HEADER LYASE 18-OCT-99 1D7K
TITLE CRYSTAL STRUCTURE OF HUMAN ORNITHINE DECARBOXYLASE AT 2.1 ANGSTROMS
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN ORNITHINE DECARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 4.1.1.17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET WITH N-TERMINAL (HIS)6 TAG
KEYWDS ALPHA-BETA BARREL, PYRIDOXAL 5'-PHOSPHATE, SHEET-DOMAIN,
KEYWDS 2 DECARBOXYLATION, ORNITHINE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.ALMRUD,M.A.OLIVEIRA,A.D.KERN,N.V.GRISHIN,M.A.PHILLIPS,M.L.HACKERT
REVDAT 3 31-JAN-18 1D7K 1 REMARK
REVDAT 2 24-FEB-09 1D7K 1 VERSN
REVDAT 1 25-OCT-00 1D7K 0
JRNL AUTH J.J.ALMRUD,M.A.OLIVEIRA,A.D.KERN,N.V.GRISHIN,M.A.PHILLIPS,
JRNL AUTH 2 M.L.HACKERT
JRNL TITL CRYSTAL STRUCTURE OF HUMAN ORNITHINE DECARBOXYLASE AT 2.1 A
JRNL TITL 2 RESOLUTION: STRUCTURAL INSIGHTS TO ANTIZYME BINDING.
JRNL REF J.MOL.BIOL. V. 295 7 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10623504
JRNL DOI 10.1006/JMBI.1999.3331
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 55799
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROYGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2789
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6423
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 401
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THIS STRUCTURE WAS REFINED USING DATA FROM 30-2.1 ANGSTROM
REMARK 3 RESOLUTION
REMARK 3 USING THE CCP4 SUITE PROGRAM REFMAC. THE REFMAC REFINEMENT WAS
REMARK 3 CARRIED OUT USING THE MAXIMUM LIKELIHOOD FUNCTION AND MINIMIZATION
REMARK 3 BY
REMARK 3 THE CONJUGATE DIRECTION METHOD.
REMARK 4
REMARK 4 1D7K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009862.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.908
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53656
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.36300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M NACL, 5MM DTT, 0.1M
REMARK 280 TRIS-HCL, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 16K, TEMPERATURE
REMARK 280 289.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 30.84000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.85500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.72500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.85500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.84000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.72500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 5430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLY A 302
REMARK 465 SER A 303
REMARK 465 ASP A 304
REMARK 465 ASP A 305
REMARK 465 GLU A 306
REMARK 465 ASP A 307
REMARK 465 GLU A 308
REMARK 465 SER A 309
REMARK 465 SER A 310
REMARK 465 THR B 301
REMARK 465 GLY B 302
REMARK 465 SER B 303
REMARK 465 ASP B 304
REMARK 465 ASP B 305
REMARK 465 GLU B 306
REMARK 465 ASP B 307
REMARK 465 GLU B 308
REMARK 465 ASN B 422
REMARK 465 PRO B 423
REMARK 465 ASP B 424
REMARK 465 PHE B 425
REMARK 465 PRO B 426
REMARK 465 PRO B 427
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 34 OG
REMARK 470 LEU A 363 CG CD1 CD2
REMARK 470 GLU B 30 CD OE1 OE2
REMARK 470 SER B 33 OG
REMARK 470 GLU B 106 CG CD OE1 OE2
REMARK 470 ASP B 158 CG OD1 OD2
REMARK 470 SER B 160 CB OG
REMARK 470 GLU B 182 CG CD OE1 OE2
REMARK 470 SER B 267 OG
REMARK 470 GLU B 299 CG CD OE1 OE2
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 ASP A 15 O GLU A 16 1.71
REMARK 500 O HOH B 434 O HOH B 594 2.01
REMARK 500 O HOH A 432 O HOH B 593 2.12
REMARK 500 O HOH B 506 O HOH B 594 2.17
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 ASP A 10 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 PHE A 18 C - N - CA ANGL. DEV. = 19.1 DEGREES
REMARK 500 ASP A 47 CB - CG - OD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 54 NE - CZ - NH1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 61 CD - NE - CZ ANGL. DEV. = 14.6 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ASP A 88 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 TYR A 110 CA - CB - CG ANGL. DEV. = 13.6 DEGREES
REMARK 500 THR A 132 N - CA - CB ANGL. DEV. = -16.0 DEGREES
REMARK 500 THR A 132 OG1 - CB - CG2 ANGL. DEV. = 15.9 DEGREES
REMARK 500 MET A 140 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ALA A 143 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG A 144 CD - NE - CZ ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 154 NH1 - CZ - NH2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 154 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 165 CG - CD - NE ANGL. DEV. = 13.5 DEGREES
REMARK 500 CYS A 202 CA - CB - SG ANGL. DEV. = 17.9 DEGREES
REMARK 500 PHE A 208 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 216 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 MET A 221 CA - CB - CG ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP A 233 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG A 270 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 277 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 277 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 GLU A 299 CA - CB - CG ANGL. DEV. = 18.7 DEGREES
REMARK 500 ARG A 365 CD - NE - CZ ANGL. DEV. = 16.8 DEGREES
REMARK 500 ARG A 365 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP A 371 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 MET A 381 CA - CB - CG ANGL. DEV. = 11.2 DEGREES
REMARK 500 GLN A 421 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 PHE A 425 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 PHE A 425 CB - CG - CD1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 PHE A 425 CG - CD2 - CE2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 PRO A 426 C - N - CA ANGL. DEV. = 13.1 DEGREES
REMARK 500 PRO A 426 N - CA - C ANGL. DEV. = 18.4 DEGREES
REMARK 500 ASP B 10 N - CA - CB ANGL. DEV. = 11.6 DEGREES
REMARK 500 ASP B 10 CA - CB - CG ANGL. DEV. = 17.2 DEGREES
REMARK 500 GLU B 16 CA - C - N ANGL. DEV. = 16.3 DEGREES
REMARK 500 GLU B 16 O - C - N ANGL. DEV. = -11.4 DEGREES
REMARK 500 LYS B 27 CD - CE - NZ ANGL. DEV. = 14.9 DEGREES
REMARK 500 ILE B 28 CA - CB - CG2 ANGL. DEV. = 17.0 DEGREES
REMARK 500 VAL B 31 CA - C - O ANGL. DEV. = 12.6 DEGREES
REMARK 500 SER B 34 N - CA - C ANGL. DEV. = 17.3 DEGREES
REMARK 500 ASP B 35 N - CA - CB ANGL. DEV. = 12.5 DEGREES
REMARK 500 ASP B 35 OD1 - CG - OD2 ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASP B 35 CB - CG - OD1 ANGL. DEV. = 15.5 DEGREES
REMARK 500 ASP B 38 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP B 47 CB - CG - OD2 ANGL. DEV. = 10.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 78 ANGLE DEVIATIONS.
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 GLU A 8 -44.64 -137.54
REMARK 500 PHE A 9 172.67 -55.33
REMARK 500 GLU A 16 -109.98 -42.36
REMARK 500 SER A 32 -23.78 -158.04
REMARK 500 SER A 34 83.58 34.47
REMARK 500 ASP A 35 -86.48 -74.54
REMARK 500 ASN A 71 102.26 -179.74
REMARK 500 ASP A 134 14.04 -147.67
REMARK 500 HIS A 146 61.97 -157.95
REMARK 500 ALA A 149 152.61 -49.37
REMARK 500 SER A 160 153.49 -19.14
REMARK 500 LYS A 161 -169.96 -124.70
REMARK 500 ALA A 162 -67.22 -101.35
REMARK 500 CYS A 202 119.44 -30.51
REMARK 500 ASP A 243 50.95 -98.55
REMARK 500 LEU A 297 -89.64 -79.06
REMARK 500 GLU A 299 115.46 98.06
REMARK 500 GLN A 312 -42.89 -17.61
REMARK 500 ASN A 319 39.84 -93.31
REMARK 500 PRO A 344 -168.76 -45.46
REMARK 500 PRO A 346 98.01 -40.23
REMARK 500 ASP A 347 64.56 70.09
REMARK 500 ARG A 349 112.56 80.66
REMARK 500 CYS A 360 30.92 -57.79
REMARK 500 GLU A 374 124.81 -36.85
REMARK 500 VAL A 377 134.01 -34.89
REMARK 500 THR A 390 -84.42 -122.92
REMARK 500 PRO A 423 -99.01 -60.26
REMARK 500 ASP A 424 70.73 67.96
REMARK 500 PHE A 425 -75.41 -176.26
REMARK 500 PRO A 426 -85.49 3.43
REMARK 500 SER B 34 88.36 -167.37
REMARK 500 ASP B 35 -97.63 -34.64
REMARK 500 ASP B 36 74.20 14.75
REMARK 500 LYS B 37 44.93 -105.94
REMARK 500 ASN B 71 99.11 -169.64
REMARK 500 ALA B 82 2.98 -69.77
REMARK 500 PRO B 105 -57.12 -17.02
REMARK 500 ALA B 111 51.12 -102.35
REMARK 500 ASP B 134 15.65 -159.57
REMARK 500 THR B 157 -155.25 -108.90
REMARK 500 ASP B 158 -124.45 -145.03
REMARK 500 ASP B 159 63.82 61.49
REMARK 500 SER B 160 137.60 78.72
REMARK 500 CYS B 164 108.56 -36.25
REMARK 500 SER B 167 114.16 74.07
REMARK 500 THR B 173 161.07 -27.18
REMARK 500 ASP B 243 39.68 -83.64
REMARK 500 VAL B 269 142.59 -28.84
REMARK 500 GLU B 299 100.14 97.13
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 GLU A 7 GLU A 8 149.24
REMARK 500 GLU A 16 GLY A 17 -148.01
REMARK 500 GLN A 26 LYS A 27 -146.44
REMARK 500 ASP A 35 ASP A 36 -149.47
REMARK 500 ASP A 158 ASP A 159 -117.43
REMARK 500 SER A 160 LYS A 161 -114.58
REMARK 500 LYS A 161 ALA A 162 137.64
REMARK 500 ARG A 165 LEU A 166 -143.73
REMARK 500 GLY A 201 CYS A 202 143.98
REMARK 500 LEU A 297 LYS A 298 -145.26
REMARK 500 LYS A 342 ARG A 343 -144.53
REMARK 500 ARG A 343 PRO A 344 -143.51
REMARK 500 GLN A 421 ASN A 422 -128.31
REMARK 500 ASN A 422 PRO A 423 134.32
REMARK 500 ASP A 424 PHE A 425 120.79
REMARK 500 PHE A 425 PRO A 426 -138.65
REMARK 500 SER B 34 ASP B 35 -120.27
REMARK 500 LEU B 101 GLY B 102 149.38
REMARK 500 SER B 160 LYS B 161 147.36
REMARK 500 CYS B 164 ARG B 165 148.15
REMARK 500 ARG B 165 LEU B 166 -125.73
REMARK 500 ALA B 172 THR B 173 141.09
REMARK 500 LEU B 297 LYS B 298 -123.73
REMARK 500 GLN B 341 LYS B 342 135.07
REMARK 500 LYS B 342 ARG B 343 140.47
REMARK 500 PRO B 346 ASP B 347 -98.94
REMARK 500 ASP B 347 GLU B 348 -141.44
REMARK 500 MET B 417 GLN B 418 -149.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN A 29 10.94
REMARK 500 LYS A 50 11.15
REMARK 500 GLN A 99 -11.85
REMARK 500 ALA A 124 -14.09
REMARK 500 ALA A 143 -10.97
REMARK 500 PHE A 208 -10.56
REMARK 500 ILE A 271 10.65
REMARK 500 GLU A 274 -10.21
REMARK 500 PRO B 104 -11.55
REMARK 500 SER B 241 -17.32
REMARK 500 ASP B 320 10.10
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1D7K A 7 427 UNP P11926 DCOR_HUMAN 7 427
DBREF 1D7K B 7 427 UNP P11926 DCOR_HUMAN 7 427
SEQADV 1D7K ARG A 349 UNP P11926 LYS 349 CONFLICT
SEQADV 1D7K GLN A 415 UNP P11926 GLU 415 CONFLICT
SEQADV 1D7K ARG B 349 UNP P11926 LYS 349 CONFLICT
SEQADV 1D7K GLN B 415 UNP P11926 GLU 415 CONFLICT
SEQRES 1 A 421 GLU GLU PHE ASP CYS HIS PHE LEU ASP GLU GLY PHE THR
SEQRES 2 A 421 ALA LYS ASP ILE LEU ASP GLN LYS ILE ASN GLU VAL SER
SEQRES 3 A 421 SER SER ASP ASP LYS ASP ALA PHE TYR VAL ALA ASP LEU
SEQRES 4 A 421 GLY ASP ILE LEU LYS LYS HIS LEU ARG TRP LEU LYS ALA
SEQRES 5 A 421 LEU PRO ARG VAL THR PRO PHE TYR ALA VAL LLP CYS ASN
SEQRES 6 A 421 ASP SER LYS ALA ILE VAL LYS THR LEU ALA ALA THR GLY
SEQRES 7 A 421 THR GLY PHE ASP CYS ALA SER LYS THR GLU ILE GLN LEU
SEQRES 8 A 421 VAL GLN SER LEU GLY VAL PRO PRO GLU ARG ILE ILE TYR
SEQRES 9 A 421 ALA ASN PRO CYS LYS GLN VAL SER GLN ILE LYS TYR ALA
SEQRES 10 A 421 ALA ASN ASN GLY VAL GLN MET MET THR PHE ASP SER GLU
SEQRES 11 A 421 VAL GLU LEU MET LYS VAL ALA ARG ALA HIS PRO LYS ALA
SEQRES 12 A 421 LYS LEU VAL LEU ARG ILE ALA THR ASP ASP SER LYS ALA
SEQRES 13 A 421 VAL CYS ARG LEU SER VAL LYS PHE GLY ALA THR LEU ARG
SEQRES 14 A 421 THR SER ARG LEU LEU LEU GLU ARG ALA LYS GLU LEU ASN
SEQRES 15 A 421 ILE ASP VAL VAL GLY VAL SER PHE HIS VAL GLY SER GLY
SEQRES 16 A 421 CYS THR ASP PRO GLU THR PHE VAL GLN ALA ILE SER ASP
SEQRES 17 A 421 ALA ARG CYS VAL PHE ASP MET GLY ALA GLU VAL GLY PHE
SEQRES 18 A 421 SER MET TYR LEU LEU ASP ILE GLY GLY GLY PHE PRO GLY
SEQRES 19 A 421 SER GLU ASP VAL LYS LEU LYS PHE GLU GLU ILE THR GLY
SEQRES 20 A 421 VAL ILE ASN PRO ALA LEU ASP LYS TYR PHE PRO SER ASP
SEQRES 21 A 421 SER GLY VAL ARG ILE ILE ALA GLU PRO GLY ARG TYR TYR
SEQRES 22 A 421 VAL ALA SER ALA PHE THR LEU ALA VAL ASN ILE ILE ALA
SEQRES 23 A 421 LYS LYS ILE VAL LEU LYS GLU GLN THR GLY SER ASP ASP
SEQRES 24 A 421 GLU ASP GLU SER SER GLU GLN THR PHE MET TYR TYR VAL
SEQRES 25 A 421 ASN ASP GLY VAL TYR GLY SER PHE ASN CYS ILE LEU TYR
SEQRES 26 A 421 ASP HIS ALA HIS VAL LYS PRO LEU LEU GLN LYS ARG PRO
SEQRES 27 A 421 LYS PRO ASP GLU ARG TYR TYR SER SER SER ILE TRP GLY
SEQRES 28 A 421 PRO THR CYS ASP GLY LEU ASP ARG ILE VAL GLU ARG CYS
SEQRES 29 A 421 ASP LEU PRO GLU MET HIS VAL GLY ASP TRP MET LEU PHE
SEQRES 30 A 421 GLU ASN MET GLY ALA TYR THR VAL ALA ALA ALA SER THR
SEQRES 31 A 421 PHE ASN GLY PHE GLN ARG PRO THR ILE TYR TYR VAL MET
SEQRES 32 A 421 SER GLY PRO ALA TRP GLN LEU MET GLN GLN PHE GLN ASN
SEQRES 33 A 421 PRO ASP PHE PRO PRO
SEQRES 1 B 421 GLU GLU PHE ASP CYS HIS PHE LEU ASP GLU GLY PHE THR
SEQRES 2 B 421 ALA LYS ASP ILE LEU ASP GLN LYS ILE ASN GLU VAL SER
SEQRES 3 B 421 SER SER ASP ASP LYS ASP ALA PHE TYR VAL ALA ASP LEU
SEQRES 4 B 421 GLY ASP ILE LEU LYS LYS HIS LEU ARG TRP LEU LYS ALA
SEQRES 5 B 421 LEU PRO ARG VAL THR PRO PHE TYR ALA VAL LLP CYS ASN
SEQRES 6 B 421 ASP SER LYS ALA ILE VAL LYS THR LEU ALA ALA THR GLY
SEQRES 7 B 421 THR GLY PHE ASP CYS ALA SER LYS THR GLU ILE GLN LEU
SEQRES 8 B 421 VAL GLN SER LEU GLY VAL PRO PRO GLU ARG ILE ILE TYR
SEQRES 9 B 421 ALA ASN PRO CYS LYS GLN VAL SER GLN ILE LYS TYR ALA
SEQRES 10 B 421 ALA ASN ASN GLY VAL GLN MET MET THR PHE ASP SER GLU
SEQRES 11 B 421 VAL GLU LEU MET LYS VAL ALA ARG ALA HIS PRO LYS ALA
SEQRES 12 B 421 LYS LEU VAL LEU ARG ILE ALA THR ASP ASP SER LYS ALA
SEQRES 13 B 421 VAL CYS ARG LEU SER VAL LYS PHE GLY ALA THR LEU ARG
SEQRES 14 B 421 THR SER ARG LEU LEU LEU GLU ARG ALA LYS GLU LEU ASN
SEQRES 15 B 421 ILE ASP VAL VAL GLY VAL SER PHE HIS VAL GLY SER GLY
SEQRES 16 B 421 CYS THR ASP PRO GLU THR PHE VAL GLN ALA ILE SER ASP
SEQRES 17 B 421 ALA ARG CYS VAL PHE ASP MET GLY ALA GLU VAL GLY PHE
SEQRES 18 B 421 SER MET TYR LEU LEU ASP ILE GLY GLY GLY PHE PRO GLY
SEQRES 19 B 421 SER GLU ASP VAL LYS LEU LYS PHE GLU GLU ILE THR GLY
SEQRES 20 B 421 VAL ILE ASN PRO ALA LEU ASP LYS TYR PHE PRO SER ASP
SEQRES 21 B 421 SER GLY VAL ARG ILE ILE ALA GLU PRO GLY ARG TYR TYR
SEQRES 22 B 421 VAL ALA SER ALA PHE THR LEU ALA VAL ASN ILE ILE ALA
SEQRES 23 B 421 LYS LYS ILE VAL LEU LYS GLU GLN THR GLY SER ASP ASP
SEQRES 24 B 421 GLU ASP GLU SER SER GLU GLN THR PHE MET TYR TYR VAL
SEQRES 25 B 421 ASN ASP GLY VAL TYR GLY SER PHE ASN CYS ILE LEU TYR
SEQRES 26 B 421 ASP HIS ALA HIS VAL LYS PRO LEU LEU GLN LYS ARG PRO
SEQRES 27 B 421 LYS PRO ASP GLU ARG TYR TYR SER SER SER ILE TRP GLY
SEQRES 28 B 421 PRO THR CYS ASP GLY LEU ASP ARG ILE VAL GLU ARG CYS
SEQRES 29 B 421 ASP LEU PRO GLU MET HIS VAL GLY ASP TRP MET LEU PHE
SEQRES 30 B 421 GLU ASN MET GLY ALA TYR THR VAL ALA ALA ALA SER THR
SEQRES 31 B 421 PHE ASN GLY PHE GLN ARG PRO THR ILE TYR TYR VAL MET
SEQRES 32 B 421 SER GLY PRO ALA TRP GLN LEU MET GLN GLN PHE GLN ASN
SEQRES 33 B 421 PRO ASP PHE PRO PRO
MODRES 1D7K LLP A 69 LYS
MODRES 1D7K LLP B 69 LYS
HET LLP A 69 24
HET LLP B 69 24
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP 2(C14 H22 N3 O7 P)
FORMUL 3 HOH *401(H2 O)
HELIX 1 1 THR A 19 ASN A 29 1 11
HELIX 2 2 LEU A 45 LEU A 59 1 15
HELIX 3 3 SER A 73 GLY A 84 1 12
HELIX 4 4 SER A 91 SER A 100 1 10
HELIX 5 5 PRO A 104 GLU A 106 5 3
HELIX 6 6 GLN A 116 ASN A 126 1 11
HELIX 7 7 SER A 135 HIS A 146 1 12
HELIX 8 8 THR A 173 LEU A 187 1 15
HELIX 9 9 PRO A 205 GLY A 226 1 22
HELIX 10 10 LYS A 247 PHE A 263 1 17
HELIX 11 11 PRO A 264 GLY A 268 5 5
HELIX 12 12 GLY A 276 ALA A 281 1 6
HELIX 13 13 PHE A 326 ASP A 332 1 7
HELIX 14 14 THR A 390 ALA A 394 5 5
HELIX 15 15 THR A 396 PHE A 400 5 5
HELIX 16 16 SER A 410 GLN A 421 1 12
HELIX 17 17 THR B 19 GLU B 30 1 12
HELIX 18 18 LEU B 45 LEU B 59 1 15
HELIX 19 19 SER B 73 ALA B 82 1 10
HELIX 20 20 SER B 91 SER B 100 1 10
HELIX 21 21 PRO B 104 GLU B 106 5 3
HELIX 22 22 GLN B 116 ASN B 126 1 11
HELIX 23 23 SER B 135 HIS B 146 1 12
HELIX 24 24 THR B 173 ASN B 188 1 16
HELIX 25 25 PRO B 205 GLU B 224 1 20
HELIX 26 26 LYS B 247 PHE B 263 1 17
HELIX 27 27 PRO B 264 GLY B 268 5 5
HELIX 28 28 GLY B 276 ALA B 281 1 6
HELIX 29 29 GLY B 324 PHE B 326 5 3
HELIX 30 30 ASN B 327 ASP B 332 1 6
HELIX 31 31 THR B 390 ALA B 394 5 5
HELIX 32 32 THR B 396 PHE B 400 5 5
HELIX 33 33 SER B 410 GLN B 419 1 10
SHEET 1 A 7 ARG A 365 PRO A 373 0
SHEET 2 A 7 TYR A 350 TRP A 356 -1 N TYR A 351 O LEU A 372
SHEET 3 A 7 THR A 313 VAL A 318 1 O PHE A 314 N SER A 354
SHEET 4 A 7 PHE A 284 VAL A 296 -1 N ILE A 291 O TYR A 317
SHEET 5 A 7 PHE A 40 ASP A 44 -1 O PHE A 40 N ALA A 287
SHEET 6 A 7 THR A 404 MET A 409 1 O THR A 404 N TYR A 41
SHEET 7 A 7 CYS A 11 PHE A 13 1 N HIS A 12 O TYR A 407
SHEET 1 A1 6 ARG A 365 PRO A 373 0
SHEET 2 A1 6 TYR A 350 TRP A 356 -1 N TYR A 351 O LEU A 372
SHEET 3 A1 6 THR A 313 VAL A 318 1 O PHE A 314 N SER A 354
SHEET 4 A1 6 PHE A 284 VAL A 296 -1 N ILE A 291 O TYR A 317
SHEET 5 A1 6 TRP A 380 PHE A 383 -1 N MET A 381 O VAL A 288
SHEET 6 A1 6 LEU A 339 LEU A 340 -1 O LEU A 339 N LEU A 382
SHEET 1 B 9 VAL A 62 ALA A 67 0
SHEET 2 B 9 GLY A 86 CYS A 89 1 O GLY A 86 N TYR A 66
SHEET 3 B 9 ILE A 108 TYR A 110 1 N ILE A 109 O PHE A 87
SHEET 4 B 9 MET A 130 PHE A 133 1 O MET A 130 N TYR A 110
SHEET 5 B 9 LYS A 150 ARG A 154 1 O LYS A 150 N MET A 131
SHEET 6 B 9 ASP A 190 SER A 195 1 O ASP A 190 N LEU A 151
SHEET 7 B 9 LEU A 231 ASP A 233 1 N LEU A 231 O VAL A 192
SHEET 8 B 9 ARG A 270 ALA A 273 1 O ARG A 270 N LEU A 232
SHEET 9 B 9 VAL A 62 ALA A 67 1 N THR A 63 O ILE A 271
SHEET 1 C 7 ARG B 365 PRO B 373 0
SHEET 2 C 7 TYR B 350 TRP B 356 -1 N TYR B 351 O LEU B 372
SHEET 3 C 7 THR B 313 VAL B 318 1 O PHE B 314 N SER B 354
SHEET 4 C 7 PHE B 284 VAL B 296 -1 N ILE B 291 O TYR B 317
SHEET 5 C 7 PHE B 40 ASP B 44 -1 O PHE B 40 N ALA B 287
SHEET 6 C 7 THR B 404 MET B 409 1 O THR B 404 N TYR B 41
SHEET 7 C 7 HIS B 12 PHE B 13 1 N HIS B 12 O TYR B 407
SHEET 1 C1 6 ARG B 365 PRO B 373 0
SHEET 2 C1 6 TYR B 350 TRP B 356 -1 N TYR B 351 O LEU B 372
SHEET 3 C1 6 THR B 313 VAL B 318 1 O PHE B 314 N SER B 354
SHEET 4 C1 6 PHE B 284 VAL B 296 -1 N ILE B 291 O TYR B 317
SHEET 5 C1 6 TRP B 380 PHE B 383 -1 N MET B 381 O VAL B 288
SHEET 6 C1 6 LEU B 339 LEU B 340 -1 O LEU B 339 N LEU B 382
SHEET 1 D 9 THR B 63 ALA B 67 0
SHEET 2 D 9 GLY B 86 CYS B 89 1 N GLY B 86 O PRO B 64
SHEET 3 D 9 ILE B 108 TYR B 110 1 O ILE B 109 N CYS B 89
SHEET 4 D 9 MET B 130 PHE B 133 1 O MET B 130 N TYR B 110
SHEET 5 D 9 LYS B 150 ARG B 154 1 O LYS B 150 N MET B 131
SHEET 6 D 9 VAL B 191 SER B 195 1 N VAL B 192 O LEU B 151
SHEET 7 D 9 LEU B 231 ASP B 233 1 N LEU B 231 O VAL B 192
SHEET 8 D 9 ARG B 270 ALA B 273 1 O ARG B 270 N LEU B 232
SHEET 9 D 9 THR B 63 ALA B 67 1 N THR B 63 O ILE B 271
LINK C VAL A 68 N LLP A 69 1555 1555 1.35
LINK C LLP A 69 N CYS A 70 1555 1555 1.34
LINK C VAL B 68 N LLP B 69 1555 1555 1.33
LINK C LLP B 69 N CYS B 70 1555 1555 1.34
CRYST1 61.680 107.450 139.710 90.00 90.00 90.00 P 21 21 21 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 0.016213 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009307 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007158 0.00000
(ATOM LINES ARE NOT SHOWN.)
END