HEADER TRANSFERASE/PEPTIDE 10-FEB-12 4AIM
TITLE CRYSTAL STRUCTURE OF C. CRESCENTUS PNPASE BOUND TO RNASE E RECOGNITION
TITLE 2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POLYNUCLEOTIDE PHOSPHORYLASE, PNPASE;
COMPND 5 EC: 2.7.7.8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RIBONUCLEASE, RNE/RNG FAMILY PROTEIN;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: PNPASE BINDING PEPTIDE - GWW, RESIDUES 885-898;
COMPND 11 SYNONYM: RNASE E;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAULOBACTER VIBRIOIDES;
SOURCE 3 ORGANISM_TAXID: 190650;
SOURCE 4 STRAIN: CB15;
SOURCE 5 ATCC: 19089;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: CAULOBACTER VIBRIOIDES;
SOURCE 12 ORGANISM_COMMON: CAULOBACTER CRESCENTUS;
SOURCE 13 ORGANISM_TAXID: 155892
KEYWDS TRANSFERASE-PEPTIDE COMPLEX, KH DOMAIN, S1 DOMAIN, GWW PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.W.HARDWICK,T.GUBBEY,I.HUG,U.JENAL,B.F.LUISI
REVDAT 4 20-DEC-23 4AIM 1 REMARK
REVDAT 3 05-FEB-14 4AIM 1 SOURCE JRNL
REVDAT 2 04-JUL-12 4AIM 1 JRNL
REVDAT 1 18-APR-12 4AIM 0
JRNL AUTH S.W.HARDWICK,T.GUBBEY,I.HUG,U.JENAL,B.F.LUISI
JRNL TITL CRYSTAL STRUCTURE OF CAULOBACTER CRESCENTUS POLYNUCLEOTIDE
JRNL TITL 2 PHOSPHORYLASE REVEALS A MECHANISM OF RNA SUBSTRATE
JRNL TITL 3 CHANNELLING AND RNA DEGRADOSOME ASSEMBLY.
JRNL REF OPEN BIOL. V. 2 20028 2012
JRNL REFN ESSN 2046-2441
JRNL PMID 22724061
JRNL DOI 10.1098/RSOB.120028
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 14616
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 771
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) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1038
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4950
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 2
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 96.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.04000
REMARK 3 B12 (A**2) : -0.01000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.510
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.420
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.049
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5038 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6874 ; 1.703 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 704 ; 7.095 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;36.982 ;24.611
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 701 ;19.755 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;19.221 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 814 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3850 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
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 : A 623 A 697
REMARK 3 ORIGIN FOR THE GROUP (A): -37.4778 -6.7915 100.0420
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.7689
REMARK 3 T33: 0.2034 T12: 0.0126
REMARK 3 T13: -0.0258 T23: -0.2520
REMARK 3 L TENSOR
REMARK 3 L11: 9.0218 L22: 21.9036
REMARK 3 L33: 9.0839 L12: 7.5120
REMARK 3 L13: -4.7778 L23: -14.1048
REMARK 3 S TENSOR
REMARK 3 S11: 1.0108 S12: -0.0410 S13: -0.3593
REMARK 3 S21: 1.1125 S22: -0.3024 S23: 1.0630
REMARK 3 S31: -0.7110 S32: 0.1594 S33: -0.7085
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 4AIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1290051258.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9778
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15391
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 ENTRY 3GME
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17 % WT/V PEG 3000, 0.1 M TRI-SODIUM
REMARK 280 CITRATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 95.95500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 95.95500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 95.95500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 86990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.9 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 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
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 -13
REMARK 465 GLY A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 GLN A -2
REMARK 465 GLU A 697
REMARK 465 THR A 698
REMARK 465 GLY A 699
REMARK 465 GLU A 700
REMARK 465 ASP A 701
REMARK 465 LEU A 702
REMARK 465 SER A 703
REMARK 465 LYS A 704
REMARK 465 LYS A 705
REMARK 465 GLU A 706
REMARK 465 ALA A 707
REMARK 465 ALA A 708
REMARK 465 ALA A 709
REMARK 465 GLU A 710
REMARK 465 GLU A 711
REMARK 465 ALA A 712
REMARK 465 THR C 885
REMARK 465 ALA C 886
REMARK 465 PRO C 887
REMARK 465 PRO C 888
REMARK 465 GLU C 889
REMARK 465 ARG C 898
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 SER A -1 OG
REMARK 470 ARG A 6 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 7 CG CD CE NZ
REMARK 470 LYS A 14 CG CD CE NZ
REMARK 470 ARG A 83 CD NE CZ NH1 NH2
REMARK 470 LYS A 105 CD CE NZ
REMARK 470 LYS A 171 CD CE NZ
REMARK 470 GLU A 172 CG CD OE1 OE2
REMARK 470 ASP A 221 CG OD1 OD2
REMARK 470 LYS A 242 CG CD CE NZ
REMARK 470 LYS A 244 CG CD CE NZ
REMARK 470 MET A 245 CG SD CE
REMARK 470 LYS A 246 CG CD CE NZ
REMARK 470 LEU A 248 CG CD1 CD2
REMARK 470 LYS A 258 CG CD CE NZ
REMARK 470 GLN A 260 CG CD OE1 NE2
REMARK 470 LYS A 261 CG CD CE NZ
REMARK 470 LYS A 262 CG CD CE NZ
REMARK 470 GLN A 263 CG CD OE1 NE2
REMARK 470 ASP A 264 CG OD1 OD2
REMARK 470 ARG A 265 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 267 CG CD OE1 OE2
REMARK 470 LYS A 273 CG CD CE NZ
REMARK 470 LYS A 274 CG CD CE NZ
REMARK 470 LYS A 275 CG CD CE NZ
REMARK 470 ILE A 277 CG1 CG2 CD1
REMARK 470 LEU A 282 CG CD1 CD2
REMARK 470 GLU A 285 CG CD OE1 OE2
REMARK 470 ASN A 286 CG OD1 ND2
REMARK 470 TYR A 290 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 293 CG CD1 CD2
REMARK 470 LYS A 294 CG CD CE NZ
REMARK 470 LEU A 295 CG CD1 CD2
REMARK 470 ILE A 298 CG1 CG2 CD1
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 LYS A 324 CG CD CE NZ
REMARK 470 ARG A 394 NE CZ NH1 NH2
REMARK 470 LYS A 420 CG CD CE NZ
REMARK 470 GLU A 421 CG CD OE1 OE2
REMARK 470 LEU A 459 CG CD1 CD2
REMARK 470 GLN A 474 CG CD OE1 NE2
REMARK 470 HIS A 489 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 496 CD CE NZ
REMARK 470 LYS A 512 CD CE NZ
REMARK 470 GLU A 522 CG CD OE1 OE2
REMARK 470 LYS A 529 CG CD CE NZ
REMARK 470 GLU A 530 CG CD OE1 OE2
REMARK 470 ASP A 552 CG OD1 OD2
REMARK 470 LYS A 556 CG CD CE NZ
REMARK 470 ILE A 557 CG1 CG2 CD1
REMARK 470 GLU A 558 CG CD OE1 OE2
REMARK 470 LYS A 566 CG CD CE NZ
REMARK 470 ILE A 567 CG1 CG2 CD1
REMARK 470 ARG A 568 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 571 CG1 CG2 CD1
REMARK 470 LYS A 576 CG CD CE NZ
REMARK 470 ILE A 578 CG1 CG2 CD1
REMARK 470 ARG A 579 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 580 CG CD OE1 OE2
REMARK 470 ILE A 581 CG1 CG2 CD1
REMARK 470 VAL A 582 CG1 CG2
REMARK 470 LYS A 588 CG CD CE NZ
REMARK 470 ASP A 590 CG OD1 OD2
REMARK 470 ASP A 594 CG OD1 OD2
REMARK 470 VAL A 596 CG1 CG2
REMARK 470 LYS A 598 CG CD CE NZ
REMARK 470 VAL A 599 CG1 CG2
REMARK 470 ASP A 603 CG OD1 OD2
REMARK 470 LYS A 606 CG CD CE NZ
REMARK 470 ILE A 607 CG1 CG2 CD1
REMARK 470 LYS A 608 CG CD CE NZ
REMARK 470 ILE A 611 CG1 CG2 CD1
REMARK 470 ILE A 614 CG1 CG2 CD1
REMARK 470 LYS A 615 CG CD CE NZ
REMARK 470 GLU A 620 CG CD OE1 OE2
REMARK 470 GLU A 622 CG CD OE1 OE2
REMARK 470 ILE A 623 CG1 CG2 CD1
REMARK 470 LYS A 625 CG CD CE NZ
REMARK 470 ILE A 626 CG1 CG2 CD1
REMARK 470 ASP A 628 CG OD1 OD2
REMARK 470 LYS A 630 CG CD CE NZ
REMARK 470 LYS A 633 CG CD CE NZ
REMARK 470 PHE A 644 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 647 CD CE NZ
REMARK 470 VAL A 653 CG1 CG2
REMARK 470 GLN A 655 CG CD OE1 NE2
REMARK 470 GLU A 659 CG CD OE1 OE2
REMARK 470 ARG A 660 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 663 CG CD CE NZ
REMARK 470 ASP A 666 CG OD1 OD2
REMARK 470 VAL A 667 CG1 CG2
REMARK 470 LEU A 668 CG CD1 CD2
REMARK 470 LYS A 669 CG CD CE NZ
REMARK 470 GLU A 670 CG CD OE1 OE2
REMARK 470 MET A 673 CG SD CE
REMARK 470 LYS A 675 CG CD CE NZ
REMARK 470 LYS A 677 CG CD CE NZ
REMARK 470 LEU A 679 CG CD1 CD2
REMARK 470 ASP A 682 CG OD1 OD2
REMARK 470 ASP A 683 CG OD1 OD2
REMARK 470 ARG A 684 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 686 CG CD CE NZ
REMARK 470 LYS A 688 CG CD CE NZ
REMARK 470 LYS A 692 CD CE NZ
REMARK 470 LYS C 890 CG CD CE NZ
REMARK 470 ARG C 897 O 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 ASN A 206 OE1 GLN A 210 2.05
REMARK 500 O ILE A 656 CE MET A 691 2.07
REMARK 500 O VAL A 635 N PHE A 637 2.09
REMARK 500 O ALA A 646 N ASP A 648 2.11
REMARK 500 O GLY A 281 N SER A 283 2.13
REMARK 500 O ALA A 639 CD1 LEU A 650 2.13
REMARK 500 O LYS A 556 O ALA A 601 2.14
REMARK 500 O LYS A 246 N GLY A 250 2.15
REMARK 500 OH TYR A 161 O ILE A 200 2.15
REMARK 500 O VAL A 635 N GLY A 638 2.15
REMARK 500 OD1 ASP A 368 CG2 THR A 373 2.18
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 NE2 GLN A 119 O PRO A 337 3555 1.99
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 MET A 1 122.17 67.31
REMARK 500 ILE A 4 113.94 101.26
REMARK 500 LYS A 5 117.79 164.59
REMARK 500 THR A 8 167.82 -44.57
REMARK 500 ILE A 9 90.17 87.14
REMARK 500 THR A 20 -158.61 -129.40
REMARK 500 ALA A 30 86.09 -152.17
REMARK 500 PRO A 52 -87.37 -42.54
REMARK 500 LYS A 79 9.02 50.00
REMARK 500 VAL A 104 127.40 -28.73
REMARK 500 LEU A 122 14.83 52.17
REMARK 500 GLU A 123 -60.76 -127.99
REMARK 500 ASP A 158 -60.61 62.76
REMARK 500 THR A 166 172.42 -57.81
REMARK 500 THR A 182 -168.63 -102.79
REMARK 500 ALA A 226 -36.59 172.83
REMARK 500 PRO A 235 102.42 -50.01
REMARK 500 ASP A 239 -58.78 -28.10
REMARK 500 ALA A 255 46.25 -109.13
REMARK 500 ALA A 256 -59.91 -137.56
REMARK 500 ILE A 259 100.80 -55.59
REMARK 500 GLN A 263 -106.79 -55.74
REMARK 500 VAL A 269 -79.46 -49.43
REMARK 500 ALA A 271 -85.71 -50.83
REMARK 500 ALA A 272 -69.53 -21.19
REMARK 500 LYS A 273 -92.18 -27.80
REMARK 500 LYS A 274 -75.22 -34.52
REMARK 500 LYS A 275 -73.34 -29.08
REMARK 500 ILE A 277 -49.99 -28.87
REMARK 500 ALA A 278 -101.06 -58.27
REMARK 500 ALA A 279 93.92 -31.91
REMARK 500 LEU A 280 130.09 75.10
REMARK 500 LEU A 282 -44.04 57.43
REMARK 500 SER A 283 161.95 71.91
REMARK 500 ASP A 284 79.51 38.72
REMARK 500 GLU A 285 -76.36 -65.39
REMARK 500 ASN A 286 47.76 160.72
REMARK 500 PRO A 287 -80.50 -2.21
REMARK 500 LEU A 293 -79.04 -66.53
REMARK 500 ALA A 297 -52.11 -27.32
REMARK 500 THR A 314 115.94 71.86
REMARK 500 VAL A 323 -27.46 -35.65
REMARK 500 GLU A 332 119.22 -177.01
REMARK 500 LEU A 336 89.11 57.64
REMARK 500 PRO A 337 -161.88 -72.19
REMARK 500 ARG A 338 -39.30 71.70
REMARK 500 HIS A 340 -29.83 -37.45
REMARK 500 ILE A 367 75.55 -113.42
REMARK 500 ASP A 368 80.09 -58.74
REMARK 500 LEU A 379 76.99 -115.65
REMARK 500
REMARK 500 THIS ENTRY HAS 111 RAMACHANDRAN OUTLIERS.
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 ILE A 9 GLU A 10 147.33
REMARK 500 ALA A 554 PRO A 555 -148.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1697
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4AID RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF C. CRESCENTUS PNPASE BOUND TO RNASE E
REMARK 900 RECOGNITION PEPTIDE
DBREF 4AIM A 1 712 UNP Q9AC32 PNP_CAUCR 1 712
DBREF 4AIM C 885 898 UNP Q9A749 Q9A749_CAUCR 885 898
SEQADV 4AIM MET A -13 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM GLY A -12 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM SER A -11 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM SER A -10 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM HIS A -9 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM HIS A -8 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM HIS A -7 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM HIS A -6 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM HIS A -5 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM HIS A -4 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM SER A -3 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM GLN A -2 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM SER A -1 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM PRO A 0 UNP Q9AC32 EXPRESSION TAG
SEQADV 4AIM ILE A 623 UNP Q9AC32 VAL 623 CONFLICT
SEQRES 1 A 726 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN SER
SEQRES 2 A 726 PRO MET PHE ASP ILE LYS ARG LYS THR ILE GLU TRP GLY
SEQRES 3 A 726 GLY LYS THR LEU VAL LEU GLU THR GLY ARG ILE ALA ARG
SEQRES 4 A 726 GLN ALA ASP GLY ALA VAL LEU ALA THR MET GLY GLU THR
SEQRES 5 A 726 VAL VAL LEU ALA THR ALA VAL PHE ALA LYS SER GLN LYS
SEQRES 6 A 726 PRO GLY GLN ASP PHE PHE PRO LEU THR VAL ASN TYR GLN
SEQRES 7 A 726 GLU LYS THR PHE ALA ALA GLY LYS ILE PRO GLY GLY PHE
SEQRES 8 A 726 PHE LYS ARG GLU GLY ARG PRO SER GLU LYS GLU THR LEU
SEQRES 9 A 726 VAL SER ARG LEU ILE ASP ARG PRO ILE ARG PRO LEU PHE
SEQRES 10 A 726 VAL LYS GLY PHE LYS ASN GLU VAL GLN VAL VAL VAL THR
SEQRES 11 A 726 VAL LEU GLN HIS ASP LEU GLU ASN ASP PRO ASP ILE LEU
SEQRES 12 A 726 GLY MET VAL ALA ALA SER ALA ALA LEU CYS LEU SER GLY
SEQRES 13 A 726 ALA PRO PHE MET GLY PRO ILE GLY ALA ALA ARG VAL GLY
SEQRES 14 A 726 TRP VAL ASP GLY ALA TYR VAL LEU ASN PRO THR LEU ASP
SEQRES 15 A 726 GLU MET LYS GLU SER LYS MET ASP LEU VAL VAL ALA GLY
SEQRES 16 A 726 THR ALA ASP ALA VAL MET MET VAL GLU SER GLU ILE GLN
SEQRES 17 A 726 GLU LEU SER GLU GLU ILE VAL LEU GLY GLY VAL ASN PHE
SEQRES 18 A 726 ALA HIS GLN GLN MET GLN ALA VAL ILE ASP ALA ILE ILE
SEQRES 19 A 726 ASP LEU ALA GLU HIS ALA ALA LYS GLU PRO PHE ALA PHE
SEQRES 20 A 726 GLU PRO GLU ASP THR ASP ALA ILE LYS ALA LYS MET LYS
SEQRES 21 A 726 ASP LEU VAL GLY ALA ASP ILE ALA ALA ALA TYR LYS ILE
SEQRES 22 A 726 GLN LYS LYS GLN ASP ARG TYR GLU ALA VAL GLY ALA ALA
SEQRES 23 A 726 LYS LYS LYS ALA ILE ALA ALA LEU GLY LEU SER ASP GLU
SEQRES 24 A 726 ASN PRO THR GLY TYR ASP PRO LEU LYS LEU GLY ALA ILE
SEQRES 25 A 726 PHE LYS GLU LEU GLU ALA ASP VAL VAL ARG ARG GLY ILE
SEQRES 26 A 726 LEU ASP THR GLY LEU ARG ILE ASP GLY ARG ASP VAL LYS
SEQRES 27 A 726 THR VAL ARG PRO ILE LEU GLY GLU VAL GLY ILE LEU PRO
SEQRES 28 A 726 ARG THR HIS GLY SER ALA LEU PHE THR ARG GLY GLU THR
SEQRES 29 A 726 GLN ALA ILE VAL VAL ALA THR LEU GLY THR GLY ASP ASP
SEQRES 30 A 726 GLU GLN PHE ILE ASP ALA LEU GLU GLY THR TYR LYS GLU
SEQRES 31 A 726 SER PHE LEU LEU HIS TYR ASN PHE PRO PRO TYR SER VAL
SEQRES 32 A 726 GLY GLU THR GLY ARG MET GLY SER PRO GLY ARG ARG GLU
SEQRES 33 A 726 ILE GLY HIS GLY LYS LEU ALA TRP ARG ALA LEU ARG PRO
SEQRES 34 A 726 MET LEU PRO THR LYS GLU ASP PHE PRO TYR THR ILE ARG
SEQRES 35 A 726 LEU VAL SER GLU ILE THR GLU SER ASN GLY SER SER SER
SEQRES 36 A 726 MET ALA THR VAL CYS GLY SER SER LEU ALA MET MET ASP
SEQRES 37 A 726 ALA GLY VAL PRO LEU VAL ARG PRO VAL SER GLY ILE ALA
SEQRES 38 A 726 MET GLY LEU ILE LEU GLU GLN ASP GLY PHE ALA VAL LEU
SEQRES 39 A 726 SER ASP ILE LEU GLY ASP GLU ASP HIS LEU GLY ASP MET
SEQRES 40 A 726 ASP PHE LYS VAL ALA GLY THR SER GLU GLY LEU THR SER
SEQRES 41 A 726 LEU GLN MET ASP ILE LYS ILE ALA GLY ILE THR PRO ALA
SEQRES 42 A 726 ILE MET GLU GLN ALA LEU ALA GLN ALA LYS GLU GLY ARG
SEQRES 43 A 726 ALA HIS ILE LEU GLY GLU MET ASN LYS ALA MET ASP ALA
SEQRES 44 A 726 PRO ARG ALA ASP VAL GLY ASP PHE ALA PRO LYS ILE GLU
SEQRES 45 A 726 THR ILE ASN ILE PRO THR ASP LYS ILE ARG GLU VAL ILE
SEQRES 46 A 726 GLY SER GLY GLY LYS VAL ILE ARG GLU ILE VAL ALA THR
SEQRES 47 A 726 THR GLY ALA LYS VAL ASP ILE ASN ASP ASP GLY VAL VAL
SEQRES 48 A 726 LYS VAL SER ALA SER ASP GLY ALA LYS ILE LYS ALA ALA
SEQRES 49 A 726 ILE ASP TRP ILE LYS SER ILE THR ASP GLU ALA GLU ILE
SEQRES 50 A 726 GLY LYS ILE TYR ASP GLY LYS VAL VAL LYS VAL VAL ASP
SEQRES 51 A 726 PHE GLY ALA PHE VAL ASN PHE PHE GLY ALA LYS ASP GLY
SEQRES 52 A 726 LEU VAL HIS VAL SER GLN ILE SER ASN GLU ARG VAL ALA
SEQRES 53 A 726 LYS PRO SER ASP VAL LEU LYS GLU GLY GLN MET VAL LYS
SEQRES 54 A 726 VAL LYS LEU LEU GLY PHE ASP ASP ARG GLY LYS THR LYS
SEQRES 55 A 726 LEU SER MET LYS VAL VAL ASP GLN GLU THR GLY GLU ASP
SEQRES 56 A 726 LEU SER LYS LYS GLU ALA ALA ALA GLU GLU ALA
SEQRES 1 C 14 THR ALA PRO PRO GLU LYS PRO ARG ARG GLY TRP TRP ARG
SEQRES 2 C 14 ARG
HET PO4 A1697 5
HETNAM PO4 PHOSPHATE ION
FORMUL 3 PO4 O4 P 3-
FORMUL 4 HOH *2(H2 O)
HELIX 1 1 THR A 67 GLY A 71 5 5
HELIX 2 2 SER A 85 ARG A 100 1 16
HELIX 3 3 ASP A 125 GLY A 142 1 18
HELIX 4 4 THR A 166 GLU A 172 1 7
HELIX 5 5 SER A 197 HIS A 225 1 29
HELIX 6 6 THR A 238 GLY A 250 1 13
HELIX 7 7 LYS A 261 ALA A 279 1 19
HELIX 8 8 LYS A 294 ASP A 313 1 20
HELIX 9 9 PRO A 385 GLY A 390 5 6
HELIX 10 10 GLY A 399 ARG A 411 1 13
HELIX 11 11 SER A 439 GLY A 456 1 18
HELIX 12 12 LEU A 484 HIS A 489 1 6
HELIX 13 13 THR A 517 LYS A 541 1 25
HELIX 14 14 PRO A 563 ASP A 565 5 3
HELIX 15 15 LYS A 566 GLY A 572 1 7
HELIX 16 16 GLY A 575 GLY A 586 1 12
HELIX 17 17 ASP A 603 ASP A 619 1 17
SHEET 1 AA 6 GLU A 10 TRP A 11 0
SHEET 2 AA 6 LYS A 14 GLU A 19 -1 O LYS A 14 N TRP A 11
SHEET 3 AA 6 GLY A 29 MET A 35 -1 O LEU A 32 N GLU A 19
SHEET 4 AA 6 THR A 38 PHE A 46 -1 O THR A 38 N MET A 35
SHEET 5 AA 6 VAL A 111 GLN A 119 -1 O GLN A 112 N VAL A 45
SHEET 6 AA 6 LEU A 59 GLU A 65 1 O THR A 60 N VAL A 113
SHEET 1 AB 7 ALA A 160 LEU A 163 0
SHEET 2 AB 7 GLY A 150 VAL A 157 -1 O GLY A 155 N VAL A 162
SHEET 3 AB 7 MET A 175 GLY A 181 -1 O LEU A 177 N VAL A 154
SHEET 4 AB 7 VAL A 186 ILE A 193 -1 N MET A 187 O ALA A 180
SHEET 5 AB 7 GLY A 503 ILE A 511 -1 O THR A 505 N ILE A 193
SHEET 6 AB 7 MET A 493 THR A 500 -1 O ASP A 494 N ASP A 510
SHEET 7 AB 7 SER A 464 GLY A 469 -1 O SER A 464 N GLY A 499
SHEET 1 AC 2 ILE A 329 LEU A 330 0
SHEET 2 AC 2 THR A 346 ARG A 347 -1 O THR A 346 N LEU A 330
SHEET 1 AD 4 GLY A 341 ALA A 343 0
SHEET 2 AD 4 ALA A 352 ALA A 356 -1 O VAL A 354 N ALA A 343
SHEET 3 AD 4 VAL A 430 ILE A 433 -1 O VAL A 430 N VAL A 355
SHEET 4 AD 4 HIS A 381 ASN A 383 1 O HIS A 381 N SER A 431
SHEET 1 AE 2 GLN A 365 ILE A 367 0
SHEET 2 AE 2 TYR A 374 GLU A 376 -1 O TYR A 374 N ILE A 367
SHEET 1 AF 2 ILE A 471 LEU A 472 0
SHEET 2 AF 2 PHE A 477 ALA A 478 -1 O ALA A 478 N ILE A 471
SHEET 1 AG 3 LYS A 556 ASN A 561 0
SHEET 2 AG 3 VAL A 596 ALA A 601 -1 O VAL A 597 N ILE A 560
SHEET 3 AG 3 LYS A 588 ASP A 590 -1 O LYS A 588 N SER A 600
SHEET 1 AH 5 GLY A 649 HIS A 652 0
SHEET 2 AH 5 GLY A 638 ASN A 642 -1 O ALA A 639 N VAL A 651
SHEET 3 AH 5 TYR A 627 VAL A 635 -1 O LYS A 630 N ASN A 642
SHEET 4 AH 5 MET A 673 GLY A 680 -1 O VAL A 674 N GLY A 629
SHEET 5 AH 5 LYS A 688 SER A 690 -1 O LYS A 688 N GLY A 680
CISPEP 1 ASP A 3 ILE A 4 0 -12.75
CISPEP 2 SER A 283 ASP A 284 0 -8.63
CISPEP 3 ASP A 284 GLU A 285 0 -4.32
CISPEP 4 GLU A 285 ASN A 286 0 -4.95
CISPEP 5 THR A 288 GLY A 289 0 3.67
CISPEP 6 PHE A 553 ALA A 554 0 13.03
CISPEP 7 LYS A 556 ILE A 557 0 -7.83
CISPEP 8 ASP A 590 ILE A 591 0 -0.96
CISPEP 9 ALA A 621 GLU A 622 0 -5.02
CISPEP 10 GLU A 622 ILE A 623 0 -4.71
CISPEP 11 GLY A 624 LYS A 625 0 -3.23
CISPEP 12 ASP A 683 ARG A 684 0 -4.54
CISPEP 13 VAL A 693 VAL A 694 0 9.04
CISPEP 14 VAL A 694 ASP A 695 0 -0.73
CISPEP 15 ARG C 893 GLY C 894 0 13.09
CISPEP 16 TRP C 896 ARG C 897 0 7.24
SITE 1 AC1 4 ARG A 401 HIS A 405 SER A 436 GLY A 438
CRYST1 97.329 97.329 191.910 90.00 90.00 120.00 P 63 6
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 0.010274 0.005932 0.000000 0.00000
SCALE2 0.000000 0.011864 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005211 0.00000
(ATOM LINES ARE NOT SHOWN.)
END