HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-OCT-13 4N70
TITLE PIM1 COMPLEXED WITH A PYRIDYLCARBOXAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PIM-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 93-404;
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 DE3
KEYWDS KINASE, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.BELLAMACINA,V.LE,W.SHU,M.T.BURGER,D.BUSSIERE
REVDAT 2 02-JUL-14 4N70 1 JRNL
REVDAT 1 06-NOV-13 4N70 0
JRNL AUTH M.T.BURGER,W.HAN,J.LAN,G.NISHIGUCHI,C.BELLAMACINA,M.LINDVAL,
JRNL AUTH 2 G.ATALLAH,Y.DING,M.MATHUR,C.MCBRIDE,E.L.BEANS,K.MULLER,
JRNL AUTH 3 V.TAMEZ,Y.ZHANG,K.HUH,P.FEUCHT,T.ZAVOROTINSKAYA,Y.DAI,
JRNL AUTH 4 J.HOLASH,J.CASTILLO,J.LANGOWSKI,Y.WANG,M.Y.CHEN,P.D.GARCIA
JRNL TITL STRUCTURE GUIDED OPTIMIZATION, IN VITRO ACTIVITY, AND IN
JRNL TITL 2 VIVO ACTIVITY OF PAN-PIM KINASE INHIBITORS.
JRNL REF ACS MED CHEM LETT V. 4 1193 2013
JRNL REFN ISSN 1948-5875
JRNL PMID 24900629
JRNL DOI 10.1021/ML400307J
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25888
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1317
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 42.4222 - 4.3668 0.99 2784 133 0.1643 0.1908
REMARK 3 2 4.3668 - 3.4665 1.00 2735 162 0.1467 0.1854
REMARK 3 3 3.4665 - 3.0285 1.00 2712 152 0.1691 0.2214
REMARK 3 4 3.0285 - 2.7516 1.00 2722 156 0.1669 0.2251
REMARK 3 5 2.7516 - 2.5544 1.00 2716 156 0.1566 0.2069
REMARK 3 6 2.5544 - 2.4039 1.00 2717 136 0.1516 0.2035
REMARK 3 7 2.4039 - 2.2835 1.00 2731 133 0.1521 0.1920
REMARK 3 8 2.2835 - 2.1841 1.00 2694 150 0.1725 0.2087
REMARK 3 9 2.1841 - 2.1000 1.00 2760 139 0.1868 0.2291
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 57.77
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.060
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.32840
REMARK 3 B22 (A**2) : 3.32840
REMARK 3 B33 (A**2) : -6.65670
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.014 4530
REMARK 3 ANGLE : 1.370 8165
REMARK 3 CHIRALITY : 0.103 336
REMARK 3 PLANARITY : 0.008 690
REMARK 3 DIHEDRAL : 15.966 1141
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4N70 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB082831.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 160.0
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25905
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 42.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 0.0890
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.47100
REMARK 200 R SYM FOR SHELL (I) : 0.19100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR SOLUTION - 0.7M (NH4)2HPO4,
REMARK 280 0.3M NACL, 0.1M NACITRATE, PH 5.5, PROTEIN SOLUTION - 7.5MG/ML IN
REMARK 280 20MM HEPES, 100MM NACL, 5MM DTT, PH 8, COMPOUND WAS SOAKED IN,
REMARK 280 TEMPERATURE 298.0K, VAPOR DIFFUSION, HANGING DROP
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 54.05333
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 27.02667
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 40.54000
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 13.51333
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 67.56667
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: 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 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 -14
REMARK 465 ALA A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 LEU A -6
REMARK 465 GLU A -5
REMARK 465 VAL A -4
REMARK 465 LEU A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 PRO A 1
REMARK 465 LEU A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 ILE A 6
REMARK 465 ASN A 7
REMARK 465 SER A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 HIS A 11
REMARK 465 LEU A 12
REMARK 465 ARG A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 CYS A 17
REMARK 465 ASN A 18
REMARK 465 ASP A 19
REMARK 465 LEU A 20
REMARK 465 HIS A 21
REMARK 465 ALA A 22
REMARK 465 THR A 23
REMARK 465 LYS A 24
REMARK 465 LEU A 25
REMARK 465 ALA A 26
REMARK 465 PRO A 27
REMARK 465 GLY A 28
REMARK 465 LYS A 29
REMARK 465 GLU A 30
REMARK 465 LYS A 31
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 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 GLU A 32 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 NH2 ARG A 258 O HOH A 539 2.09
REMARK 500 NH1 ARG A 258 O HOH A 608 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 O HOH A 585 O HOH A 548 2664 2.10
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 112 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 61 18.62 58.06
REMARK 500 ASN A 82 24.51 -77.90
REMARK 500 SER A 98 -144.28 -143.00
REMARK 500 ASP A 167 45.37 -146.17
REMARK 500 ASP A 186 80.83 64.36
REMARK 500 ASP A 202 33.23 -140.37
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 2HX A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N6Y RELATED DB: PDB
REMARK 900 PIM1 COMPLEXED WITH A PHENYLCARBOXAMIDE
REMARK 900 RELATED ID: 4N6Z RELATED DB: PDB
REMARK 900 PIM1 COMPLEXED WITH A PYRIDYLCARBOXAMIDE
DBREF 4N70 A 2 313 UNP P11309 PIM1_HUMAN 93 404
SEQADV 4N70 MET A -14 UNP P11309 EXPRESSION TAG
SEQADV 4N70 ALA A -13 UNP P11309 EXPRESSION TAG
SEQADV 4N70 HIS A -12 UNP P11309 EXPRESSION TAG
SEQADV 4N70 HIS A -11 UNP P11309 EXPRESSION TAG
SEQADV 4N70 HIS A -10 UNP P11309 EXPRESSION TAG
SEQADV 4N70 HIS A -9 UNP P11309 EXPRESSION TAG
SEQADV 4N70 HIS A -8 UNP P11309 EXPRESSION TAG
SEQADV 4N70 HIS A -7 UNP P11309 EXPRESSION TAG
SEQADV 4N70 LEU A -6 UNP P11309 EXPRESSION TAG
SEQADV 4N70 GLU A -5 UNP P11309 EXPRESSION TAG
SEQADV 4N70 VAL A -4 UNP P11309 EXPRESSION TAG
SEQADV 4N70 LEU A -3 UNP P11309 EXPRESSION TAG
SEQADV 4N70 PHE A -2 UNP P11309 EXPRESSION TAG
SEQADV 4N70 GLN A -1 UNP P11309 EXPRESSION TAG
SEQADV 4N70 GLY A 0 UNP P11309 EXPRESSION TAG
SEQADV 4N70 PRO A 1 UNP P11309 EXPRESSION TAG
SEQRES 1 A 328 MET ALA HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE
SEQRES 2 A 328 GLN GLY PRO LEU LEU SER LYS ILE ASN SER LEU ALA HIS
SEQRES 3 A 328 LEU ARG ALA ALA PRO CYS ASN ASP LEU HIS ALA THR LYS
SEQRES 4 A 328 LEU ALA PRO GLY LYS GLU LYS GLU PRO LEU GLU SER GLN
SEQRES 5 A 328 TYR GLN VAL GLY PRO LEU LEU GLY SER GLY GLY PHE GLY
SEQRES 6 A 328 SER VAL TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO
SEQRES 7 A 328 VAL ALA ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP
SEQRES 8 A 328 TRP GLY GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU
SEQRES 9 A 328 VAL VAL LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY
SEQRES 10 A 328 VAL ILE ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER
SEQRES 11 A 328 PHE VAL LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP
SEQRES 12 A 328 LEU PHE ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU
SEQRES 13 A 328 GLU LEU ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA
SEQRES 14 A 328 VAL ARG HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP
SEQRES 15 A 328 ILE LYS ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY
SEQRES 16 A 328 GLU LEU LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU
SEQRES 17 A 328 LYS ASP THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL
SEQRES 18 A 328 TYR SER PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS
SEQRES 19 A 328 GLY ARG SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU
SEQRES 20 A 328 TYR ASP MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP
SEQRES 21 A 328 GLU GLU ILE ILE ARG GLY GLN VAL PHE PHE ARG GLN ARG
SEQRES 22 A 328 VAL SER SEP GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU
SEQRES 23 A 328 ALA LEU ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE
SEQRES 24 A 328 GLN ASN HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN
SEQRES 25 A 328 GLU THR ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY
SEQRES 26 A 328 PRO SER LYS
MODRES 4N70 SEP A 261 SER PHOSPHOSERINE
HET SEP A 261 10
HET 2HX A 401 33
HETNAM SEP PHOSPHOSERINE
HETNAM 2HX N-{4-[(3R,4R,5S)-3-AMINO-4-HYDROXY-5-METHYLPIPERIDIN-1-
HETNAM 2 2HX YL]PYRIDIN-3-YL}-6-(2,6-DIFLUOROPHENYL)-5-
HETNAM 3 2HX FLUOROPYRIDINE-2-CARBOXAMIDE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 2HX C23 H22 F3 N5 O2
FORMUL 3 HOH *234(H2 O)
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 GLY A 47 0
SHEET 2 A 5 GLY A 50 ARG A 57 -1 O VAL A 52 N GLY A 45
SHEET 3 A 5 PRO A 63 GLU A 70 -1 O HIS A 68 N SER A 51
SHEET 4 A 5 SER A 115 GLU A 121 -1 O LEU A 118 N LYS A 67
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 GLU A 181 N ASP A 176
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 1.33
LINK C SEP A 261 N GLU A 262 1555 1555 1.32
CISPEP 1 GLU A 124 PRO A 125 0 0.61
SITE 1 AC1 18 LEU A 44 PHE A 49 ALA A 65 LYS A 67
SITE 2 AC1 18 ILE A 104 LEU A 120 GLU A 121 ARG A 122
SITE 3 AC1 18 PRO A 123 VAL A 126 ASP A 128 GLU A 171
SITE 4 AC1 18 LEU A 174 ILE A 185 ASP A 186 HOH A 525
SITE 5 AC1 18 HOH A 549 HOH A 715
CRYST1 97.950 97.950 81.080 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 0.010209 0.005894 0.000000 0.00000
SCALE2 0.000000 0.011789 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012333 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
