HEADER TRANSFERASE INHIBITOR 16-SEP-13 4MQU
TITLE HUMAN GKRP COMPLEXED TO AMG-3969 AND S6P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOKINASE REGULATORY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLUCOKINASE REGULATOR;
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 GENE: GCKR;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS SIS DOMAINS, REGULATORY PROTEIN, BINDS FRUCTOSE PHOSPHATES AND
KEYWDS 2 GLUCOKINASE, TRANSFERASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.ST JEAN,K.S.ASHTON,M.D.BARTBERGER,J.CHEN,S.CHMAIT,R.CUPPLES,
AUTHOR 2 E.GALBREATH,J.HELMERING,S.R.JORDAN,L.LIU
REVDAT 3 03-APR-24 4MQU 1 REMARK
REVDAT 2 28-FEB-24 4MQU 1 REMARK SEQADV HETSYN
REVDAT 1 07-MAY-14 4MQU 0
JRNL AUTH D.J.ST JEAN,K.S.ASHTON,M.D.BARTBERGER,J.CHEN,S.CHMAIT,
JRNL AUTH 2 R.CUPPLES,E.GALBREATH,J.HELMERING,F.T.HONG,S.R.JORDAN,L.LIU,
JRNL AUTH 3 R.K.KUNZ,K.MICHELSEN,N.NISHIMURA,L.D.PENNINGTON,S.F.POON,
JRNL AUTH 4 D.REID,G.SIVITS,M.M.STEC,S.TADESSE,N.TAMAYO,G.VAN,K.C.YANG,
JRNL AUTH 5 J.ZHANG,M.H.NORMAN,C.FOTSCH,D.J.LLOYD,C.HALE
JRNL TITL SMALL MOLECULE DISRUPTORS OF THE GLUCOKINASE-GLUCOKINASE
JRNL TITL 2 REGULATORY PROTEIN INTERACTION: 2. LEVERAGING
JRNL TITL 3 STRUCTURE-BASED DRUG DESIGN TO IDENTIFY ANALOGUES WITH
JRNL TITL 4 IMPROVED PHARMACOKINETIC PROFILES.
JRNL REF J.MED.CHEM. V. 57 325 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 24405213
JRNL DOI 10.1021/JM4016747
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.2
REMARK 3 NUMBER OF REFLECTIONS : 58853
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3101
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) : 2.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1306
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 22.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.4070
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.4840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9075
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 148
REMARK 3 SOLVENT ATOMS : 233
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.46
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) : 0.05000
REMARK 3 B12 (A**2) : -0.02000
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): 0.354
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.275
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.181
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.408
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9361 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9159 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12683 ; 1.758 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): 21016 ; 0.873 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1169 ; 6.921 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 376 ;35.676 ;24.415
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1658 ;18.108 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;19.888 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1489 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10380 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2038 ; 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): 4694 ; 3.551 ; 4.410
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4693 ; 3.550 ; 4.410
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5857 ; 5.268 ; 6.603
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5858 ; 5.268 ; 6.603
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4667 ; 3.643 ; 4.704
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4655 ; 3.556 ; 4.701
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6809 ; 5.411 ; 6.934
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10882 ; 7.602 ;35.039
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10883 ; 7.602 ;35.040
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 4MQU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : CONFOCAL MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58853
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 35.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: INTERNAL STRUCTURES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL BUFFER: 0.1M BIS-TRIS, 0.2M NAI,
REMARK 280 16% PEG 8K, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 88.30867
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 44.15433
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 66.23150
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 22.07717
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 110.38583
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -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 ASP A -3
REMARK 465 GLU A -2
REMARK 465 VAL A -1
REMARK 465 ASP A 0
REMARK 465 ALA A 67
REMARK 465 LEU A 68
REMARK 465 GLY A 366
REMARK 465 ASP A 367
REMARK 465 HIS A 368
REMARK 465 SER A 369
REMARK 465 ASP A 370
REMARK 465 MET A 371
REMARK 465 PHE A 372
REMARK 465 ASN A 373
REMARK 465 GLN A 374
REMARK 465 LYS A 375
REMARK 465 ALA A 376
REMARK 465 GLU A 377
REMARK 465 LEU A 378
REMARK 465 THR A 379
REMARK 465 ASN A 380
REMARK 465 GLN A 381
REMARK 465 GLY A 382
REMARK 465 PRO A 383
REMARK 465 GLN A 384
REMARK 465 GLY A 607
REMARK 465 PRO A 608
REMARK 465 GLY A 609
REMARK 465 GLN A 610
REMARK 465 LYS A 611
REMARK 465 ARG A 612
REMARK 465 THR A 613
REMARK 465 ALA A 614
REMARK 465 ASP A 615
REMARK 465 PRO A 616
REMARK 465 LEU A 617
REMARK 465 GLU A 618
REMARK 465 ILE A 619
REMARK 465 LEU A 620
REMARK 465 GLU A 621
REMARK 465 PRO A 622
REMARK 465 ASP A 623
REMARK 465 VAL A 624
REMARK 465 GLN A 625
REMARK 465 MET B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 ASP B -3
REMARK 465 GLU B -2
REMARK 465 VAL B -1
REMARK 465 ASP B 0
REMARK 465 ALA B 67
REMARK 465 LEU B 68
REMARK 465 ASP B 367
REMARK 465 HIS B 368
REMARK 465 SER B 369
REMARK 465 ASP B 370
REMARK 465 MET B 371
REMARK 465 PHE B 372
REMARK 465 ASN B 373
REMARK 465 GLN B 374
REMARK 465 LYS B 375
REMARK 465 ALA B 376
REMARK 465 GLU B 377
REMARK 465 LEU B 378
REMARK 465 THR B 379
REMARK 465 ASN B 380
REMARK 465 GLY B 607
REMARK 465 PRO B 608
REMARK 465 GLY B 609
REMARK 465 GLN B 610
REMARK 465 LYS B 611
REMARK 465 ARG B 612
REMARK 465 THR B 613
REMARK 465 ALA B 614
REMARK 465 ASP B 615
REMARK 465 PRO B 616
REMARK 465 LEU B 617
REMARK 465 GLU B 618
REMARK 465 ILE B 619
REMARK 465 LEU B 620
REMARK 465 GLU B 621
REMARK 465 PRO B 622
REMARK 465 ASP B 623
REMARK 465 VAL B 624
REMARK 465 GLN B 625
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 LEU A 449 N LYS A 451 2.15
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 361 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 478 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 6 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 227 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 259 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG B 259 NE - CZ - NH2 ANGL. DEV. = -5.3 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 ALA A 168 -127.68 30.77
REMARK 500 SER A 183 -33.31 -135.31
REMARK 500 MET A 260 -102.65 -81.20
REMARK 500 GLN A 309 30.34 -78.46
REMARK 500 LYS A 326 -92.79 -76.65
REMARK 500 LYS A 327 37.51 -171.13
REMARK 500 GLN A 336 -136.76 31.03
REMARK 500 THR A 386 69.68 -103.22
REMARK 500 ASN A 415 71.27 104.08
REMARK 500 THR A 430 -72.90 -98.95
REMARK 500 ASN A 431 -44.44 82.62
REMARK 500 PRO A 446 153.12 -48.31
REMARK 500 ILE A 447 97.85 63.43
REMARK 500 LYS A 450 71.34 -63.89
REMARK 500 LYS A 451 66.49 -170.58
REMARK 500 LEU A 452 -91.10 39.57
REMARK 500 ILE A 456 156.90 -28.46
REMARK 500 PRO A 462 170.47 -40.09
REMARK 500 GLN A 502 -110.15 51.64
REMARK 500 LEU A 548 95.25 -66.78
REMARK 500 SER B 183 -38.33 -130.23
REMARK 500 MET B 260 -105.32 -84.98
REMARK 500 LYS B 279 -39.00 -38.69
REMARK 500 GLN B 336 -140.47 58.61
REMARK 500 ASN B 415 82.14 -58.02
REMARK 500 PRO B 446 131.29 -37.64
REMARK 500 PRO B 448 106.02 4.49
REMARK 500 PHE B 453 77.95 -117.38
REMARK 500 SER B 455 45.24 -106.71
REMARK 500 LEU B 464 135.61 -170.77
REMARK 500 GLN B 502 -102.14 62.74
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 MG9 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S6P A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG9 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S6P B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 714
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 716
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 717
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 718
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 719
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MRO RELATED DB: PDB
DBREF 4MQU A 1 625 UNP Q14397 GCKR_HUMAN 1 625
DBREF 4MQU B 1 625 UNP Q14397 GCKR_HUMAN 1 625
SEQADV 4MQU MET A -10 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS A -9 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS A -8 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS A -7 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS A -6 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS A -5 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS A -4 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU ASP A -3 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU GLU A -2 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU VAL A -1 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU ASP A 0 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU MET B -10 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS B -9 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS B -8 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS B -7 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS B -6 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS B -5 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU HIS B -4 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU ASP B -3 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU GLU B -2 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU VAL B -1 UNP Q14397 EXPRESSION TAG
SEQADV 4MQU ASP B 0 UNP Q14397 EXPRESSION TAG
SEQRES 1 A 636 MET HIS HIS HIS HIS HIS HIS ASP GLU VAL ASP MET PRO
SEQRES 2 A 636 GLY THR LYS ARG PHE GLN HIS VAL ILE GLU THR PRO GLU
SEQRES 3 A 636 PRO GLY LYS TRP GLU LEU SER GLY TYR GLU ALA ALA VAL
SEQRES 4 A 636 PRO ILE THR GLU LYS SER ASN PRO LEU THR GLN ASP LEU
SEQRES 5 A 636 ASP LYS ALA ASP ALA GLU ASN ILE VAL ARG LEU LEU GLY
SEQRES 6 A 636 GLN CYS ASP ALA GLU ILE PHE GLN GLU GLU GLY GLN ALA
SEQRES 7 A 636 LEU SER THR TYR GLN ARG LEU TYR SER GLU SER ILE LEU
SEQRES 8 A 636 THR THR MET VAL GLN VAL ALA GLY LYS VAL GLN GLU VAL
SEQRES 9 A 636 LEU LYS GLU PRO ASP GLY GLY LEU VAL VAL LEU SER GLY
SEQRES 10 A 636 GLY GLY THR SER GLY ARG MET ALA PHE LEU MET SER VAL
SEQRES 11 A 636 SER PHE ASN GLN LEU MET LYS GLY LEU GLY GLN LYS PRO
SEQRES 12 A 636 LEU TYR THR TYR LEU ILE ALA GLY GLY ASP ARG SER VAL
SEQRES 13 A 636 VAL ALA SER ARG GLU GLY THR GLU ASP SER ALA LEU HIS
SEQRES 14 A 636 GLY ILE GLU GLU LEU LYS LYS VAL ALA ALA GLY LYS LYS
SEQRES 15 A 636 ARG VAL ILE VAL ILE GLY ILE SER VAL GLY LEU SER ALA
SEQRES 16 A 636 PRO PHE VAL ALA GLY GLN MET ASP CYS CYS MET ASN ASN
SEQRES 17 A 636 THR ALA VAL PHE LEU PRO VAL LEU VAL GLY PHE ASN PRO
SEQRES 18 A 636 VAL SER MET ALA ARG ASN ASP PRO ILE GLU ASP TRP SER
SEQRES 19 A 636 SER THR PHE ARG GLN VAL ALA GLU ARG MET GLN LYS MET
SEQRES 20 A 636 GLN GLU LYS GLN LYS ALA PHE VAL LEU ASN PRO ALA ILE
SEQRES 21 A 636 GLY PRO GLU GLY LEU SER GLY SER SER ARG MET LYS GLY
SEQRES 22 A 636 GLY SER ALA THR LYS ILE LEU LEU GLU THR LEU LEU LEU
SEQRES 23 A 636 ALA ALA HIS LYS THR VAL ASP GLN GLY ILE ALA ALA SER
SEQRES 24 A 636 GLN ARG CYS LEU LEU GLU ILE LEU ARG THR PHE GLU ARG
SEQRES 25 A 636 ALA HIS GLN VAL THR TYR SER GLN SER PRO LYS ILE ALA
SEQRES 26 A 636 THR LEU MET LYS SER VAL SER THR SER LEU GLU LYS LYS
SEQRES 27 A 636 GLY HIS VAL TYR LEU VAL GLY TRP GLN THR LEU GLY ILE
SEQRES 28 A 636 ILE ALA ILE MET ASP GLY VAL GLU CYS ILE HIS THR PHE
SEQRES 29 A 636 GLY ALA ASP PHE ARG ASP VAL ARG GLY PHE LEU ILE GLY
SEQRES 30 A 636 ASP HIS SER ASP MET PHE ASN GLN LYS ALA GLU LEU THR
SEQRES 31 A 636 ASN GLN GLY PRO GLN PHE THR PHE SER GLN GLU ASP PHE
SEQRES 32 A 636 LEU THR SER ILE LEU PRO SER LEU THR GLU ILE ASP THR
SEQRES 33 A 636 VAL VAL PHE ILE PHE THR LEU ASP ASP ASN LEU THR GLU
SEQRES 34 A 636 VAL GLN THR ILE VAL GLU GLN VAL LYS GLU LYS THR ASN
SEQRES 35 A 636 HIS ILE GLN ALA LEU ALA HIS SER THR VAL GLY GLN THR
SEQRES 36 A 636 LEU PRO ILE PRO LEU LYS LYS LEU PHE PRO SER ILE ILE
SEQRES 37 A 636 SER ILE THR TRP PRO LEU LEU PHE PHE GLU TYR GLU GLY
SEQRES 38 A 636 ASN PHE ILE GLN LYS PHE GLN ARG GLU LEU SER THR LYS
SEQRES 39 A 636 TRP VAL LEU ASN THR VAL SER THR GLY ALA HIS VAL LEU
SEQRES 40 A 636 LEU GLY LYS ILE LEU GLN ASN HIS MET LEU ASP LEU ARG
SEQRES 41 A 636 ILE SER ASN SER LYS LEU PHE TRP ARG ALA LEU ALA MET
SEQRES 42 A 636 LEU GLN ARG PHE SER GLY GLN SER LYS ALA ARG CYS ILE
SEQRES 43 A 636 GLU SER LEU LEU ARG ALA ILE HIS PHE PRO GLN PRO LEU
SEQRES 44 A 636 SER ASP ASP ILE ARG ALA ALA PRO ILE SER CYS HIS VAL
SEQRES 45 A 636 GLN VAL ALA HIS GLU LYS GLU GLN VAL ILE PRO ILE ALA
SEQRES 46 A 636 LEU LEU SER LEU LEU PHE ARG CYS SER ILE THR GLU ALA
SEQRES 47 A 636 GLN ALA HIS LEU ALA ALA ALA PRO SER VAL CYS GLU ALA
SEQRES 48 A 636 VAL ARG SER ALA LEU ALA GLY PRO GLY GLN LYS ARG THR
SEQRES 49 A 636 ALA ASP PRO LEU GLU ILE LEU GLU PRO ASP VAL GLN
SEQRES 1 B 636 MET HIS HIS HIS HIS HIS HIS ASP GLU VAL ASP MET PRO
SEQRES 2 B 636 GLY THR LYS ARG PHE GLN HIS VAL ILE GLU THR PRO GLU
SEQRES 3 B 636 PRO GLY LYS TRP GLU LEU SER GLY TYR GLU ALA ALA VAL
SEQRES 4 B 636 PRO ILE THR GLU LYS SER ASN PRO LEU THR GLN ASP LEU
SEQRES 5 B 636 ASP LYS ALA ASP ALA GLU ASN ILE VAL ARG LEU LEU GLY
SEQRES 6 B 636 GLN CYS ASP ALA GLU ILE PHE GLN GLU GLU GLY GLN ALA
SEQRES 7 B 636 LEU SER THR TYR GLN ARG LEU TYR SER GLU SER ILE LEU
SEQRES 8 B 636 THR THR MET VAL GLN VAL ALA GLY LYS VAL GLN GLU VAL
SEQRES 9 B 636 LEU LYS GLU PRO ASP GLY GLY LEU VAL VAL LEU SER GLY
SEQRES 10 B 636 GLY GLY THR SER GLY ARG MET ALA PHE LEU MET SER VAL
SEQRES 11 B 636 SER PHE ASN GLN LEU MET LYS GLY LEU GLY GLN LYS PRO
SEQRES 12 B 636 LEU TYR THR TYR LEU ILE ALA GLY GLY ASP ARG SER VAL
SEQRES 13 B 636 VAL ALA SER ARG GLU GLY THR GLU ASP SER ALA LEU HIS
SEQRES 14 B 636 GLY ILE GLU GLU LEU LYS LYS VAL ALA ALA GLY LYS LYS
SEQRES 15 B 636 ARG VAL ILE VAL ILE GLY ILE SER VAL GLY LEU SER ALA
SEQRES 16 B 636 PRO PHE VAL ALA GLY GLN MET ASP CYS CYS MET ASN ASN
SEQRES 17 B 636 THR ALA VAL PHE LEU PRO VAL LEU VAL GLY PHE ASN PRO
SEQRES 18 B 636 VAL SER MET ALA ARG ASN ASP PRO ILE GLU ASP TRP SER
SEQRES 19 B 636 SER THR PHE ARG GLN VAL ALA GLU ARG MET GLN LYS MET
SEQRES 20 B 636 GLN GLU LYS GLN LYS ALA PHE VAL LEU ASN PRO ALA ILE
SEQRES 21 B 636 GLY PRO GLU GLY LEU SER GLY SER SER ARG MET LYS GLY
SEQRES 22 B 636 GLY SER ALA THR LYS ILE LEU LEU GLU THR LEU LEU LEU
SEQRES 23 B 636 ALA ALA HIS LYS THR VAL ASP GLN GLY ILE ALA ALA SER
SEQRES 24 B 636 GLN ARG CYS LEU LEU GLU ILE LEU ARG THR PHE GLU ARG
SEQRES 25 B 636 ALA HIS GLN VAL THR TYR SER GLN SER PRO LYS ILE ALA
SEQRES 26 B 636 THR LEU MET LYS SER VAL SER THR SER LEU GLU LYS LYS
SEQRES 27 B 636 GLY HIS VAL TYR LEU VAL GLY TRP GLN THR LEU GLY ILE
SEQRES 28 B 636 ILE ALA ILE MET ASP GLY VAL GLU CYS ILE HIS THR PHE
SEQRES 29 B 636 GLY ALA ASP PHE ARG ASP VAL ARG GLY PHE LEU ILE GLY
SEQRES 30 B 636 ASP HIS SER ASP MET PHE ASN GLN LYS ALA GLU LEU THR
SEQRES 31 B 636 ASN GLN GLY PRO GLN PHE THR PHE SER GLN GLU ASP PHE
SEQRES 32 B 636 LEU THR SER ILE LEU PRO SER LEU THR GLU ILE ASP THR
SEQRES 33 B 636 VAL VAL PHE ILE PHE THR LEU ASP ASP ASN LEU THR GLU
SEQRES 34 B 636 VAL GLN THR ILE VAL GLU GLN VAL LYS GLU LYS THR ASN
SEQRES 35 B 636 HIS ILE GLN ALA LEU ALA HIS SER THR VAL GLY GLN THR
SEQRES 36 B 636 LEU PRO ILE PRO LEU LYS LYS LEU PHE PRO SER ILE ILE
SEQRES 37 B 636 SER ILE THR TRP PRO LEU LEU PHE PHE GLU TYR GLU GLY
SEQRES 38 B 636 ASN PHE ILE GLN LYS PHE GLN ARG GLU LEU SER THR LYS
SEQRES 39 B 636 TRP VAL LEU ASN THR VAL SER THR GLY ALA HIS VAL LEU
SEQRES 40 B 636 LEU GLY LYS ILE LEU GLN ASN HIS MET LEU ASP LEU ARG
SEQRES 41 B 636 ILE SER ASN SER LYS LEU PHE TRP ARG ALA LEU ALA MET
SEQRES 42 B 636 LEU GLN ARG PHE SER GLY GLN SER LYS ALA ARG CYS ILE
SEQRES 43 B 636 GLU SER LEU LEU ARG ALA ILE HIS PHE PRO GLN PRO LEU
SEQRES 44 B 636 SER ASP ASP ILE ARG ALA ALA PRO ILE SER CYS HIS VAL
SEQRES 45 B 636 GLN VAL ALA HIS GLU LYS GLU GLN VAL ILE PRO ILE ALA
SEQRES 46 B 636 LEU LEU SER LEU LEU PHE ARG CYS SER ILE THR GLU ALA
SEQRES 47 B 636 GLN ALA HIS LEU ALA ALA ALA PRO SER VAL CYS GLU ALA
SEQRES 48 B 636 VAL ARG SER ALA LEU ALA GLY PRO GLY GLN LYS ARG THR
SEQRES 49 B 636 ALA ASP PRO LEU GLU ILE LEU GLU PRO ASP VAL GLN
HET MG9 A 701 35
HET S6P A 702 16
HET IOD A 703 1
HET IOD A 704 1
HET IOD A 705 1
HET IOD A 706 1
HET IOD A 707 1
HET IOD A 708 1
HET IOD A 709 1
HET IOD A 710 1
HET IOD A 711 1
HET IOD A 712 1
HET IOD A 713 1
HET IOD A 714 1
HET MG9 B 701 35
HET S6P B 702 16
HET IOD B 703 1
HET IOD B 704 1
HET IOD B 705 1
HET IOD B 706 1
HET IOD B 707 1
HET IOD B 708 1
HET IOD B 709 1
HET IOD B 710 1
HET IOD B 711 1
HET IOD B 712 1
HET IOD B 713 1
HET IOD B 714 1
HET IOD B 715 1
HET GOL B 716 6
HET SO4 B 717 5
HET SO4 B 718 5
HET SO4 B 719 5
HETNAM MG9 2-{4-[(2S)-4-[(6-AMINOPYRIDIN-3-YL)SULFONYL]-2-(PROP-1-
HETNAM 2 MG9 YN-1-YL)PIPERAZIN-1-YL]PHENYL}-1,1,1,3,3,3-
HETNAM 3 MG9 HEXAFLUOROPROPAN-2-OL
HETNAM S6P D-SORBITOL-6-PHOSPHATE
HETNAM IOD IODIDE ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN MG9 AMG-3969
HETSYN S6P 1-O-PHOSPHONO-D-GLUCITOL; D-GLUCITOL-6-PHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MG9 2(C21 H20 F6 N4 O3 S)
FORMUL 4 S6P 2(C6 H15 O9 P)
FORMUL 5 IOD 25(I 1-)
FORMUL 32 GOL C3 H8 O3
FORMUL 33 SO4 3(O4 S 2-)
FORMUL 36 HOH *233(H2 O)
HELIX 1 1 GLY A 3 GLN A 8 1 6
HELIX 2 2 TYR A 24 VAL A 28 5 5
HELIX 3 3 PRO A 29 LYS A 33 5 5
HELIX 4 4 ASN A 35 GLN A 39 5 5
HELIX 5 5 ASP A 45 GLU A 59 1 15
HELIX 6 6 ILE A 60 GLN A 62 5 3
HELIX 7 7 SER A 76 GLU A 96 1 21
HELIX 8 8 GLY A 107 LEU A 128 1 22
HELIX 9 9 GLY A 141 ALA A 147 5 7
HELIX 10 10 ARG A 149 ASP A 154 5 6
HELIX 11 11 SER A 155 ALA A 167 1 13
HELIX 12 12 ALA A 184 ASN A 197 1 14
HELIX 13 13 PRO A 210 ALA A 214 5 5
HELIX 14 14 THR A 225 GLU A 238 1 14
HELIX 15 15 MET A 260 ASP A 282 1 23
HELIX 16 16 SER A 288 GLN A 309 1 22
HELIX 17 17 GLN A 309 LYS A 327 1 19
HELIX 18 18 TRP A 335 GLY A 354 1 20
HELIX 19 19 SER A 388 ILE A 396 1 9
HELIX 20 20 LEU A 397 LEU A 400 5 4
HELIX 21 21 ASN A 415 THR A 430 1 16
HELIX 22 22 ASN A 471 LEU A 497 1 27
HELIX 23 23 ASN A 512 GLY A 528 1 17
HELIX 24 24 SER A 530 PHE A 544 1 15
HELIX 25 25 SER A 549 ALA A 555 1 7
HELIX 26 26 PRO A 556 HIS A 565 1 10
HELIX 27 27 GLN A 569 PHE A 580 1 12
HELIX 28 28 SER A 583 ALA A 592 1 10
HELIX 29 29 SER A 596 LEU A 605 1 10
HELIX 30 30 GLY B 3 GLN B 8 1 6
HELIX 31 31 TYR B 24 VAL B 28 5 5
HELIX 32 32 PRO B 29 LYS B 33 5 5
HELIX 33 33 ASN B 35 GLN B 39 5 5
HELIX 34 34 ASP B 40 ALA B 44 5 5
HELIX 35 35 ASP B 45 GLU B 59 1 15
HELIX 36 36 ILE B 60 GLN B 62 5 3
HELIX 37 37 SER B 76 GLU B 96 1 21
HELIX 38 38 GLY B 107 GLY B 127 1 21
HELIX 39 39 GLY B 141 ALA B 147 5 7
HELIX 40 40 ARG B 149 ASP B 154 5 6
HELIX 41 41 SER B 155 ALA B 168 1 14
HELIX 42 42 ALA B 184 ASN B 197 1 14
HELIX 43 43 PRO B 210 ALA B 214 5 5
HELIX 44 44 THR B 225 GLU B 238 1 14
HELIX 45 45 MET B 260 THR B 280 1 21
HELIX 46 46 GLN B 283 SER B 308 1 26
HELIX 47 47 GLN B 309 LYS B 326 1 18
HELIX 48 48 TRP B 335 GLY B 354 1 20
HELIX 49 49 SER B 388 ILE B 396 1 9
HELIX 50 50 LEU B 397 LEU B 400 5 4
HELIX 51 51 ASN B 415 THR B 430 1 16
HELIX 52 52 ASN B 471 LEU B 497 1 27
HELIX 53 53 ASN B 512 GLY B 528 1 17
HELIX 54 54 SER B 530 PHE B 544 1 15
HELIX 55 55 SER B 549 ALA B 554 1 6
HELIX 56 56 PRO B 556 HIS B 565 1 10
HELIX 57 57 GLN B 569 ARG B 581 1 13
HELIX 58 58 SER B 583 ALA B 594 1 12
HELIX 59 59 SER B 596 ALA B 606 1 11
SHEET 1 A 5 TYR A 134 ILE A 138 0
SHEET 2 A 5 GLY A 100 GLY A 106 1 N LEU A 104 O THR A 135
SHEET 3 A 5 ARG A 172 ILE A 178 1 O ILE A 178 N SER A 105
SHEET 4 A 5 PHE A 201 VAL A 206 1 O LEU A 202 N VAL A 175
SHEET 5 A 5 PHE A 243 LEU A 245 1 O LEU A 245 N LEU A 205
SHEET 1 B 5 ARG A 361 LEU A 364 0
SHEET 2 B 5 VAL A 330 GLY A 334 1 N VAL A 330 O ARG A 361
SHEET 3 B 5 THR A 405 THR A 411 1 O VAL A 407 N VAL A 333
SHEET 4 B 5 ILE A 433 THR A 440 1 O LEU A 436 N PHE A 408
SHEET 5 B 5 ILE A 457 TRP A 461 1 O ILE A 459 N ALA A 437
SHEET 1 C 5 TYR B 134 ILE B 138 0
SHEET 2 C 5 GLY B 100 GLY B 106 1 N LEU B 104 O THR B 135
SHEET 3 C 5 ARG B 172 ILE B 178 1 O ILE B 174 N VAL B 103
SHEET 4 C 5 PHE B 201 VAL B 206 1 O VAL B 204 N VAL B 175
SHEET 5 C 5 PHE B 243 LEU B 245 1 O LEU B 245 N LEU B 205
SHEET 1 D 6 THR B 386 PHE B 387 0
SHEET 2 D 6 VAL B 360 ILE B 365 1 N LEU B 364 O PHE B 387
SHEET 3 D 6 VAL B 330 GLY B 334 1 N LEU B 332 O ARG B 361
SHEET 4 D 6 THR B 405 THR B 411 1 O VAL B 407 N VAL B 333
SHEET 5 D 6 ILE B 433 THR B 440 1 O LEU B 436 N PHE B 408
SHEET 6 D 6 ILE B 457 TRP B 461 1 O TRP B 461 N SER B 439
CISPEP 1 LYS A 451 LEU A 452 0 19.25
CISPEP 2 PHE A 544 PRO A 545 0 5.17
CISPEP 3 PRO B 448 LEU B 449 0 19.42
CISPEP 4 PHE B 544 PRO B 545 0 -0.84
SITE 1 AC1 18 VAL A 28 PRO A 29 GLU A 32 SER A 34
SITE 2 AC1 18 GLY A 181 ASN A 209 MET A 213 ARG A 215
SITE 3 AC1 18 ASP A 217 HIS A 504 LYS A 514 TRP A 517
SITE 4 AC1 18 ALA A 521 MET A 522 ARG A 525 IOD A 710
SITE 5 AC1 18 HOH A 801 HOH A 890
SITE 1 AC2 22 GLY A 107 GLY A 108 THR A 109 SER A 110
SITE 2 AC2 22 GLU A 150 GLU A 153 SER A 179 VAL A 180
SITE 3 AC2 22 GLY A 181 ALA A 184 SER A 257 SER A 258
SITE 4 AC2 22 ARG A 259 HIS A 351 LYS A 514 HOH A 835
SITE 5 AC2 22 HOH A 836 HOH A 852 HOH A 859 HOH A 874
SITE 6 AC2 22 HOH A 884 HOH A 885
SITE 1 AC3 1 PHE A 472
SITE 1 AC4 2 ARG A 73 GLY A 250
SITE 1 AC5 1 ALA A 46
SITE 1 AC6 1 THR A 298
SITE 1 AC7 1 GLY A 151
SITE 1 AC8 2 GLY A 3 LYS A 5
SITE 1 AC9 3 GLU A 25 LYS A 33 MG9 A 701
SITE 1 BC1 1 LYS A 531
SITE 1 BC2 1 ASN A 196
SITE 1 BC3 2 GLN A 529 SER A 530
SITE 1 BC4 17 VAL B 28 PRO B 29 GLU B 32 SER B 34
SITE 2 BC4 17 GLY B 181 MET B 213 ARG B 215 ASP B 217
SITE 3 BC4 17 HIS B 504 LYS B 514 TRP B 517 ALA B 521
SITE 4 BC4 17 MET B 522 ARG B 525 IOD B 711 HOH B 801
SITE 5 BC4 17 HOH B 934
SITE 1 BC5 21 GLY B 107 THR B 109 SER B 110 GLU B 150
SITE 2 BC5 21 GLU B 153 SER B 179 VAL B 180 GLY B 181
SITE 3 BC5 21 ALA B 184 SER B 257 SER B 258 ARG B 259
SITE 4 BC5 21 HIS B 351 LYS B 514 HOH B 853 HOH B 855
SITE 5 BC5 21 HOH B 886 HOH B 892 HOH B 901 HOH B 913
SITE 6 BC5 21 HOH B 916
SITE 1 BC6 1 PHE B 472
SITE 1 BC7 2 ARG B 73 GLY B 250
SITE 1 BC8 1 THR B 298
SITE 1 BC9 1 ALA B 46
SITE 1 CC1 1 GLY B 151
SITE 1 CC2 1 SER B 530
SITE 1 CC3 3 GLY B 3 LYS B 5 ALA B 554
SITE 1 CC4 4 GLU B 25 LYS B 33 SER B 34 MG9 B 701
SITE 1 CC5 2 LEU B 445 SER B 458
SITE 1 CC6 1 ASN B 196
SITE 1 CC7 7 GLY B 354 ASP B 507 ARG B 509 LYS B 567
SITE 2 CC7 7 GLU B 568 GLN B 569 HOH B 808
SITE 1 CC8 2 ALA B 44 ASP B 45
SITE 1 CC9 4 LYS B 18 LEU B 21 SER B 22 HOH B 852
SITE 1 DC1 3 GLN B 336 THR B 337 LEU B 364
CRYST1 149.066 149.066 132.463 90.00 90.00 120.00 P 65 12
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 0.006708 0.003873 0.000000 0.00000
SCALE2 0.000000 0.007746 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007549 0.00000
(ATOM LINES ARE NOT SHOWN.)
END