1JO4 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF GRAMICIDIN C IN SODIUM DODECYL SULFATE
REMARK 900 MICELLES
REMARK 900 RELATED ID: 1NT6 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF F1-GRAMICIDIN C IN SODIUM DODECYL SULFATE
REMARK 900 MICELLES
REMARK 900 RELATED ID: 1TKQ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF A LINKED UNSYMMETRIC GRAMICIDIN A IN A
REMARK 900 MEMBRANE-ISOELECTRICAL SOLVENTS MIXTURE, IN THE PRESENCE OF CSCL
REMARK 900 RELATED ID: 1W5U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D IN ETHANOL
REMARK 900 RELATED ID: 2IZQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D COMPLEX WITH KI IN METHANOL
REMARK 900 RELATED ID: 3L8L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D COMPLEX WITH NAI
REMARK 900 RELATED ID: 1AL4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D IN N-PROPANOL
REMARK 900 RELATED ID: 1ALX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D IN METHANOL
REMARK 900 RELATED ID: 1ALZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GRAMICIDIN D IN ETHANOL
DBREF 1TK2 A 1 269 UNP P29600 SUBS_BACLE 1 269
DBREF 1TK2 B 1 10 NOR NOR00249 NOR00249 1 10
SEQRES 1 A 269 ALA GLN SER VAL PRO TRP GLY ILE SER ARG VAL GLN ALA
SEQRES 2 A 269 PRO ALA ALA HIS ASN ARG GLY LEU THR GLY SER GLY VAL
SEQRES 3 A 269 LYS VAL ALA VAL LEU ASP THR GLY ILE SER THR HIS PRO
SEQRES 4 A 269 ASP LEU ASN ILE ARG GLY GLY ALA SER PHE VAL PRO GLY
SEQRES 5 A 269 GLU PRO SER THR GLN ASP GLY ASN GLY HIS GLY THR HIS
SEQRES 6 A 269 VAL ALA GLY THR ILE ALA ALA LEU ASN ASN SER ILE GLY
SEQRES 7 A 269 VAL LEU GLY VAL ALA PRO SER ALA GLU LEU TYR ALA VAL
SEQRES 8 A 269 LYS VAL LEU GLY ALA SER GLY SER GLY SER VAL SER SER
SEQRES 9 A 269 ILE ALA GLN GLY LEU GLU TRP ALA GLY ASN ASN GLY MET
SEQRES 10 A 269 HIS VAL ALA ASN LEU SER LEU GLY SER PRO SER PRO SER
SEQRES 11 A 269 ALA THR LEU GLU GLN ALA VAL ASN SER ALA THR SER ARG
SEQRES 12 A 269 GLY VAL LEU VAL VAL ALA ALA SER GLY ASN SER GLY ALA
SEQRES 13 A 269 GLY SER ILE SER TYR PRO ALA ARG TYR ALA ASN ALA MET
SEQRES 14 A 269 ALA VAL GLY ALA THR ASP GLN ASN ASN ASN ARG ALA SER
SEQRES 15 A 269 PHE SER GLN TYR GLY ALA GLY LEU ASP ILE VAL ALA PRO
SEQRES 16 A 269 GLY VAL ASN VAL GLN SER THR TYR PRO GLY SER THR TYR
SEQRES 17 A 269 ALA SER LEU ASN GLY THR SER MET ALA THR PRO HIS VAL
SEQRES 18 A 269 ALA GLY ALA ALA ALA LEU VAL LYS GLN LYS ASN PRO SER
SEQRES 19 A 269 TRP SER ASN VAL GLN ILE ARG ASN HIS LEU LYS ASN THR
SEQRES 20 A 269 ALA THR SER LEU GLY SER THR ASN LEU TYR GLY SER GLY
SEQRES 21 A 269 LEU VAL ASN ALA GLU ALA ALA THR ARG
SEQRES 1 B 10 VAL ORN LEU DPN PRO VAL ORN LEU DPN PRO
HET ORN B 2 8
HET DPN B 4 11
HET ORN B 7 8
HET DPN B 9 11
HET CA A1276 1
HET CA A1277 1
HETNAM ORN L-ORNITHINE
HETNAM DPN D-PHENYLALANINE
HETNAM CA CALCIUM ION
FORMUL 2 ORN 2(C5 H12 N2 O2)
FORMUL 2 DPN 2(C9 H11 N O2)
FORMUL 3 CA 2(CA 2+)
FORMUL 5 HOH *192(H2 O)
HELIX 1 1 PRO A 5 VAL A 11 1 7
HELIX 2 2 GLN A 12 ASN A 18 1 7
HELIX 3 3 GLY A 63 ALA A 74 1 12
HELIX 4 4 SER A 103 ASN A 117 1 15
HELIX 5 5 SER A 132 ARG A 145 1 14
HELIX 6 6 GLY A 219 ASN A 238 1 20
HELIX 7 7 SER A 242 THR A 253 1 12
HELIX 8 8 SER A 259 GLY A 264 1 6
HELIX 9 9 ASN A 269 THR A 274 1 6
SHEET 1 AA 7 ILE A 44 SER A 49 0
SHEET 2 AA 7 GLU A 89 LYS A 94 1 O LEU A 90 N ARG A 45
SHEET 3 AA 7 LYS A 27 ASP A 32 1 O VAL A 28 N TYR A 91
SHEET 4 AA 7 VAL A 121 LEU A 124 1 O VAL A 121 N ALA A 29
SHEET 5 AA 7 LEU A 148 ALA A 152 1 O LEU A 148 N ALA A 122
SHEET 6 AA 7 ALA A 174 THR A 180 1 O MET A 175 N ALA A 151
SHEET 7 AA 7 ILE A 198 PRO A 201 1 O ILE A 198 N GLY A 178
SHEET 1 AB 2 VAL A 205 TYR A 209 0
SHEET 2 AB 2 THR A 213 LEU A 217 -1 O THR A 213 N TYR A 209
SHEET 1 BA 2 ORN B 2 LEU B 3 0
SHEET 2 BA 2 VAL B 6 ORN B 7 -1 O VAL B 6 N LEU B 3
LINK C VAL B 1 N ORN B 2 1555 1555 1.33
LINK N VAL B 1 C PRO B 10 1555 1555 1.32
LINK C ORN B 2 N LEU B 3 1555 1555 1.32
LINK C LEU B 3 N DPN B 4 1555 1555 1.35
LINK C DPN B 4 N PRO B 5 1555 1555 1.34
LINK C VAL B 6 N ORN B 7 1555 1555 1.32
LINK C ORN B 7 N LEU B 8 1555 1555 1.30
LINK C LEU B 8 N DPN B 9 1555 1555 1.28
LINK C DPN B 9 N PRO B 10 1555 1555 1.32
LINK OE1 GLN A 2 CA CA A1277 1555 1555 2.30
LINK OD1 ASP A 41 CA CA A1277 1555 1555 2.52
LINK OD2 ASP A 41 CA CA A1277 1555 1555 2.48
LINK O LEU A 75 CA CA A1277 1555 1555 2.46
LINK O ILE A 79 CA CA A1277 1555 1555 2.22
LINK O VAL A 81 CA CA A1277 1555 1555 2.37
LINK O ALA A 169 CA CA A1276 1555 1555 2.29
LINK O TYR A 171 CA CA A1276 1555 1555 2.32
LINK O ALA A 174 CA CA A1276 1555 1555 2.32
LINK CA CA A1276 O HOH A2114 1555 1555 2.73
LINK CA CA A1276 O HOH A2137 1555 1555 2.32
CISPEP 1 TYR A 167 PRO A 168 0 6.44
SITE 1 AC1 5 ALA A 169 TYR A 171 ALA A 174 HOH A2114
SITE 2 AC1 5 HOH A2137
SITE 1 AC2 6 GLN A 2 ASP A 41 LEU A 75 ASN A 77
SITE 2 AC2 6 ILE A 79 VAL A 81
SITE 1 AC3 16 LEU A 96 GLY A 100 GLY A 102 ILE A 107
SITE 2 AC3 16 LEU A 126 GLY A 127 SER A 128 PRO A 129
SITE 3 AC3 16 SER A 130 GLY A 154 ASN A 155 SER A 166
SITE 4 AC3 16 GLN A 191 SER A 240 HOH A2127 HOH B2001
CRYST1 76.250 73.340 40.890 90.00 90.00 90.00 P 21 21 21 4
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 0.013115 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024456 0.00000
(ATOM LINES ARE NOT SHOWN.)
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