HEADER SIGNALING PROTEIN 12-SEP-14 4RBL
TITLE CRYSTAL STRUCTURE OF SER/THR KINASE PIM1 IN COMPLEX WITH MITOXANTRONE
TITLE 2 DERIVATIVES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PIM-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PIM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS KINASE, PHOSPHORYLATION, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.ZHANG,X.WAN,N.HUANG
REVDAT 2 20-SEP-23 4RBL 1 REMARK SEQADV LINK
REVDAT 1 18-MAR-15 4RBL 0
JRNL AUTH W.ZHANG,X.WAN,N.HUANG
JRNL TITL CRYSTAL STRUCTURE OF SER/THR KINASE PIM1 IN COMPLEX WITH
JRNL TITL 2 MITOXANTRONE DERIVATIVES
JRNL REF TO BE PUBLISHED 2014
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 13779
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 730
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 995
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 59
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2224
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.332
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.260
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.184
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.639
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2294 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2143 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3115 ; 1.798 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4916 ; 0.856 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 268 ; 6.815 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;37.140 ;23.136
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 379 ;17.506 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;19.164 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 330 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2571 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 560 ; 0.001 ; 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): 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4RBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000087142.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97622
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13779
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 12.30
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.76500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.07700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1YWV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4 M POTASSIUM SODIUM, TARTRATE
REMARK 280 TETRAHYDRATE, PH 9.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 53.54600
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 26.77300
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 40.15950
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 13.38650
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 66.93250
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 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 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 25
REMARK 465 PRO A 26
REMARK 465 HIS A 27
REMARK 465 MET A 28
REMARK 465 LYS A 29
REMARK 465 GLU A 30
REMARK 465 LYS A 31
REMARK 465 GLU A 32
REMARK 465 GLY A 48
REMARK 465 SER A 306
REMARK 465 LEU A 307
REMARK 465 SER A 308
REMARK 465 PRO A 309
REMARK 465 GLY A 310
REMARK 465 PRO A 311
REMARK 465 SER A 312
REMARK 465 LYS A 313
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 112 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -3.9 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 SER A 46 158.80 174.14
REMARK 500 SER A 59 -48.23 -22.79
REMARK 500 PRO A 81 -89.20 -30.43
REMARK 500 ASN A 82 -16.75 -34.23
REMARK 500 SER A 101 -162.99 173.88
REMARK 500 ASP A 167 43.30 -142.41
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 3O7 A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4I41 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MITOXANTRONE
DBREF 4RBL A 29 313 UNP P11309 PIM1_HUMAN 120 404
SEQADV 4RBL GLY A 25 UNP P11309 EXPRESSION TAG
SEQADV 4RBL PRO A 26 UNP P11309 EXPRESSION TAG
SEQADV 4RBL HIS A 27 UNP P11309 EXPRESSION TAG
SEQADV 4RBL MET A 28 UNP P11309 EXPRESSION TAG
SEQRES 1 A 289 GLY PRO HIS MET LYS GLU LYS GLU PRO LEU GLU SER GLN
SEQRES 2 A 289 TYR GLN VAL GLY PRO LEU LEU GLY SER GLY GLY PHE GLY
SEQRES 3 A 289 SER VAL TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO
SEQRES 4 A 289 VAL ALA ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP
SEQRES 5 A 289 TRP GLY GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU
SEQRES 6 A 289 VAL VAL LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY
SEQRES 7 A 289 VAL ILE ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER
SEQRES 8 A 289 PHE VAL LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP
SEQRES 9 A 289 LEU PHE ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU
SEQRES 10 A 289 GLU LEU ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA
SEQRES 11 A 289 VAL ARG HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP
SEQRES 12 A 289 ILE LYS ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY
SEQRES 13 A 289 GLU LEU LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU
SEQRES 14 A 289 LYS ASP THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL
SEQRES 15 A 289 TYR SER PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS
SEQRES 16 A 289 GLY ARG SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU
SEQRES 17 A 289 TYR ASP MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP
SEQRES 18 A 289 GLU GLU ILE ILE ARG GLY GLN VAL PHE PHE ARG GLN ARG
SEQRES 19 A 289 VAL SER SEP GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU
SEQRES 20 A 289 ALA LEU ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE
SEQRES 21 A 289 GLN ASN HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN
SEQRES 22 A 289 GLU THR ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY
SEQRES 23 A 289 PRO SER LYS
MODRES 4RBL SEP A 261 SER PHOSPHOSERINE
HET SEP A 261 10
HET 3O7 A 401 20
HETNAM SEP PHOSPHOSERINE
HETNAM 3O7 1,4,5,8-TETRAHYDROXYANTHRACENE-9,10-DIONE
HETSYN SEP PHOSPHONOSERINE
HETSYN 3O7 1,4,5,8-TETRAHYDROXY ANTHRAQUINONE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 3O7 C14 H8 O6
HELIX 1 1 PRO A 33 GLN A 37 1 5
HELIX 2 2 ASP A 72 ILE A 74 5 3
HELIX 3 3 MET A 88 SER A 97 1 10
HELIX 4 4 LEU A 129 GLY A 137 1 9
HELIX 5 5 GLN A 140 CYS A 161 1 22
HELIX 6 6 LYS A 169 GLU A 171 5 3
HELIX 7 7 THR A 204 SER A 208 5 5
HELIX 8 8 PRO A 209 HIS A 216 1 8
HELIX 9 9 HIS A 219 GLY A 238 1 20
HELIX 10 10 HIS A 244 GLY A 251 1 8
HELIX 11 11 SER A 260 LEU A 271 1 12
HELIX 12 12 ARG A 274 ARG A 278 5 5
HELIX 13 13 THR A 280 ASN A 286 1 7
HELIX 14 14 HIS A 287 GLN A 291 5 5
HELIX 15 15 LEU A 295 LEU A 304 1 10
SHEET 1 A 5 TYR A 38 SER A 46 0
SHEET 2 A 5 SER A 51 ARG A 57 -1 O SER A 54 N PRO A 42
SHEET 3 A 5 PRO A 63 GLU A 70 -1 O ILE A 66 N TYR A 53
SHEET 4 A 5 SER A 115 GLU A 121 -1 O LEU A 120 N ALA A 65
SHEET 5 A 5 LEU A 106 GLU A 111 -1 N ASP A 108 O ILE A 119
SHEET 1 B 2 TRP A 77 GLU A 79 0
SHEET 2 B 2 ARG A 85 PRO A 87 -1 O VAL A 86 N GLY A 78
SHEET 1 C 3 VAL A 126 ASP A 128 0
SHEET 2 C 3 ILE A 173 ASP A 176 -1 O ILE A 175 N GLN A 127
SHEET 3 C 3 GLU A 181 LEU A 184 -1 O LYS A 183 N LEU A 174
SHEET 1 D 2 VAL A 163 LEU A 164 0
SHEET 2 D 2 ALA A 191 LEU A 192 -1 O ALA A 191 N LEU A 164
LINK C SER A 260 N SEP A 261 1555 1555 1.31
LINK C SEP A 261 N GLU A 262 1555 1555 1.31
CISPEP 1 SER A 46 GLY A 47 0 0.02
CISPEP 2 GLU A 124 PRO A 125 0 -3.05
SITE 1 AC1 7 PHE A 49 LYS A 67 ILE A 104 LEU A 120
SITE 2 AC1 7 GLU A 121 ILE A 185 ASP A 186
CRYST1 98.418 98.418 80.319 90.00 90.00 120.00 P 65 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 0.010161 0.005866 0.000000 0.00000
SCALE2 0.000000 0.011733 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012450 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
