HEADER HYDROLASE/HYDROLASE INHIBITOR 11-JAN-08 3BX1
TITLE COMPLEX BETWEEN THE BARLEY ALPHA-AMYLASE/SUBTILISIN INHIBITOR AND THE
TITLE 2 SUBTILISIN SAVINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN SAVINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALKALINE PROTEASE;
COMPND 5 EC: 3.4.21.62;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ALPHA-AMYLASE/SUBTILISIN INHIBITOR;
COMPND 9 CHAIN: D, C;
COMPND 10 SYNONYM: BASI;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LENTUS;
SOURCE 3 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HORDEUM VULGARE;
SOURCE 6 ORGANISM_COMMON: BARLEY;
SOURCE 7 EXPRESSION_SYSTEM: PICHIA PASTORIS
KEYWDS COMPLEX (PROTEINASE-INHIBITOR) ENZYME INHIBITION, SAVINASE, BARLEY
KEYWDS 2 ALPHA-AMYLASE/SUBTILISIN INHIBITOR, CALCIUM, HYDROLASE, METAL-
KEYWDS 3 BINDING, PROTEASE, SECRETED, SERINE PROTEASE, SPORULATION, ALPHA-
KEYWDS 4 AMYLASE INHIBITOR, PROTEASE INHIBITOR, SERINE PROTEASE INHIBITOR,
KEYWDS 5 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.O.MICHEELSEN,J.VEVODOVA,K.WILSON,M.SKJOT
REVDAT 3 30-AUG-23 3BX1 1 REMARK LINK
REVDAT 2 24-FEB-09 3BX1 1 VERSN
REVDAT 1 08-JUL-08 3BX1 0
JRNL AUTH P.O.MICHEELSEN,J.VEVODOVA,L.DE MARIA,P.R.OSTERGAARD,
JRNL AUTH 2 E.P.FRIIS,K.WILSON,M.SKJOT
JRNL TITL STRUCTURAL AND MUTATIONAL ANALYSES OF THE INTERACTION
JRNL TITL 2 BETWEEN THE BARLEY ALPHA-AMYLASE/SUBTILISIN INHIBITOR AND
JRNL TITL 3 THE SUBTILISIN SAVINASE REVEAL A NOVEL MODE OF INHIBITION
JRNL REF J.MOL.BIOL. V. 380 681 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18556023
JRNL DOI 10.1016/J.JMB.2008.05.034
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.3
REMARK 3 NUMBER OF REFLECTIONS : 79404
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4208
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2499
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 37.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 120
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6566
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 574
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.81000
REMARK 3 B22 (A**2) : 0.81000
REMARK 3 B33 (A**2) : -1.61000
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): 0.150
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.220
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6791 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9287 ; 1.915 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 921 ;13.901 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 277 ;38.832 ;23.718
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 963 ;18.222 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;19.940 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1029 ; 0.165 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5315 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3257 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4558 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 453 ; 0.167 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 26 ; 0.148 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 90 ; 0.287 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.335 ; 0.200
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): 4485 ; 1.039 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7166 ; 1.847 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2368 ; 2.690 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2108 ; 4.099 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : D C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 10 D 30 4
REMARK 3 1 C 10 C 30 4
REMARK 3 2 D 46 D 125 4
REMARK 3 2 C 46 C 125 4
REMARK 3 3 D 142 D 152 4
REMARK 3 3 C 142 C 152 4
REMARK 3 4 D 165 D 177 4
REMARK 3 4 C 165 C 177 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 D (A): 961 ; .61 ; .50
REMARK 3 MEDIUM THERMAL 1 D (A**2): 961 ; 2.59 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 5 A 270 4
REMARK 3 1 B 5 B 270 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 1829 ; .23 ; .50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 1829 ; 3.35 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3BX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000046062.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.004
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84089
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 41.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.47100
REMARK 200 R SYM FOR SHELL (I) : 0.41500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 1AVA AND 1SVN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE BUFFER PH 5.6 AND
REMARK 280 4 M NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 108.12100
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 50.31850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 50.31850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 54.06050
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 50.31850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 50.31850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 162.18150
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 50.31850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.31850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 54.06050
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 50.31850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.31850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 162.18150
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 108.12100
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
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: 3170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -724.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, 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 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -108.12100
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 275 OXT
REMARK 480 ARG B 275 OXT
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 HOH A 466 O HOH A 491 1.80
REMARK 500 CL CL C 184 O HOH C 307 1.80
REMARK 500 ND2 ASN A 116 NH2 ARG A 145 2.01
REMARK 500 NH1 ARG A 45 O HOH A 497 2.01
REMARK 500 ND2 ASN D 19 NH1 ARG D 61 2.02
REMARK 500 ND2 ASN B 116 NH1 ARG B 145 2.19
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 OH TYR D 131 OH TYR C 131 3545 1.78
REMARK 500
REMARK 500 REMARK: NULL
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 PRO D 69 N PRO D 69 CA 0.113
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 148 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 ALA B 174 N - CA - C ANGL. DEV. = 19.8 DEGREES
REMARK 500 HIS D 137 N - CA - C ANGL. DEV. = -19.4 DEGREES
REMARK 500 GLY D 159 N - CA - C ANGL. DEV. = 19.1 DEGREES
REMARK 500 LEU C 33 CB - CG - CD1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG C 61 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG C 61 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG C 85 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG C 85 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG C 107 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG C 107 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG C 122 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU C 157 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 VAL C 174 CG1 - CB - CG2 ANGL. DEV. = 10.4 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 -149.17 -166.07
REMARK 500 ALA A 73 24.81 -141.49
REMARK 500 ASN A 77 -151.67 -157.49
REMARK 500 VAL A 81 -157.78 -124.81
REMARK 500 ASP B 32 -148.72 -163.21
REMARK 500 ASN B 77 -145.38 -165.24
REMARK 500 VAL B 81 -156.68 -128.93
REMARK 500 ASP D 2 -169.05 -107.58
REMARK 500 THR D 34 -156.84 -149.81
REMARK 500 VAL D 67 -86.22 -115.13
REMARK 500 PRO D 69 126.48 -21.16
REMARK 500 SER D 70 -74.30 -42.18
REMARK 500 VAL D 136 -122.85 37.33
REMARK 500 ASP D 156 146.03 -38.72
REMARK 500 LYS D 158 -46.71 -133.37
REMARK 500 PRO C 3 154.51 -49.80
REMARK 500 ASP C 17 -6.28 75.40
REMARK 500 ASP C 116 66.92 68.13
REMARK 500 SER C 132 7.52 -68.29
REMARK 500 ALA C 134 68.75 -101.72
REMARK 500 GLU C 135 55.66 -93.83
REMARK 500 VAL C 136 -154.30 -158.67
REMARK 500 LYS C 158 -67.68 -14.67
REMARK 500 PRO C 180 110.42 -31.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 173 ALA A 174 134.77
REMARK 500 ASN B 173 ALA B 174 113.67
REMARK 500 VAL D 67 ALA D 68 -146.99
REMARK 500 ALA D 68 PRO D 69 97.15
REMARK 500 PRO D 69 SER D 70 52.21
REMARK 500 SER D 70 ASP D 71 -138.88
REMARK 500 ALA D 134 GLU D 135 -149.65
REMARK 500 GLU D 135 VAL D 136 139.93
REMARK 500 VAL D 136 HIS D 137 -144.34
REMARK 500 ASP D 156 LEU D 157 66.43
REMARK 500 LYS D 158 GLY D 159 56.72
REMARK 500 GLY C 38 HIS C 39 123.37
REMARK 500 GLY C 133 ALA C 134 -128.45
REMARK 500 GLU C 135 VAL C 136 87.15
REMARK 500 VAL C 136 HIS C 137 -133.51
REMARK 500 LEU C 157 LYS C 158 97.30
REMARK 500 PRO C 180 ALA C 181 -146.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 276 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 2 OE1
REMARK 620 2 ASP A 41 OD1 149.1
REMARK 620 3 ASP A 41 OD2 158.2 52.0
REMARK 620 4 LEU A 75 O 77.3 82.4 109.6
REMARK 620 5 ASN A 77 ND2 76.6 79.8 123.3 88.4
REMARK 620 6 ILE A 79 O 94.0 100.1 83.1 164.9 77.5
REMARK 620 7 VAL A 81 O 80.3 123.8 78.8 91.9 156.3 98.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 290 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 169 O
REMARK 620 2 TYR A 171 O 90.8
REMARK 620 3 ALA A 174 O 108.1 92.3
REMARK 620 4 HOH A 445 O 127.3 141.9 79.0
REMARK 620 5 HOH A 446 O 100.6 93.0 150.8 79.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 288 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 194 O
REMARK 620 2 LEU A 196 O 108.1
REMARK 620 3 HOH A 447 O 79.9 85.8
REMARK 620 4 HOH A 448 O 88.2 89.9 165.3
REMARK 620 5 HOH A 449 O 155.7 96.3 101.6 92.7
REMARK 620 6 HOH A 485 O 73.4 168.5 83.3 101.5 82.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 289 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 204 ND2
REMARK 620 2 SER A 216 OG 98.0
REMARK 620 3 HOH A 450 O 172.2 82.0
REMARK 620 4 HOH A 451 O 80.9 98.0 91.4
REMARK 620 5 GLN D 149 OE1 95.3 90.4 92.5 171.1
REMARK 620 6 HOH D 262 O 89.6 172.4 90.4 82.5 89.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 276 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 2 OE1
REMARK 620 2 ASP B 41 OD1 147.7
REMARK 620 3 ASP B 41 OD2 157.2 54.5
REMARK 620 4 LEU B 75 O 78.0 80.4 110.6
REMARK 620 5 ASN B 77 OD1 74.5 82.3 124.9 91.2
REMARK 620 6 ILE B 79 O 88.2 107.8 85.8 163.3 76.0
REMARK 620 7 VAL B 81 O 76.6 125.5 82.9 86.0 150.9 100.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 284 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 169 O
REMARK 620 2 TYR B 171 O 98.8
REMARK 620 3 ALA B 174 O 104.4 101.5
REMARK 620 4 HOH B 289 O 150.3 108.8 81.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 283 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 204 ND2
REMARK 620 2 SER B 216 OG 95.0
REMARK 620 3 HOH B 381 O 173.3 78.3
REMARK 620 4 HOH B 382 O 87.1 100.1 93.0
REMARK 620 5 GLN C 149 NE2 86.7 88.9 94.1 169.5
REMARK 620 6 HOH C 300 O 92.9 169.5 93.8 87.1 84.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 182 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL D 153 O
REMARK 620 2 HOH D 214 O 136.8
REMARK 620 3 HOH D 264 O 102.2 120.6
REMARK 620 4 HOH D 265 O 90.4 100.3 82.2
REMARK 620 5 HOH D 266 O 78.3 85.4 104.2 167.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 187 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C 134 O
REMARK 620 2 HOH C 326 O 107.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 182 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL C 153 O
REMARK 620 2 HOH C 243 O 81.6
REMARK 620 3 HOH C 308 O 76.3 147.7
REMARK 620 4 HOH C 322 O 127.5 101.3 75.0
REMARK 620 5 HOH C 323 O 106.7 86.5 122.2 125.9
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 B 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 183
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 184
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 285
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 286
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 185
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 186
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 185
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 287
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 289
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 290
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 187
DBREF 3BX1 A 1 275 UNP P29600 SUBS_BACLE 1 269
DBREF 3BX1 B 1 275 UNP P29600 SUBS_BACLE 1 269
DBREF 3BX1 D 1 181 UNP P07596 IAAS_HORVU 23 203
DBREF 3BX1 C 1 181 UNP P07596 IAAS_HORVU 23 203
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 269 ALA GLN SER VAL PRO TRP GLY ILE SER ARG VAL GLN ALA
SEQRES 2 B 269 PRO ALA ALA HIS ASN ARG GLY LEU THR GLY SER GLY VAL
SEQRES 3 B 269 LYS VAL ALA VAL LEU ASP THR GLY ILE SER THR HIS PRO
SEQRES 4 B 269 ASP LEU ASN ILE ARG GLY GLY ALA SER PHE VAL PRO GLY
SEQRES 5 B 269 GLU PRO SER THR GLN ASP GLY ASN GLY HIS GLY THR HIS
SEQRES 6 B 269 VAL ALA GLY THR ILE ALA ALA LEU ASN ASN SER ILE GLY
SEQRES 7 B 269 VAL LEU GLY VAL ALA PRO SER ALA GLU LEU TYR ALA VAL
SEQRES 8 B 269 LYS VAL LEU GLY ALA SER GLY SER GLY SER VAL SER SER
SEQRES 9 B 269 ILE ALA GLN GLY LEU GLU TRP ALA GLY ASN ASN GLY MET
SEQRES 10 B 269 HIS VAL ALA ASN LEU SER LEU GLY SER PRO SER PRO SER
SEQRES 11 B 269 ALA THR LEU GLU GLN ALA VAL ASN SER ALA THR SER ARG
SEQRES 12 B 269 GLY VAL LEU VAL VAL ALA ALA SER GLY ASN SER GLY ALA
SEQRES 13 B 269 GLY SER ILE SER TYR PRO ALA ARG TYR ALA ASN ALA MET
SEQRES 14 B 269 ALA VAL GLY ALA THR ASP GLN ASN ASN ASN ARG ALA SER
SEQRES 15 B 269 PHE SER GLN TYR GLY ALA GLY LEU ASP ILE VAL ALA PRO
SEQRES 16 B 269 GLY VAL ASN VAL GLN SER THR TYR PRO GLY SER THR TYR
SEQRES 17 B 269 ALA SER LEU ASN GLY THR SER MET ALA THR PRO HIS VAL
SEQRES 18 B 269 ALA GLY ALA ALA ALA LEU VAL LYS GLN LYS ASN PRO SER
SEQRES 19 B 269 TRP SER ASN VAL GLN ILE ARG ASN HIS LEU LYS ASN THR
SEQRES 20 B 269 ALA THR SER LEU GLY SER THR ASN LEU TYR GLY SER GLY
SEQRES 21 B 269 LEU VAL ASN ALA GLU ALA ALA THR ARG
SEQRES 1 D 181 ALA ASP PRO PRO PRO VAL HIS ASP THR ASP GLY HIS GLU
SEQRES 2 D 181 LEU ARG ALA ASP ALA ASN TYR TYR VAL LEU SER ALA ASN
SEQRES 3 D 181 ARG ALA HIS GLY GLY GLY LEU THR MET ALA PRO GLY HIS
SEQRES 4 D 181 GLY ARG HIS CYS PRO LEU PHE VAL SER GLN ASP PRO ASN
SEQRES 5 D 181 GLY GLN HIS ASP GLY PHE PRO VAL ARG ILE THR PRO TYR
SEQRES 6 D 181 GLY VAL ALA PRO SER ASP LYS ILE ILE ARG LEU SER THR
SEQRES 7 D 181 ASP VAL ARG ILE SER PHE ARG ALA TYR THR THR CYS LEU
SEQRES 8 D 181 GLN SER THR GLU TRP HIS ILE ASP SER GLU LEU ALA ALA
SEQRES 9 D 181 GLY ARG ARG HIS VAL ILE THR GLY PRO VAL LYS ASP PRO
SEQRES 10 D 181 SER PRO SER GLY ARG GLU ASN ALA PHE ARG ILE GLU LYS
SEQRES 11 D 181 TYR SER GLY ALA GLU VAL HIS GLU TYR LYS LEU MET SER
SEQRES 12 D 181 CYS GLY ASP TRP CYS GLN ASP LEU GLY VAL PHE ARG ASP
SEQRES 13 D 181 LEU LYS GLY GLY ALA TRP PHE LEU GLY ALA THR GLU PRO
SEQRES 14 D 181 TYR HIS VAL VAL VAL PHE LYS LYS ALA PRO PRO ALA
SEQRES 1 C 181 ALA ASP PRO PRO PRO VAL HIS ASP THR ASP GLY HIS GLU
SEQRES 2 C 181 LEU ARG ALA ASP ALA ASN TYR TYR VAL LEU SER ALA ASN
SEQRES 3 C 181 ARG ALA HIS GLY GLY GLY LEU THR MET ALA PRO GLY HIS
SEQRES 4 C 181 GLY ARG HIS CYS PRO LEU PHE VAL SER GLN ASP PRO ASN
SEQRES 5 C 181 GLY GLN HIS ASP GLY PHE PRO VAL ARG ILE THR PRO TYR
SEQRES 6 C 181 GLY VAL ALA PRO SER ASP LYS ILE ILE ARG LEU SER THR
SEQRES 7 C 181 ASP VAL ARG ILE SER PHE ARG ALA TYR THR THR CYS LEU
SEQRES 8 C 181 GLN SER THR GLU TRP HIS ILE ASP SER GLU LEU ALA ALA
SEQRES 9 C 181 GLY ARG ARG HIS VAL ILE THR GLY PRO VAL LYS ASP PRO
SEQRES 10 C 181 SER PRO SER GLY ARG GLU ASN ALA PHE ARG ILE GLU LYS
SEQRES 11 C 181 TYR SER GLY ALA GLU VAL HIS GLU TYR LYS LEU MET SER
SEQRES 12 C 181 CYS GLY ASP TRP CYS GLN ASP LEU GLY VAL PHE ARG ASP
SEQRES 13 C 181 LEU LYS GLY GLY ALA TRP PHE LEU GLY ALA THR GLU PRO
SEQRES 14 C 181 TYR HIS VAL VAL VAL PHE LYS LYS ALA PRO PRO ALA
HET CA A 276 1
HET CL A 277 1
HET CL A 278 1
HET CL A 279 1
HET CL A 280 1
HET CL A 281 1
HET CL A 282 1
HET CL A 283 1
HET CL A 284 1
HET CL A 285 1
HET CL A 286 1
HET CL A 287 1
HET NA A 288 1
HET NA A 289 1
HET NA A 290 1
HET CA B 276 1
HET CL B 277 1
HET CL B 278 1
HET CL B 279 1
HET CL B 280 1
HET CL B 281 1
HET CL B 282 1
HET NA B 283 1
HET NA B 284 1
HET CA D 182 1
HET CL D 183 1
HET CL D 184 1
HET CL D 185 1
HET CA C 182 1
HET CL C 183 1
HET CL C 184 1
HET CL C 185 1
HET CL C 186 1
HET NA C 187 1
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 5 CA 4(CA 2+)
FORMUL 6 CL 24(CL 1-)
FORMUL 17 NA 6(NA 1+)
FORMUL 39 HOH *574(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 ALA A 254 1 13
HELIX 8 8 SER A 259 GLY A 264 1 6
HELIX 9 9 ASN A 269 ARG A 275 1 7
HELIX 10 10 PRO B 5 VAL B 11 1 7
HELIX 11 11 GLN B 12 ARG B 19 1 8
HELIX 12 12 GLY B 63 ALA B 74 1 12
HELIX 13 13 SER B 103 ASN B 117 1 15
HELIX 14 14 SER B 132 ARG B 145 1 14
HELIX 15 15 GLY B 219 ASN B 238 1 20
HELIX 16 16 SER B 242 ALA B 254 1 13
HELIX 17 17 SER B 259 GLY B 264 1 6
HELIX 18 18 ASN D 26 GLY D 30 5 5
HELIX 19 19 ASN C 26 GLY C 30 5 5
HELIX 20 20 GLY C 121 ASN C 124 5 4
SHEET 1 A 7 ILE A 44 SER A 49 0
SHEET 2 A 7 GLU A 89 LYS A 94 1 O LEU A 90 N ARG A 45
SHEET 3 A 7 LYS A 27 ASP A 32 1 N VAL A 28 O GLU A 89
SHEET 4 A 7 VAL A 121 LEU A 124 1 O VAL A 121 N ALA A 29
SHEET 5 A 7 LEU A 148 ALA A 152 1 O VAL A 150 N ALA A 122
SHEET 6 A 7 ALA A 174 THR A 180 1 O MET A 175 N VAL A 149
SHEET 7 A 7 LEU A 196 PRO A 201 1 O ALA A 200 N THR A 180
SHEET 1 B 2 SER A 101 GLY A 102 0
SHEET 2 B 2 TYR C 87 THR C 88 -1 O TYR C 87 N GLY A 102
SHEET 1 C 3 VAL A 205 TYR A 209 0
SHEET 2 C 3 THR A 213 LEU A 217 -1 O LEU A 217 N VAL A 205
SHEET 3 C 3 THR D 167 GLU D 168 -1 O GLU D 168 N TYR A 214
SHEET 1 D 7 ILE B 44 SER B 49 0
SHEET 2 D 7 GLU B 89 LYS B 94 1 O ALA B 92 N GLY B 46
SHEET 3 D 7 LYS B 27 ASP B 32 1 N VAL B 28 O GLU B 89
SHEET 4 D 7 VAL B 121 LEU B 124 1 O VAL B 121 N ALA B 29
SHEET 5 D 7 LEU B 148 ALA B 152 1 O VAL B 150 N LEU B 124
SHEET 6 D 7 ALA B 174 THR B 180 1 O MET B 175 N ALA B 151
SHEET 7 D 7 ILE B 198 PRO B 201 1 O ALA B 200 N THR B 180
SHEET 1 E 2 SER B 101 GLY B 102 0
SHEET 2 E 2 TYR D 87 THR D 88 -1 O TYR D 87 N GLY B 102
SHEET 1 F 3 VAL B 205 TYR B 209 0
SHEET 2 F 3 THR B 213 ASN B 218 -1 O LEU B 217 N VAL B 205
SHEET 3 F 3 GLY C 105 ARG C 106 -1 O GLY C 105 N ASN B 218
SHEET 1 G 3 VAL B 205 TYR B 209 0
SHEET 2 G 3 THR B 213 ASN B 218 -1 O LEU B 217 N VAL B 205
SHEET 3 G 3 THR C 167 GLU C 168 -1 O GLU C 168 N TYR B 214
SHEET 1 H 4 TYR D 20 SER D 24 0
SHEET 2 H 4 VAL D 172 LYS D 177 -1 O LYS D 176 N TYR D 21
SHEET 3 H 4 TYR D 139 CYS D 144 -1 N TYR D 139 O VAL D 173
SHEET 4 H 4 PHE D 126 LYS D 130 -1 N GLU D 129 O LYS D 140
SHEET 1 I 4 TYR D 20 SER D 24 0
SHEET 2 I 4 VAL D 172 LYS D 177 -1 O LYS D 176 N TYR D 21
SHEET 3 I 4 TYR D 139 CYS D 144 -1 N TYR D 139 O VAL D 173
SHEET 4 I 4 CYS D 148 ASP D 150 -1 O GLN D 149 N SER D 143
SHEET 1 J 4 LEU D 33 ALA D 36 0
SHEET 2 J 4 PHE D 46 GLN D 49 -1 O PHE D 46 N ALA D 36
SHEET 3 J 4 TRP D 162 GLY D 165 -1 O LEU D 164 N VAL D 47
SHEET 4 J 4 GLY D 152 PHE D 154 -1 N PHE D 154 O PHE D 163
SHEET 1 K 2 VAL D 60 PRO D 64 0
SHEET 2 K 2 VAL D 80 PHE D 84 -1 O ARG D 81 N THR D 63
SHEET 1 L 2 HIS D 97 ILE D 98 0
SHEET 2 L 2 VAL D 109 ILE D 110 -1 O ILE D 110 N HIS D 97
SHEET 1 M 4 VAL C 80 PHE C 84 0
SHEET 2 M 4 PRO C 59 PRO C 64 -1 N THR C 63 O ARG C 81
SHEET 3 M 4 ASN C 19 SER C 24 -1 N TYR C 20 O VAL C 60
SHEET 4 M 4 VAL C 173 LYS C 177 -1 O LYS C 176 N TYR C 21
SHEET 1 N 2 LEU C 33 ALA C 36 0
SHEET 2 N 2 PHE C 46 GLN C 49 -1 O PHE C 46 N ALA C 36
SHEET 1 O 2 TRP C 96 ILE C 98 0
SHEET 2 O 2 VAL C 109 THR C 111 -1 O ILE C 110 N HIS C 97
SHEET 1 P 3 PHE C 126 LYS C 130 0
SHEET 2 P 3 TYR C 139 CYS C 144 -1 O LYS C 140 N GLU C 129
SHEET 3 P 3 CYS C 148 ASP C 150 -1 O GLN C 149 N SER C 143
SHEET 1 Q 2 GLY C 152 PHE C 154 0
SHEET 2 Q 2 PHE C 163 GLY C 165 -1 O PHE C 163 N PHE C 154
SSBOND 1 CYS D 43 CYS D 90 1555 1555 2.05
SSBOND 2 CYS D 144 CYS D 148 1555 1555 2.07
SSBOND 3 CYS C 43 CYS C 90 1555 1555 2.00
SSBOND 4 CYS C 144 CYS C 148 1555 1555 2.07
LINK OE1 GLN A 2 CA CA A 276 1555 1555 2.40
LINK OD1 ASP A 41 CA CA A 276 1555 1555 2.34
LINK OD2 ASP A 41 CA CA A 276 1555 1555 2.54
LINK O LEU A 75 CA CA A 276 1555 1555 2.35
LINK ND2 ASN A 77 CA CA A 276 1555 1555 2.43
LINK O ILE A 79 CA CA A 276 1555 1555 2.34
LINK O VAL A 81 CA CA A 276 1555 1555 2.24
LINK O ALA A 169 NA NA A 290 1555 1555 2.25
LINK O TYR A 171 NA NA A 290 1555 1555 2.36
LINK O ALA A 174 NA NA A 290 1555 1555 2.21
LINK O ALA A 194 NA NA A 288 1555 1555 2.49
LINK O LEU A 196 NA NA A 288 1555 1555 2.40
LINK ND2 ASN A 204 NA NA A 289 1555 1555 2.46
LINK OG SER A 216 NA NA A 289 1555 1555 2.46
LINK NA NA A 288 O HOH A 447 1555 1555 2.41
LINK NA NA A 288 O HOH A 448 1555 1555 2.33
LINK NA NA A 288 O HOH A 449 1555 1555 2.45
LINK NA NA A 288 O HOH A 485 1555 1555 2.55
LINK NA NA A 289 O HOH A 450 1555 1555 2.36
LINK NA NA A 289 O HOH A 451 1555 1555 2.38
LINK NA NA A 289 OE1 GLN D 149 1555 1555 2.45
LINK NA NA A 289 O HOH D 262 1555 1555 2.49
LINK NA NA A 290 O HOH A 445 1555 1555 2.20
LINK NA NA A 290 O HOH A 446 1555 1555 2.45
LINK OE1 GLN B 2 CA CA B 276 1555 1555 2.31
LINK OD1 ASP B 41 CA CA B 276 1555 1555 2.35
LINK OD2 ASP B 41 CA CA B 276 1555 1555 2.44
LINK O LEU B 75 CA CA B 276 1555 1555 2.34
LINK OD1 ASN B 77 CA CA B 276 1555 1555 2.48
LINK O ILE B 79 CA CA B 276 1555 1555 2.28
LINK O VAL B 81 CA CA B 276 1555 1555 2.47
LINK O ALA B 169 NA NA B 284 1555 1555 2.26
LINK O TYR B 171 NA NA B 284 1555 1555 2.16
LINK O ALA B 174 NA NA B 284 1555 1555 2.08
LINK ND2 ASN B 204 NA NA B 283 1555 1555 2.43
LINK OG SER B 216 NA NA B 283 1555 1555 2.46
LINK NA NA B 283 O HOH B 381 1555 1555 2.41
LINK NA NA B 283 O HOH B 382 1555 1555 2.44
LINK NA NA B 283 NE2 GLN C 149 1555 1555 2.47
LINK NA NA B 283 O HOH C 300 1555 1555 2.49
LINK NA NA B 284 O HOH B 289 1555 1555 2.90
LINK O VAL D 153 CA CA D 182 1555 1555 2.25
LINK CA CA D 182 O HOH D 214 1555 1555 2.38
LINK CA CA D 182 O HOH D 264 1555 1555 2.50
LINK CA CA D 182 O HOH D 265 1555 1555 2.70
LINK CA CA D 182 O HOH D 266 1555 1555 2.50
LINK O ALA C 134 NA NA C 187 1555 1555 2.54
LINK O VAL C 153 CA CA C 182 1555 1555 2.38
LINK CA CA C 182 O HOH C 243 1555 1555 2.88
LINK CA CA C 182 O HOH C 308 1555 1555 2.57
LINK CA CA C 182 O HOH C 322 1555 1555 2.68
LINK CA CA C 182 O HOH C 323 1555 1555 2.08
LINK NA NA C 187 O HOH C 326 1555 1555 2.86
CISPEP 1 TYR A 167 PRO A 168 0 4.55
CISPEP 2 TYR B 167 PRO B 168 0 6.35
CISPEP 3 CYS D 43 PRO D 44 0 0.81
CISPEP 4 LEU D 157 LYS D 158 0 0.37
CISPEP 5 GLU D 168 PRO D 169 0 7.66
CISPEP 6 PRO D 180 ALA D 181 0 5.92
CISPEP 7 CYS C 43 PRO C 44 0 -6.33
CISPEP 8 LYS C 158 GLY C 159 0 -6.06
CISPEP 9 GLU C 168 PRO C 169 0 7.67
SITE 1 AC1 5 GLN B 2 ASP B 41 LEU B 75 ASN B 77
SITE 2 AC1 5 ILE B 79
SITE 1 AC2 5 GLN A 2 ASP A 41 LEU A 75 ASN A 77
SITE 2 AC2 5 ILE A 79
SITE 1 AC5 4 GLU A 54 PRO A 55 SER A 56 LYS A 94
SITE 1 AC6 2 ALA A 48 SER A 49
SITE 1 AC7 2 HIS C 42 ARG D 106
SITE 1 AC8 1 TRP A 6
SITE 1 AC9 2 PRO B 5 TRP B 6
SITE 1 BC1 1 GLY A 80
SITE 1 BC2 2 HIS C 29 HIS C 171
SITE 1 BC3 2 ARG B 10 ASN B 183
SITE 1 BC4 3 GLN B 12 PRO B 14 ALA B 15
SITE 1 BC5 3 SER A 156 LYS C 72 SER C 93
SITE 1 BC6 1 GLN A 137
SITE 1 BC7 3 GLN A 206 SER A 216 GLN D 149
SITE 1 BC8 4 GLN B 206 SER B 216 GLN C 149 THR C 167
SITE 1 BC9 4 ILE A 165 ARG A 170 ALA A 194 GLY A 195
SITE 1 CC1 2 ARG A 10 ASN A 183
SITE 1 CC2 4 ARG A 19 SER B 259 THR B 260 ASN B 261
SITE 1 CC3 3 ASN B 155 GLY B 219 SER B 221
SITE 1 CC4 2 ARG C 106 HIS D 42
SITE 1 CC5 3 ASN C 19 ARG C 61 ARG C 85
SITE 1 CC6 4 HIS D 39 ARG D 41 PRO D 44 PHE D 46
SITE 1 CC7 2 GLY A 211 SER A 212
SITE 1 CC8 3 ASN B 204 SER B 216 GLN C 149
SITE 1 CC9 2 ALA A 194 LEU A 196
SITE 1 DC1 3 ASN A 204 SER A 216 GLN D 149
SITE 1 DC2 3 ALA B 169 TYR B 171 ALA B 174
SITE 1 DC3 3 ALA A 169 TYR A 171 ALA A 174
SITE 1 DC4 2 ALA C 134 HIS C 137
CRYST1 100.637 100.637 216.242 90.00 90.00 90.00 P 41 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 0.009937 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009937 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004624 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
