HEADER UNKNOWN FUNCTION 22-MAY-14 4PMO
TITLE CRYSTAL STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS TAT-SECRETED
TITLE 2 PROTEIN RV2525C, MONOCLINIC CRYSTAL FORM I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TAT-SECRETED PROTEIN RV2525C;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83331;
SOURCE 4 STRAIN: CDC 1551 / OSHKOSH;
SOURCE 5 GENE: MT2601;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDEST17
KEYWDS TAT SECRETION GH25, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BELLINZONI,A.HAOUZ,W.SHEPARD,P.M.ALZARI
REVDAT 3 20-DEC-23 4PMO 1 LINK
REVDAT 2 10-DEC-14 4PMO 1 JRNL
REVDAT 1 08-OCT-14 4PMO 0
JRNL AUTH M.BELLINZONI,A.HAOUZ,I.MIRAS,S.MAGNET,G.ANDRE-LEROUX,
JRNL AUTH 2 R.MUKHERJEE,W.SHEPARD,S.T.COLE,P.M.ALZARI
JRNL TITL STRUCTURAL STUDIES SUGGEST A PEPTIDOGLYCAN HYDROLASE
JRNL TITL 2 FUNCTION FOR THE MYCOBACTERIUM TUBERCULOSIS TAT-SECRETED
JRNL TITL 3 PROTEIN RV2525C.
JRNL REF J.STRUCT.BIOL. V. 188 156 2014
JRNL REFN ESSN 1095-8657
JRNL PMID 25260828
JRNL DOI 10.1016/J.JSB.2014.09.003
REMARK 2
REMARK 2 RESOLUTION. 1.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 85995
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4528
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) : 1.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5002
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.3500
REMARK 3 BIN FREE R VALUE SET COUNT : 279
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3178
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.35000
REMARK 3 B33 (A**2) : 0.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.32000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.046
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.037
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.872
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.972
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3380 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3094 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4592 ; 1.751 ; 1.933
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7093 ; 1.106 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 443 ; 6.199 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;39.267 ;23.288
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 480 ;10.711 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;23.557 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 474 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3994 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 850 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1710 ; 1.017 ; 0.684
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1711 ; 1.017 ; 0.684
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2140 ; 1.651 ; 1.024
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2141 ; 1.651 ; 1.024
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1670 ; 1.806 ; 0.861
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1650 ; 1.742 ; 0.848
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2441 ; 2.716 ; 1.198
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4141 ; 5.244 ; 6.790
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3980 ; 5.071 ; 6.189
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 30 240 B 30 240 12322 0.07 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 30 B 240
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8720 8.9260 1.4650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0420 T22: 0.0018
REMARK 3 T33: 0.0488 T12: 0.0029
REMARK 3 T13: -0.0437 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.3541 L22: 0.7778
REMARK 3 L33: 0.4347 L12: -0.0437
REMARK 3 L13: 0.2362 L23: -0.0386
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: 0.0051 S13: -0.0114
REMARK 3 S21: -0.0431 S22: 0.0080 S23: 0.0111
REMARK 3 S31: -0.0081 S32: -0.0168 S33: -0.0152
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 30 B 240
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8250 -8.9310 26.0080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0366 T22: 0.0036
REMARK 3 T33: 0.0615 T12: 0.0029
REMARK 3 T13: -0.0465 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.3783 L22: 0.8617
REMARK 3 L33: 0.4286 L12: 0.0495
REMARK 3 L13: 0.2196 L23: -0.0290
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: -0.0311 S13: -0.0047
REMARK 3 S21: 0.0070 S22: 0.0045 S23: -0.0289
REMARK 3 S31: -0.0041 S32: -0.0024 S33: 0.0091
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 4PMO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201641.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90524
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.330
REMARK 200 RESOLUTION RANGE LOW (A) : 37.610
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.64000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: 4PMN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M NA FORMATE, 100 MM SODIUM ACETATE
REMARK 280 PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 49.72100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.83950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.72100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.83950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 A 429 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 471 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 7
REMARK 465 SER A 8
REMARK 465 TYR A 9
REMARK 465 TYR A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 LEU A 17
REMARK 465 GLU A 18
REMARK 465 SER A 19
REMARK 465 THR A 20
REMARK 465 SER A 21
REMARK 465 LEU A 22
REMARK 465 TYR A 23
REMARK 465 LYS A 24
REMARK 465 LYS A 25
REMARK 465 ALA A 26
REMARK 465 GLY A 27
REMARK 465 SER A 28
REMARK 465 GLU A 29
REMARK 465 MET B 7
REMARK 465 SER B 8
REMARK 465 TYR B 9
REMARK 465 TYR B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 HIS B 15
REMARK 465 HIS B 16
REMARK 465 LEU B 17
REMARK 465 GLU B 18
REMARK 465 SER B 19
REMARK 465 THR B 20
REMARK 465 SER B 21
REMARK 465 LEU B 22
REMARK 465 TYR B 23
REMARK 465 LYS B 24
REMARK 465 LYS B 25
REMARK 465 ALA B 26
REMARK 465 GLY B 27
REMARK 465 SER B 28
REMARK 465 GLU B 29
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 30 CG OD1 ND2
REMARK 470 GLU A 150 CG CD OE1 OE2
REMARK 470 GLN A 170 CG CD OE1 NE2
REMARK 470 ASP A 217 CG OD1 OD2
REMARK 470 ASN B 30 CG OD1 ND2
REMARK 470 GLU B 150 CG CD OE1 OE2
REMARK 470 LYS B 202 CG CD CE NZ
REMARK 470 ASP B 217 CG OD1 OD2
REMARK 470 LYS B 218 CG CD CE NZ
REMARK 470 ARG B 219 CG CD NE CZ NH1 NH2
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 B 574 O HOH B 582 2.08
REMARK 500 O HOH A 543 O HOH A 575 2.09
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 O HOH A 454 O HOH B 451 1454 2.18
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 GLU A 126 CD GLU A 126 OE1 0.151
REMARK 500 GLU B 126 CD GLU B 126 OE1 0.121
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 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 4.2 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 VAL A 66 50.85 -104.74
REMARK 500 TYR A 102 -65.88 -103.89
REMARK 500 ASN A 146 73.02 -117.10
REMARK 500 VAL B 66 50.55 -106.08
REMARK 500 TYR B 102 -65.93 -103.82
REMARK 500 ASN B 146 73.14 -117.09
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 NA A 311 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 34 O
REMARK 620 2 GLN A 34 OE1 77.1
REMARK 620 3 GOL A 302 O3 82.0 83.8
REMARK 620 4 HOH A 424 O 107.8 90.2 167.1
REMARK 620 5 HOH A 438 O 93.4 170.2 92.5 95.1
REMARK 620 6 HOH A 485 O 155.9 84.6 80.5 87.6 103.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 312 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 34 OE1
REMARK 620 2 GOL A 302 O2 149.3
REMARK 620 3 GOL A 302 O3 85.2 68.4
REMARK 620 4 HOH A 485 O 84.9 74.9 78.3
REMARK 620 5 HOH A 541 O 115.8 90.2 158.6 98.4
REMARK 620 6 HOH A 542 O 97.4 97.8 89.7 167.6 91.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 310 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 35 O
REMARK 620 2 GLY A 36 O 83.6
REMARK 620 3 FMT A 305 O1 95.9 97.4
REMARK 620 4 HOH A 412 O 101.6 82.0 162.3
REMARK 620 5 HOH A 418 O 91.7 166.6 95.6 86.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 309 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 34 O
REMARK 620 2 GLN B 34 OE1 77.8
REMARK 620 3 GOL B 302 O3 81.9 83.4
REMARK 620 4 HOH B 426 O 108.2 89.0 165.9
REMARK 620 5 HOH B 430 O 93.2 170.7 93.1 96.1
REMARK 620 6 HOH B 434 O 156.0 83.8 80.8 86.5 104.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 310 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 34 OE1
REMARK 620 2 GOL B 302 O2 149.7
REMARK 620 3 GOL B 302 O3 86.3 67.9
REMARK 620 4 HOH B 434 O 85.6 74.3 78.7
REMARK 620 5 HOH B 479 O 117.4 87.9 155.7 96.9
REMARK 620 6 HOH B 530 O 98.7 97.3 90.7 168.3 90.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 308 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 35 O
REMARK 620 2 GLY B 36 O 84.6
REMARK 620 3 FMT B 306 O2 106.2 31.7
REMARK 620 4 HOH B 414 O 103.8 83.0 99.9
REMARK 620 5 HOH B 422 O 92.4 167.4 158.3 85.9
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 310
DBREF 4PMO A 36 240 UNP P95028 P95028_MYCTO 36 240
DBREF 4PMO B 36 240 UNP P95028 P95028_MYCTO 36 240
SEQADV 4PMO MET A 7 UNP P95028 INITIATING METHIONINE
SEQADV 4PMO SER A 8 UNP P95028 EXPRESSION TAG
SEQADV 4PMO TYR A 9 UNP P95028 EXPRESSION TAG
SEQADV 4PMO TYR A 10 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS A 11 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS A 12 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS A 13 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS A 14 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS A 15 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS A 16 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LEU A 17 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLU A 18 UNP P95028 EXPRESSION TAG
SEQADV 4PMO SER A 19 UNP P95028 EXPRESSION TAG
SEQADV 4PMO THR A 20 UNP P95028 EXPRESSION TAG
SEQADV 4PMO SER A 21 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LEU A 22 UNP P95028 EXPRESSION TAG
SEQADV 4PMO TYR A 23 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LYS A 24 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LYS A 25 UNP P95028 EXPRESSION TAG
SEQADV 4PMO ALA A 26 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLY A 27 UNP P95028 EXPRESSION TAG
SEQADV 4PMO SER A 28 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLU A 29 UNP P95028 EXPRESSION TAG
SEQADV 4PMO ASN A 30 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LEU A 31 UNP P95028 EXPRESSION TAG
SEQADV 4PMO TYR A 32 UNP P95028 EXPRESSION TAG
SEQADV 4PMO PHE A 33 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLN A 34 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLY A 35 UNP P95028 EXPRESSION TAG
SEQADV 4PMO MET B 7 UNP P95028 INITIATING METHIONINE
SEQADV 4PMO SER B 8 UNP P95028 EXPRESSION TAG
SEQADV 4PMO TYR B 9 UNP P95028 EXPRESSION TAG
SEQADV 4PMO TYR B 10 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS B 11 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS B 12 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS B 13 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS B 14 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS B 15 UNP P95028 EXPRESSION TAG
SEQADV 4PMO HIS B 16 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LEU B 17 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLU B 18 UNP P95028 EXPRESSION TAG
SEQADV 4PMO SER B 19 UNP P95028 EXPRESSION TAG
SEQADV 4PMO THR B 20 UNP P95028 EXPRESSION TAG
SEQADV 4PMO SER B 21 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LEU B 22 UNP P95028 EXPRESSION TAG
SEQADV 4PMO TYR B 23 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LYS B 24 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LYS B 25 UNP P95028 EXPRESSION TAG
SEQADV 4PMO ALA B 26 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLY B 27 UNP P95028 EXPRESSION TAG
SEQADV 4PMO SER B 28 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLU B 29 UNP P95028 EXPRESSION TAG
SEQADV 4PMO ASN B 30 UNP P95028 EXPRESSION TAG
SEQADV 4PMO LEU B 31 UNP P95028 EXPRESSION TAG
SEQADV 4PMO TYR B 32 UNP P95028 EXPRESSION TAG
SEQADV 4PMO PHE B 33 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLN B 34 UNP P95028 EXPRESSION TAG
SEQADV 4PMO GLY B 35 UNP P95028 EXPRESSION TAG
SEQRES 1 A 234 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 A 234 THR SER LEU TYR LYS LYS ALA GLY SER GLU ASN LEU TYR
SEQRES 3 A 234 PHE GLN GLY GLY SER LEU GLY THR LEU LEU ASP TYR ALA
SEQRES 4 A 234 ALA GLY VAL ILE PRO ALA SER GLN ILE ARG ALA ALA GLY
SEQRES 5 A 234 ALA VAL GLY ALA ILE ARG TYR VAL SER ASP ARG ARG PRO
SEQRES 6 A 234 GLY GLY ALA TRP MET LEU GLY LYS PRO ILE GLN LEU SER
SEQRES 7 A 234 GLU ALA ARG ASP LEU SER GLY ASN GLY LEU LYS ILE VAL
SEQRES 8 A 234 SER CYS TYR GLN TYR GLY LYS GLY SER THR ALA ASP TRP
SEQRES 9 A 234 LEU GLY GLY ALA SER ALA GLY VAL GLN HIS ALA ARG ARG
SEQRES 10 A 234 GLY SER GLU LEU HIS ALA ALA ALA GLY GLY PRO THR SER
SEQRES 11 A 234 ALA PRO ILE TYR ALA SER ILE ASP ASP ASN PRO SER TYR
SEQRES 12 A 234 GLU GLN TYR LYS ASN GLN ILE VAL PRO TYR LEU ARG SER
SEQRES 13 A 234 TRP GLU SER VAL ILE GLY HIS GLN ARG THR GLY VAL TYR
SEQRES 14 A 234 ALA ASN SER LYS THR ILE ASP TRP ALA VAL ASN ASP GLY
SEQRES 15 A 234 LEU GLY SER TYR PHE TRP GLN HIS ASN TRP GLY SER PRO
SEQRES 16 A 234 LYS GLY TYR THR HIS PRO ALA ALA HIS LEU HIS GLN VAL
SEQRES 17 A 234 GLU ILE ASP LYS ARG LYS VAL GLY GLY VAL GLY VAL ASP
SEQRES 18 A 234 VAL ASN GLN ILE LEU LYS PRO GLN PHE GLY GLN TRP ALA
SEQRES 1 B 234 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 B 234 THR SER LEU TYR LYS LYS ALA GLY SER GLU ASN LEU TYR
SEQRES 3 B 234 PHE GLN GLY GLY SER LEU GLY THR LEU LEU ASP TYR ALA
SEQRES 4 B 234 ALA GLY VAL ILE PRO ALA SER GLN ILE ARG ALA ALA GLY
SEQRES 5 B 234 ALA VAL GLY ALA ILE ARG TYR VAL SER ASP ARG ARG PRO
SEQRES 6 B 234 GLY GLY ALA TRP MET LEU GLY LYS PRO ILE GLN LEU SER
SEQRES 7 B 234 GLU ALA ARG ASP LEU SER GLY ASN GLY LEU LYS ILE VAL
SEQRES 8 B 234 SER CYS TYR GLN TYR GLY LYS GLY SER THR ALA ASP TRP
SEQRES 9 B 234 LEU GLY GLY ALA SER ALA GLY VAL GLN HIS ALA ARG ARG
SEQRES 10 B 234 GLY SER GLU LEU HIS ALA ALA ALA GLY GLY PRO THR SER
SEQRES 11 B 234 ALA PRO ILE TYR ALA SER ILE ASP ASP ASN PRO SER TYR
SEQRES 12 B 234 GLU GLN TYR LYS ASN GLN ILE VAL PRO TYR LEU ARG SER
SEQRES 13 B 234 TRP GLU SER VAL ILE GLY HIS GLN ARG THR GLY VAL TYR
SEQRES 14 B 234 ALA ASN SER LYS THR ILE ASP TRP ALA VAL ASN ASP GLY
SEQRES 15 B 234 LEU GLY SER TYR PHE TRP GLN HIS ASN TRP GLY SER PRO
SEQRES 16 B 234 LYS GLY TYR THR HIS PRO ALA ALA HIS LEU HIS GLN VAL
SEQRES 17 B 234 GLU ILE ASP LYS ARG LYS VAL GLY GLY VAL GLY VAL ASP
SEQRES 18 B 234 VAL ASN GLN ILE LEU LYS PRO GLN PHE GLY GLN TRP ALA
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET FMT A 304 3
HET FMT A 305 3
HET FMT A 306 3
HET FMT A 307 3
HET FMT A 308 3
HET FMT A 309 3
HET NA A 310 1
HET NA A 311 1
HET NA A 312 1
HET GOL B 301 6
HET GOL B 302 6
HET GOL B 303 6
HET FMT B 304 3
HET FMT B 305 3
HET FMT B 306 3
HET FMT B 307 3
HET NA B 308 1
HET NA B 309 1
HET NA B 310 1
HETNAM GOL GLYCEROL
HETNAM FMT FORMIC ACID
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 6(C3 H8 O3)
FORMUL 6 FMT 10(C H2 O2)
FORMUL 12 NA 6(NA 1+)
FORMUL 25 HOH *370(H2 O)
HELIX 1 AA1 PRO A 50 ALA A 57 1 8
HELIX 2 AA2 GLN A 82 ASN A 92 1 11
HELIX 3 AA3 LYS A 104 LEU A 111 5 8
HELIX 4 AA4 GLY A 112 ALA A 131 1 20
HELIX 5 AA5 SER A 148 GLN A 155 1 8
HELIX 6 AA6 GLN A 155 GLY A 168 1 14
HELIX 7 AA7 SER A 178 GLY A 188 1 11
HELIX 8 AA8 PRO B 50 ALA B 57 1 8
HELIX 9 AA9 GLN B 82 ASN B 92 1 11
HELIX 10 AB1 LYS B 104 LEU B 111 5 8
HELIX 11 AB2 GLY B 112 ALA B 131 1 20
HELIX 12 AB3 SER B 148 GLN B 155 1 8
HELIX 13 AB4 GLN B 155 GLY B 168 1 14
HELIX 14 AB5 SER B 178 GLY B 188 1 11
SHEET 1 AA1 9 THR A 40 ASP A 43 0
SHEET 2 AA1 9 GLY A 61 TYR A 65 1 O ILE A 63 N LEU A 42
SHEET 3 AA1 9 LYS A 95 TYR A 100 1 O VAL A 97 N ARG A 64
SHEET 4 AA1 9 ILE A 139 SER A 142 1 O TYR A 140 N TYR A 100
SHEET 5 AA1 9 THR A 172 ASN A 177 1 O TYR A 175 N ALA A 141
SHEET 6 AA1 9 TYR A 192 HIS A 196 1 O TRP A 194 N VAL A 174
SHEET 7 AA1 9 LEU A 211 VAL A 221 1 O GLN A 213 N GLN A 195
SHEET 8 AA1 9 VAL A 224 ILE A 231 -1 O GLN A 230 N HIS A 212
SHEET 9 AA1 9 THR A 40 ASP A 43 -1 N ASP A 43 O ASP A 227
SHEET 1 AA2 9 THR B 40 ASP B 43 0
SHEET 2 AA2 9 GLY B 61 TYR B 65 1 O ILE B 63 N LEU B 42
SHEET 3 AA2 9 LYS B 95 TYR B 100 1 O VAL B 97 N ARG B 64
SHEET 4 AA2 9 ILE B 139 SER B 142 1 O TYR B 140 N TYR B 100
SHEET 5 AA2 9 THR B 172 ASN B 177 1 O TYR B 175 N ALA B 141
SHEET 6 AA2 9 TYR B 192 HIS B 196 1 O TRP B 194 N VAL B 174
SHEET 7 AA2 9 LEU B 211 VAL B 221 1 O GLN B 213 N GLN B 195
SHEET 8 AA2 9 VAL B 224 ILE B 231 -1 O GLN B 230 N HIS B 212
SHEET 9 AA2 9 THR B 40 ASP B 43 -1 N ASP B 43 O ASP B 227
LINK O GLN A 34 NA NA A 311 1555 1555 2.30
LINK OE1 GLN A 34 NA NA A 311 1555 1555 2.46
LINK OE1 GLN A 34 NA NA A 312 1555 1555 2.37
LINK O GLY A 35 NA NA A 310 1555 1555 2.25
LINK O GLY A 36 NA NA A 310 1555 1555 2.38
LINK O3 GOL A 302 NA NA A 311 1555 1555 2.39
LINK O2 GOL A 302 NA NA A 312 1555 1555 2.57
LINK O3 GOL A 302 NA NA A 312 1555 1555 2.42
LINK O1 FMT A 305 NA NA A 310 1555 1555 2.30
LINK NA NA A 310 O HOH A 412 1555 1555 2.48
LINK NA NA A 310 O HOH A 418 1555 4455 2.30
LINK NA NA A 311 O HOH A 424 1555 1555 2.37
LINK NA NA A 311 O HOH A 438 1555 1555 2.29
LINK NA NA A 311 O HOH A 485 1555 1555 2.39
LINK NA NA A 312 O HOH A 485 1555 1555 2.46
LINK NA NA A 312 O HOH A 541 1555 1555 2.22
LINK NA NA A 312 O HOH A 542 1555 1555 2.38
LINK O GLN B 34 NA NA B 309 1555 1555 2.33
LINK OE1 GLN B 34 NA NA B 309 1555 1555 2.45
LINK OE1 GLN B 34 NA NA B 310 1555 1555 2.29
LINK O GLY B 35 NA NA B 308 1555 1555 2.25
LINK O GLY B 36 NA NA B 308 1555 1555 2.36
LINK O3 GOL B 302 NA NA B 309 1555 1555 2.40
LINK O2 GOL B 302 NA NA B 310 1555 1555 2.68
LINK O3 GOL B 302 NA NA B 310 1555 1555 2.42
LINK O2 FMT B 306 NA NA B 308 1555 4556 2.36
LINK NA NA B 308 O HOH B 414 1555 1555 2.48
LINK NA NA B 308 O HOH B 422 1555 4546 2.27
LINK NA NA B 309 O HOH B 426 1555 4546 2.42
LINK NA NA B 309 O HOH B 430 1555 4546 2.30
LINK NA NA B 309 O HOH B 434 1555 1555 2.42
LINK NA NA B 310 O HOH B 434 1555 1555 2.50
LINK NA NA B 310 O HOH B 479 1555 1555 2.23
LINK NA NA B 310 O HOH B 530 1555 1555 2.35
CISPEP 1 LYS A 79 PRO A 80 0 -11.46
CISPEP 2 LYS B 79 PRO B 80 0 -11.09
SITE 1 AC1 9 ASP A 43 TYR A 65 GLN A 101 SER A 142
SITE 2 AC1 9 TYR A 175 TRP A 194 GLN A 213 HOH A 568
SITE 3 AC1 9 HOH A 572
SITE 1 AC2 9 GLN A 34 PRO A 71 PRO A 207 LYS A 233
SITE 2 AC2 9 NA A 311 NA A 312 HOH A 423 HOH A 485
SITE 3 AC2 9 HOH A 507
SITE 1 AC3 8 GLN A 82 ALA A 130 HOH A 481 HOH A 486
SITE 2 AC3 8 HOH A 487 HOH A 492 GLN B 82 ALA B 130
SITE 1 AC4 5 ARG A 69 TYR A 102 HOH A 423 HOH A 504
SITE 2 AC4 5 ARG B 87
SITE 1 AC5 9 GLY A 35 GLY A 36 LEU A 38 TYR A 102
SITE 2 AC5 9 NA A 310 HOH A 411 HOH A 420 HOH A 424
SITE 3 AC5 9 HOH A 438
SITE 1 AC6 7 PHE A 33 GLN A 34 GLY A 36 SER A 37
SITE 2 AC6 7 GLN A 119 HOH A 407 HOH A 456
SITE 1 AC7 4 TYR A 204 PRO A 207 HOH A 405 ARG B 87
SITE 1 AC8 5 ARG A 87 HOH A 434 HOH A 509 ARG B 69
SITE 2 AC8 5 TYR B 102
SITE 1 AC9 3 ARG A 70 LYS A 79 GLN A 101
SITE 1 AD1 6 GLY A 35 GLY A 36 LEU A 38 FMT A 305
SITE 2 AD1 6 HOH A 412 HOH A 418
SITE 1 AD2 6 GLN A 34 GOL A 302 NA A 312 HOH A 424
SITE 2 AD2 6 HOH A 438 HOH A 485
SITE 1 AD3 6 GLN A 34 GOL A 302 NA A 311 HOH A 485
SITE 2 AD3 6 HOH A 541 HOH A 542
SITE 1 AD4 9 ASP B 43 TYR B 65 GLN B 101 SER B 142
SITE 2 AD4 9 TYR B 175 TRP B 194 GLN B 213 HOH B 535
SITE 3 AD4 9 HOH B 546
SITE 1 AD5 8 HOH A 434 GLN B 34 PRO B 71 PRO B 207
SITE 2 AD5 8 LYS B 233 NA B 309 NA B 310 HOH B 416
SITE 1 AD6 6 TYR B 44 ALA B 45 ALA B 46 GLY B 225
SITE 2 AD6 6 ASP B 227 HOH B 509
SITE 1 AD7 6 ARG A 87 HOH A 403 HOH A 441 TYR B 204
SITE 2 AD7 6 PRO B 207 HOH B 424
SITE 1 AD8 3 ARG B 70 LYS B 79 GLN B 101
SITE 1 AD9 10 GLY B 35 GLY B 36 LEU B 38 TYR B 102
SITE 2 AD9 10 THR B 107 NA B 308 HOH B 421 HOH B 426
SITE 3 AD9 10 HOH B 430 HOH B 481
SITE 1 AE1 7 PHE B 33 GLN B 34 GLY B 36 SER B 37
SITE 2 AE1 7 GLN B 119 HOH B 417 HOH B 447
SITE 1 AE2 6 GLY B 35 GLY B 36 LEU B 38 FMT B 306
SITE 2 AE2 6 HOH B 414 HOH B 422
SITE 1 AE3 6 GLN B 34 GOL B 302 NA B 310 HOH B 426
SITE 2 AE3 6 HOH B 430 HOH B 434
SITE 1 AE4 6 GLN B 34 GOL B 302 NA B 309 HOH B 434
SITE 2 AE4 6 HOH B 479 HOH B 530
CRYST1 99.442 73.679 74.415 90.00 130.85 90.00 C 1 2 1 8
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 0.010056 0.000000 0.008695 0.00000
SCALE2 0.000000 0.013572 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017765 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
