HEADER ISOMERASE 17-JUL-06 2HP2
TITLE INTER-SUBUNIT SIGNALING IN GSAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE (GSAM) HYBRID-
COMPND 3 FORM;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: GSA, GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE, GSA-AT;
COMPND 6 EC: 5.4.3.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 269084;
SOURCE 4 STRAIN: PCC 6301;
SOURCE 5 GENE: HEML, GSA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K74;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSAT 1.4
KEYWDS INTER-SUBUNIT SIGNALING, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.STETEFELD
REVDAT 4 13-JUL-11 2HP2 1 VERSN
REVDAT 3 24-FEB-09 2HP2 1 VERSN
REVDAT 2 23-SEP-08 2HP2 1 JRNL
REVDAT 1 22-AUG-06 2HP2 0
JRNL AUTH J.STETEFELD,M.JENNY,P.BURKHARD
JRNL TITL INTERSUBUNIT SIGNALING IN
JRNL TITL 2 GLUTAMATE-1-SEMIALDEHYDE-AMINOMUTASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 13688 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16954186
JRNL DOI 10.1073/PNAS.0600306103
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1758432.620
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 23661
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 SET) : 0.229
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2335
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3402
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE : 0.3940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 349
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6404
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 362
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.91000
REMARK 3 B22 (A**2) : -8.65000
REMARK 3 B33 (A**2) : -0.26000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.45
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.49
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.66
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.88
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 55.20
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : DAV.PAR
REMARK 3 PARAMETER FILE 4 : PLP.PARAM
REMARK 3 PARAMETER FILE 5 : KE4.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HP2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-06.
REMARK 100 THE RCSB ID CODE IS RCSB038598.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-21
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23661
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 33.38600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.03600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.53950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.03600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.38600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.53950
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A LOCAL DIMER
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: 11010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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 VAL A 1002
REMARK 465 THR A 1003
REMARK 465 SER A 1004
REMARK 465 SER A 1005
REMARK 465 PRO A 1006
REMARK 465 VAL B 2002
REMARK 465 THR B 2003
REMARK 465 SER B 2004
REMARK 465 SER B 2005
REMARK 465 PRO B 2006
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 PRO A1041 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG A1338 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A1338 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B2338 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B2338 NE - CZ - NH2 ANGL. DEV. = 3.2 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 GLN A1040 80.23 57.04
REMARK 500 ASP A1049 -116.60 49.01
REMARK 500 THR A1066 25.52 47.12
REMARK 500 ALA A1070 43.23 -82.01
REMARK 500 SER A1092 130.80 -177.17
REMARK 500 LEU A1158 51.75 -90.27
REMARK 500 VAL A1165 17.10 -147.78
REMARK 500 SER A1172 31.07 -88.63
REMARK 500 SER A1218 20.53 -150.54
REMARK 500 LYS A1273 -91.57 41.66
REMARK 500 ILE A1275 0.07 -69.53
REMARK 500 ALA A1283 142.16 -171.29
REMARK 500 LYS A1287 107.68 -47.24
REMARK 500 THR A1328 -74.56 -44.02
REMARK 500 SER A1360 -143.54 41.49
REMARK 500 PRO A1402 46.16 -65.52
REMARK 500 PHE A1405 40.91 -96.14
REMARK 500 PHE B2034 -1.83 72.65
REMARK 500 GLN B2040 78.28 -116.65
REMARK 500 ASP B2049 -117.08 52.23
REMARK 500 THR B2066 28.14 42.59
REMARK 500 TRP B2067 31.22 74.07
REMARK 500 ALA B2070 45.43 -83.61
REMARK 500 SER B2092 129.22 -177.12
REMARK 500 PRO B2112 -70.20 -47.29
REMARK 500 HIS B2153 45.55 -91.00
REMARK 500 ASP B2155 -62.21 -25.40
REMARK 500 VAL B2159 107.70 -169.61
REMARK 500 ALA B2161 -168.09 -73.86
REMARK 500 SER B2163 -112.31 58.86
REMARK 500 THR B2167 -84.55 -122.89
REMARK 500 LEU B2170 123.90 73.32
REMARK 500 PRO B2171 -167.13 -103.28
REMARK 500 SER B2172 -173.85 -64.67
REMARK 500 SER B2173 -158.01 40.48
REMARK 500 THR B2180 -78.05 -58.63
REMARK 500 THR B2181 -5.77 -53.57
REMARK 500 SER B2218 18.44 -152.44
REMARK 500 GLU B2246 32.95 -99.93
REMARK 500 PHE B2251 16.73 59.49
REMARK 500 ARG B2252 -51.83 -122.44
REMARK 500 LYS B2273 -90.08 43.47
REMARK 500 ALA B2283 140.30 -170.30
REMARK 500 LYS B2287 109.78 -50.50
REMARK 500 THR B2328 -73.36 -46.44
REMARK 500 SER B2360 -152.98 70.33
REMARK 500 THR B2368 146.07 175.10
REMARK 500 PRO B2402 45.89 -63.46
REMARK 500 PHE B2405 40.17 -94.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A7001 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A7011 DISTANCE = 10.13 ANGSTROMS
REMARK 525 HOH A7036 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A7055 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH A7087 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A7112 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH A7141 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A7151 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH B7106 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH B7134 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH B7161 DISTANCE = 7.73 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KE4 A 5000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 6000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HOZ B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HOY RELATED DB: PDB
REMARK 900 INTER-SUBUNIT SIGNALING IN GSAM
REMARK 900 RELATED ID: 2HOZ RELATED DB: PDB
REMARK 900 INTER-SUBUNIT SIGNALING IN GSAM
REMARK 900 RELATED ID: 2HP1 RELATED DB: PDB
REMARK 900 INTER-SUBUNIT SIGNALING IN GSAM
DBREF 2HP2 A 1002 1433 UNP P24630 GSA_SYNP6 1 432
DBREF 2HP2 B 2002 2433 UNP P24630 GSA_SYNP6 1 432
SEQADV 2HP2 ASN A 1108 UNP P24630 ILE 107 CONFLICT
SEQADV 2HP2 ILE A 1133 UNP P24630 LEU 132 CONFLICT
SEQADV 2HP2 SER A 1172 UNP P24630 ASP 171 CONFLICT
SEQADV 2HP2 LYS A 1179 UNP P24630 SER 178 CONFLICT
SEQADV 2HP2 THR A 1187 UNP P24630 ALA 186 CONFLICT
SEQADV 2HP2 GLY A 1327 UNP P24630 ALA 326 CONFLICT
SEQADV 2HP2 ASN B 2108 UNP P24630 ILE 107 CONFLICT
SEQADV 2HP2 ILE B 2133 UNP P24630 LEU 132 CONFLICT
SEQADV 2HP2 SER B 2172 UNP P24630 ASP 171 CONFLICT
SEQADV 2HP2 LYS B 2179 UNP P24630 SER 178 CONFLICT
SEQADV 2HP2 THR B 2187 UNP P24630 ALA 186 CONFLICT
SEQADV 2HP2 GLY B 2327 UNP P24630 ALA 326 CONFLICT
SEQRES 1 A 432 VAL THR SER SER PRO PHE LYS THR ILE LYS SER ASP GLU
SEQRES 2 A 432 ILE PHE ALA ALA ALA GLN LYS LEU MET PRO GLY GLY VAL
SEQRES 3 A 432 SER SER PRO VAL ARG ALA PHE LYS SER VAL GLY GLY GLN
SEQRES 4 A 432 PRO ILE VAL PHE ASP ARG VAL LYS ASP ALA TYR ALA TRP
SEQRES 5 A 432 ASP VAL ASP GLY ASN ARG TYR ILE ASP TYR VAL GLY THR
SEQRES 6 A 432 TRP GLY PRO ALA ILE CYS GLY HIS ALA HIS PRO GLU VAL
SEQRES 7 A 432 ILE GLU ALA LEU LYS VAL ALA MET GLU LYS GLY THR SER
SEQRES 8 A 432 PHE GLY ALA PRO CYS ALA LEU GLU ASN VAL LEU ALA GLU
SEQRES 9 A 432 MET VAL ASN ASP ALA VAL PRO SER ILE GLU MET VAL ARG
SEQRES 10 A 432 PHE VAL ASN SER GLY THR GLU ALA CYS MET ALA VAL LEU
SEQRES 11 A 432 ARG ILE MET ARG ALA TYR THR GLY ARG ASP LYS ILE ILE
SEQRES 12 A 432 LYS PHE GLU GLY CYS TYR HIS GLY HIS ALA ASP MET PHE
SEQRES 13 A 432 LEU VAL LYS ALA GLY SER GLY VAL ALA THR LEU GLY LEU
SEQRES 14 A 432 PRO SER SER PRO GLY VAL PRO LYS LYS THR THR ALA ASN
SEQRES 15 A 432 THR LEU THR THR PRO TYR ASN ASP LEU GLU ALA VAL LYS
SEQRES 16 A 432 ALA LEU PHE ALA GLU ASN PRO GLY GLU ILE ALA GLY VAL
SEQRES 17 A 432 ILE LEU GLU PRO ILE VAL GLY ASN SER GLY PHE ILE VAL
SEQRES 18 A 432 PRO ASP ALA GLY PHE LEU GLU GLY LEU ARG GLU ILE THR
SEQRES 19 A 432 LEU GLU HIS ASP ALA LEU LEU VAL PHE ASP GLU VAL MET
SEQRES 20 A 432 THR GLY PHE ARG ILE ALA TYR GLY GLY VAL GLN GLU LYS
SEQRES 21 A 432 PHE GLY VAL THR PRO ASP LEU THR THR LEU GLY LYS ILE
SEQRES 22 A 432 ILE GLY GLY GLY LEU PRO VAL GLY ALA TYR GLY GLY LYS
SEQRES 23 A 432 ARG GLU ILE MET GLN LEU VAL ALA PRO ALA GLY PRO MET
SEQRES 24 A 432 TYR GLN ALA GLY THR LEU SER GLY ASN PRO LEU ALA MET
SEQRES 25 A 432 THR ALA GLY ILE LYS THR LEU GLU LEU LEU ARG GLN PRO
SEQRES 26 A 432 GLY THR TYR GLU TYR LEU ASP GLN ILE THR LYS ARG LEU
SEQRES 27 A 432 SER ASP GLY LEU LEU ALA ILE ALA GLN GLU THR GLY HIS
SEQRES 28 A 432 ALA ALA CYS GLY GLY GLN VAL SER GLY MET PHE GLY PHE
SEQRES 29 A 432 PHE PHE THR GLU GLY PRO VAL HIS ASN TYR GLU ASP ALA
SEQRES 30 A 432 LYS LYS SER ASP LEU GLN LYS PHE SER ARG PHE HIS ARG
SEQRES 31 A 432 GLY MET LEU GLU GLN GLY ILE TYR LEU ALA PRO SER GLN
SEQRES 32 A 432 PHE GLU ALA GLY PHE THR SER LEU ALA HIS THR GLU GLU
SEQRES 33 A 432 ASP ILE ASP ALA THR LEU ALA ALA ALA ARG THR VAL MET
SEQRES 34 A 432 SER ALA LEU
SEQRES 1 B 432 VAL THR SER SER PRO PHE LYS THR ILE LYS SER ASP GLU
SEQRES 2 B 432 ILE PHE ALA ALA ALA GLN LYS LEU MET PRO GLY GLY VAL
SEQRES 3 B 432 SER SER PRO VAL ARG ALA PHE LYS SER VAL GLY GLY GLN
SEQRES 4 B 432 PRO ILE VAL PHE ASP ARG VAL LYS ASP ALA TYR ALA TRP
SEQRES 5 B 432 ASP VAL ASP GLY ASN ARG TYR ILE ASP TYR VAL GLY THR
SEQRES 6 B 432 TRP GLY PRO ALA ILE CYS GLY HIS ALA HIS PRO GLU VAL
SEQRES 7 B 432 ILE GLU ALA LEU LYS VAL ALA MET GLU LYS GLY THR SER
SEQRES 8 B 432 PHE GLY ALA PRO CYS ALA LEU GLU ASN VAL LEU ALA GLU
SEQRES 9 B 432 MET VAL ASN ASP ALA VAL PRO SER ILE GLU MET VAL ARG
SEQRES 10 B 432 PHE VAL ASN SER GLY THR GLU ALA CYS MET ALA VAL LEU
SEQRES 11 B 432 ARG ILE MET ARG ALA TYR THR GLY ARG ASP LYS ILE ILE
SEQRES 12 B 432 LYS PHE GLU GLY CYS TYR HIS GLY HIS ALA ASP MET PHE
SEQRES 13 B 432 LEU VAL LYS ALA GLY SER GLY VAL ALA THR LEU GLY LEU
SEQRES 14 B 432 PRO SER SER PRO GLY VAL PRO LYS LYS THR THR ALA ASN
SEQRES 15 B 432 THR LEU THR THR PRO TYR ASN ASP LEU GLU ALA VAL LYS
SEQRES 16 B 432 ALA LEU PHE ALA GLU ASN PRO GLY GLU ILE ALA GLY VAL
SEQRES 17 B 432 ILE LEU GLU PRO ILE VAL GLY ASN SER GLY PHE ILE VAL
SEQRES 18 B 432 PRO ASP ALA GLY PHE LEU GLU GLY LEU ARG GLU ILE THR
SEQRES 19 B 432 LEU GLU HIS ASP ALA LEU LEU VAL PHE ASP GLU VAL MET
SEQRES 20 B 432 THR GLY PHE ARG ILE ALA TYR GLY GLY VAL GLN GLU LYS
SEQRES 21 B 432 PHE GLY VAL THR PRO ASP LEU THR THR LEU GLY LYS ILE
SEQRES 22 B 432 ILE GLY GLY GLY LEU PRO VAL GLY ALA TYR GLY GLY LYS
SEQRES 23 B 432 ARG GLU ILE MET GLN LEU VAL ALA PRO ALA GLY PRO MET
SEQRES 24 B 432 TYR GLN ALA GLY THR LEU SER GLY ASN PRO LEU ALA MET
SEQRES 25 B 432 THR ALA GLY ILE LYS THR LEU GLU LEU LEU ARG GLN PRO
SEQRES 26 B 432 GLY THR TYR GLU TYR LEU ASP GLN ILE THR LYS ARG LEU
SEQRES 27 B 432 SER ASP GLY LEU LEU ALA ILE ALA GLN GLU THR GLY HIS
SEQRES 28 B 432 ALA ALA CYS GLY GLY GLN VAL SER GLY MET PHE GLY PHE
SEQRES 29 B 432 PHE PHE THR GLU GLY PRO VAL HIS ASN TYR GLU ASP ALA
SEQRES 30 B 432 LYS LYS SER ASP LEU GLN LYS PHE SER ARG PHE HIS ARG
SEQRES 31 B 432 GLY MET LEU GLU GLN GLY ILE TYR LEU ALA PRO SER GLN
SEQRES 32 B 432 PHE GLU ALA GLY PHE THR SER LEU ALA HIS THR GLU GLU
SEQRES 33 B 432 ASP ILE ASP ALA THR LEU ALA ALA ALA ARG THR VAL MET
SEQRES 34 B 432 SER ALA LEU
HET KE4 A5000 24
HET PLP B6000 15
HET HOZ B 2 9
HETNAM KE4 (4R)-5-AMINO-4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
HETNAM 2 KE4 METHYL]PYRIDIN-4-YL}METHYL)AMINO]PENTANOIC ACID
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM HOZ (4S)-4,5-DIAMINOPENTANOIC ACID
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 KE4 C13 H22 N3 O7 P
FORMUL 4 PLP C8 H10 N O6 P
FORMUL 5 HOZ C5 H12 N2 O2
FORMUL 6 HOH *362(H2 O)
HELIX 1 1 THR A 1009 MET A 1023 1 15
HELIX 2 2 PRO A 1024 VAL A 1027 5 4
HELIX 3 3 SER A 1029 GLY A 1038 5 10
HELIX 4 4 VAL A 1064 GLY A 1068 5 5
HELIX 5 5 HIS A 1076 GLU A 1088 1 13
HELIX 6 6 CYS A 1097 VAL A 1111 1 15
HELIX 7 7 SER A 1122 GLY A 1139 1 18
HELIX 8 8 ALA A 1154 LEU A 1158 5 5
HELIX 9 9 PRO A 1177 ALA A 1182 1 6
HELIX 10 10 ASP A 1191 ASN A 1202 1 12
HELIX 11 11 GLY A 1226 HIS A 1238 1 13
HELIX 12 12 GLY A 1256 PHE A 1262 1 7
HELIX 13 13 ILE A 1274 GLY A 1277 5 4
HELIX 14 14 LYS A 1287 GLN A 1292 1 6
HELIX 15 15 ASN A 1309 ARG A 1324 1 16
HELIX 16 16 GLY A 1327 THR A 1350 1 24
HELIX 17 17 ASN A 1374 LYS A 1380 1 7
HELIX 18 18 ASP A 1382 GLN A 1396 1 15
HELIX 19 19 THR A 1415 LEU A 1433 1 19
HELIX 20 20 THR B 2009 MET B 2023 1 15
HELIX 21 21 PRO B 2024 VAL B 2027 5 4
HELIX 22 22 SER B 2029 GLY B 2038 5 10
HELIX 23 23 VAL B 2064 GLY B 2068 5 5
HELIX 24 24 HIS B 2076 GLU B 2088 1 13
HELIX 25 25 CYS B 2097 VAL B 2111 1 15
HELIX 26 26 SER B 2122 GLY B 2139 1 18
HELIX 27 27 ALA B 2154 LEU B 2158 5 5
HELIX 28 28 PRO B 2177 ASN B 2183 1 7
HELIX 29 29 ASP B 2191 ASN B 2202 1 12
HELIX 30 30 GLY B 2226 HIS B 2238 1 13
HELIX 31 31 GLY B 2256 PHE B 2262 1 7
HELIX 32 32 ILE B 2274 GLY B 2277 5 4
HELIX 33 33 LYS B 2287 GLN B 2292 1 6
HELIX 34 34 ASN B 2309 ARG B 2324 1 16
HELIX 35 35 GLY B 2327 THR B 2350 1 24
HELIX 36 36 ASN B 2374 LYS B 2380 1 7
HELIX 37 37 ASP B 2382 GLN B 2396 1 15
HELIX 38 38 THR B 2415 LEU B 2433 1 19
SHEET 1 A 4 PHE A1044 LYS A1048 0
SHEET 2 A 4 TYR A1051 ASP A1054 -1 O TYR A1051 N LYS A1048
SHEET 3 A 4 ARG A1059 ASP A1062 -1 O TYR A1060 N ALA A1052
SHEET 4 A 4 ILE A1398 TYR A1399 1 O TYR A1399 N ILE A1061
SHEET 1 B 7 MET A1116 VAL A1120 0
SHEET 2 B 7 GLY A1282 GLY A1286 -1 O GLY A1286 N MET A1116
SHEET 3 B 7 LEU A1268 GLY A1272 -1 N LEU A1271 O ALA A1283
SHEET 4 B 7 LEU A1241 ASP A1245 1 N PHE A1244 O THR A1270
SHEET 5 B 7 ILE A1206 LEU A1211 1 N VAL A1209 O VAL A1243
SHEET 6 B 7 LYS A1142 GLU A1147 1 N LYS A1142 O ALA A1207
SHEET 7 B 7 THR A1184 PRO A1188 1 O LEU A1185 N ILE A1143
SHEET 1 C 3 GLN A1358 VAL A1359 0
SHEET 2 C 3 MET A1362 PHE A1363 -1 O MET A1362 N VAL A1359
SHEET 3 C 3 GLY A1408 PHE A1409 -1 O GLY A1408 N PHE A1363
SHEET 1 D 4 PHE B2044 LYS B2048 0
SHEET 2 D 4 TYR B2051 ASP B2054 -1 O TYR B2051 N LYS B2048
SHEET 3 D 4 ARG B2059 ASP B2062 -1 O TYR B2060 N ALA B2052
SHEET 4 D 4 ILE B2398 TYR B2399 1 O TYR B2399 N ILE B2061
SHEET 1 E 7 MET B2116 VAL B2120 0
SHEET 2 E 7 GLY B2282 GLY B2286 -1 O GLY B2282 N VAL B2120
SHEET 3 E 7 LEU B2268 GLY B2272 -1 N LEU B2271 O ALA B2283
SHEET 4 E 7 LEU B2241 ASP B2245 1 N PHE B2244 O THR B2270
SHEET 5 E 7 ILE B2206 LEU B2211 1 N VAL B2209 O VAL B2243
SHEET 6 E 7 LYS B2142 PHE B2146 1 N LYS B2142 O ALA B2207
SHEET 7 E 7 THR B2184 THR B2187 1 O LEU B2185 N ILE B2143
SHEET 1 F 3 CYS B2355 GLN B2358 0
SHEET 2 F 3 MET B2362 PHE B2366 -1 O PHE B2366 N CYS B2355
SHEET 3 F 3 GLY B2408 PHE B2409 -1 O GLY B2408 N PHE B2363
LINK NZ LYS B2273 C4A PLP B6000 1555 1555 1.31
CISPEP 1 ALA A 1295 PRO A 1296 0 0.12
CISPEP 2 GLY A 1370 PRO A 1371 0 0.10
CISPEP 3 SER B 2173 PRO B 2174 0 -0.43
CISPEP 4 ALA B 2295 PRO B 2296 0 0.23
CISPEP 5 GLY B 2370 PRO B 2371 0 -0.12
SITE 1 AC1 21 SER A1029 VAL A1031 TRP A1067 GLY A1123
SITE 2 AC1 21 THR A1124 TYR A1150 HIS A1151 ASN A1217
SITE 3 AC1 21 ASP A1245 VAL A1247 MET A1248 LYS A1273
SITE 4 AC1 21 GLU A1406 HOH A7051 HOH A7167 HOH A7239
SITE 5 AC1 21 HOH A7316 HOH A7364 HOH A7367 ALA B2303
SITE 6 AC1 21 THR B2305
SITE 1 AC2 15 GLY A1304 THR A1305 HOH A7052 HOH A7371
SITE 2 AC2 15 HOZ B 2 SER B2122 GLY B2123 THR B2124
SITE 3 AC2 15 TYR B2150 ASN B2217 ASP B2245 VAL B2247
SITE 4 AC2 15 MET B2248 LYS B2273 HOH B7368
SITE 1 AC3 11 GLY A1304 THR A1305 SER B2029 ARG B2032
SITE 2 AC3 11 TRP B2067 SER B2163 ASN B2217 MET B2248
SITE 3 AC3 11 LYS B2273 GLU B2406 PLP B6000
CRYST1 66.772 109.079 124.072 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 0.014976 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009168 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008060 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
