HEADER TRANSFERASE/TRANSFERASE INHIBITOR 18-MAY-11 3S3P
TITLE TRANSGLUTAMINASE 2 IN COMPLEX WITH A NOVEL INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 2-687;
COMPND 5 SYNONYM: TISSUE TRANSGLUTAMINASE, TRANSGLUTAMINASE C, TG(C), TGC,
COMPND 6 TGASE C, TRANSGLUTAMINASE H, TGASE H, TRANSGLUTAMINASE-2, TGASE-2;
COMPND 7 EC: 2.3.2.13;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PEPTIDE INHIBITOR;
COMPND 11 CHAIN: B;
COMPND 12 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: TGM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS TRANSGLUTAMINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR I.LINDEMANN,A.HEINE,G.KLEBE
REVDAT 4 06-DEC-23 3S3P 1 REMARK
REVDAT 3 13-SEP-23 3S3P 1 REMARK SEQADV LINK
REVDAT 2 26-JUN-13 3S3P 1 REMARK
REVDAT 1 06-JUN-12 3S3P 0
JRNL AUTH I.LINDEMANN,J.BOETTCHER,K.OERTEL,J.WEBER,M.HILS,
JRNL AUTH 2 R.PASTERNACK,A.HEINE,G.KLEBE
JRNL TITL TRANSGLUTAMINASE 2 IN COMPLEX WITH A NOVEL INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.8
REMARK 3 NUMBER OF REFLECTIONS : 25323
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1220
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 46.7394 - 5.1892 0.95 3144 162 0.2541 0.2845
REMARK 3 2 5.1892 - 4.1196 0.91 2833 141 0.1932 0.2280
REMARK 3 3 4.1196 - 3.5991 0.94 2861 154 0.1895 0.2591
REMARK 3 4 3.5991 - 3.2701 0.97 2932 149 0.2084 0.2948
REMARK 3 5 3.2701 - 3.0358 0.97 2916 142 0.2285 0.2933
REMARK 3 6 3.0358 - 2.8568 0.92 2762 133 0.2418 0.3486
REMARK 3 7 2.8568 - 2.7138 0.83 2482 119 0.2546 0.3532
REMARK 3 8 2.7138 - 2.5956 0.73 2166 121 0.2749 0.3372
REMARK 3 9 2.5956 - 2.4957 0.68 2007 99 0.3034 0.4768
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 52.61
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 15.43040
REMARK 3 B22 (A**2) : 15.43040
REMARK 3 B33 (A**2) : -30.86090
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 : 0.007 4854
REMARK 3 ANGLE : 1.071 6617
REMARK 3 CHIRALITY : 0.065 757
REMARK 3 PLANARITY : 0.004 847
REMARK 3 DIHEDRAL : 15.995 1710
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 3S3P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065721.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR KMC
REMARK 200 -2
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25858
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.14700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2Q3Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, 0.1 M HEPES,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 155.18000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.50000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 77.59000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.50000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.50000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 232.77000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.50000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 77.59000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.50000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 232.77000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 155.18000
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 MAIN POLYMERIC PROTEIN-GLUTAMINE GAMMA-
REMARK 300 GLUTAMYLTRANSFERASE 2 IS A MONOMER IN THE ABSENCE OF THE PEPTIDE
REMARK 300 INHIBITOR
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 844 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE UNREACTED FORM OF THE PEPTIDE INHIBITOR, CHAIN B HAS A DOUBLE
REMARK 400 BOND BETWEEN C15 AND C17 OF THE AMINOACID XW1. UPON REACTION WITH
REMARK 400 PROTEIN, A COVALENT BOND BETWEEN C15 AND SG OF CYS 277 CHAIN A IS
REMARK 400 FORMED
REMARK 400
REMARK 400 THE N~2~-[(2S)-2-{[(BENZYLOXY)CARBONYL]AMINO}-7-ETHOXY-7-
REMARK 400 OXOHEPTANOYL]-L-GLUTAMINYL-L-PROLYL-L-LEUCINE IS PEPTIDE-LIKE, A
REMARK 400 MEMBER OF INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: N~2~-[(2S)-2-{[(BENZYLOXY)CARBONYL]AMINO}-7-ETHOXY-7-
REMARK 400 OXOHEPTANOYL]-L-GLUTAMINYL-L-PROLYL-L-LEUCINE
REMARK 400 CHAIN: B
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 -6
REMARK 465 ALA A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 ARG A 240
REMARK 465 TRP A 241
REMARK 465 ASP A 242
REMARK 465 ASN A 243
REMARK 465 ASN A 244
REMARK 465 TYR A 245
REMARK 465 GLY A 246
REMARK 465 ASP A 247
REMARK 465 GLY A 248
REMARK 465 VAL A 249
REMARK 465 SER A 250
REMARK 465 PRO A 251
REMARK 465 MET A 252
REMARK 465 HIS A 267
REMARK 465 GLY A 268
REMARK 465 CYS A 269
REMARK 465 GLN A 270
REMARK 465 ARG A 271
REMARK 465 VAL A 272
REMARK 465 LYS A 273
REMARK 465 TYR A 274
REMARK 465 GLY A 275
REMARK 465 GLN A 276
REMARK 465 HIS A 305
REMARK 465 ASP A 306
REMARK 465 GLN A 307
REMARK 465 ASN A 308
REMARK 465 ASN A 318
REMARK 465 GLU A 319
REMARK 465 PHE A 320
REMARK 465 GLY A 321
REMARK 465 GLU A 322
REMARK 465 ILE A 323
REMARK 465 GLN A 324
REMARK 465 GLY A 325
REMARK 465 ASP A 326
REMARK 465 LYS A 327
REMARK 465 GLN A 362
REMARK 465 GLU A 363
REMARK 465 LYS A 364
REMARK 465 SER A 365
REMARK 465 GLU A 366
REMARK 465 GLY A 367
REMARK 465 THR A 368
REMARK 465 TYR A 369
REMARK 465 GLN A 407
REMARK 465 ASP A 408
REMARK 465 ASP A 409
REMARK 465 GLY A 410
REMARK 465 SER A 411
REMARK 465 VAL A 412
REMARK 465 HIS A 413
REMARK 465 LEU A 462
REMARK 465 ASN A 463
REMARK 465 LYS A 464
REMARK 465 LEU A 465
REMARK 465 ALA A 466
REMARK 465 GLU A 467
REMARK 465 LYS A 468
REMARK 465 GLU A 469
REMARK 465 GLU A 470
REMARK 465 THR A 471
REMARK 465 GLY A 595
REMARK 465 GLU A 596
REMARK 465 PRO A 597
REMARK 465 LYS A 598
REMARK 465 GLN A 599
REMARK 465 LYS A 600
REMARK 465 ARG A 601
REMARK 465 LYS A 602
REMARK 465 LEU A 603
REMARK 465 ILE A 684
REMARK 465 GLY A 685
REMARK 465 PRO A 686
REMARK 465 ALA A 687
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 ARG A 28 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 ASP A 97 CG OD1 OD2
REMARK 470 CYS A 98 SG
REMARK 470 GLU A 120 CG CD OE1 OE2
REMARK 470 TYR A 125 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 LYS A 176 CG CD CE NZ
REMARK 470 ILE A 178 CG1 CG2 CD1
REMARK 470 ASN A 231 CG OD1 ND2
REMARK 470 ASP A 232 CG OD1 OD2
REMARK 470 ASP A 233 CG OD1 OD2
REMARK 470 GLN A 234 CG CD OE1 NE2
REMARK 470 ARG A 263 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 329 CG CD OE1 OE2
REMARK 470 GLN A 348 CG CD OE1 NE2
REMARK 470 ARG A 418 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 433 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 476 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 478 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 501 CG CD OE1 OE2
REMARK 470 GLU A 523 CG CD OE1 OE2
REMARK 470 GLU A 549 CG CD OE1 OE2
REMARK 470 LYS A 550 CG CD CE NZ
REMARK 470 GLU A 557 CG CD OE1 OE2
REMARK 470 SER A 558 OG
REMARK 470 ARG A 592 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 631 CG CD OE1 OE2
REMARK 470 LYS A 634 CG CD CE NZ
REMARK 470 MET A 652 CG SD CE
REMARK 470 LEU A 655 CG CD1 CD2
REMARK 470 LEU A 657 CG CD1 CD2
REMARK 470 MET A 659 CG SD CE
REMARK 470 LYS A 674 CG CD CE NZ
REMARK 470 ARG A 680 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 XW1 B 2 C GLN B 3 N 0.205
REMARK 500 GLN B 3 CD GLN B 3 NE2 0.170
REMARK 500 GLN B 3 C PRO B 4 N 0.120
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 CYS A 277 CA - CB - SG ANGL. DEV. = 9.1 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 CYS A 27 43.85 -95.29
REMARK 500 GLU A 29 -68.68 -108.42
REMARK 500 ALA A 52 -33.39 -38.62
REMARK 500 GLN A 96 -159.73 -117.46
REMARK 500 ASP A 97 -79.45 -41.29
REMARK 500 THR A 123 57.15 -112.76
REMARK 500 PHE A 130 154.60 177.19
REMARK 500 GLN A 169 -159.03 -137.26
REMARK 500 ASN A 206 79.23 -156.06
REMARK 500 ASN A 231 66.19 -100.18
REMARK 500 ASP A 232 -29.93 68.13
REMARK 500 LEU A 312 -76.57 -53.84
REMARK 500 PHE A 316 -82.83 -66.93
REMARK 500 MET A 330 -164.62 -101.90
REMARK 500 MET A 485 116.47 -38.87
REMARK 500 ASN A 498 49.94 -81.62
REMARK 500 ASN A 559 9.44 82.75
REMARK 500 LEU A 629 -36.77 -143.22
REMARK 500 LEU A 655 75.73 -118.19
REMARK 500 PRO A 656 99.18 -28.58
REMARK 500 HIS A 658 -138.15 -113.61
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 SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF PEPTIDE INHIBITOR
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q3Z RELATED DB: PDB
REMARK 900 RELATED ID: 3S3J RELATED DB: PDB
REMARK 900 RELATED ID: 3S3S RELATED DB: PDB
DBREF 3S3P A 2 687 UNP P21980 TGM2_HUMAN 2 687
DBREF 3S3P B 1 5 PDB 3S3P 3S3P 1 5
SEQADV 3S3P MET A -6 UNP P21980 INITIATING METHIONINE
SEQADV 3S3P ALA A -5 UNP P21980 EXPRESSION TAG
SEQADV 3S3P HIS A -4 UNP P21980 EXPRESSION TAG
SEQADV 3S3P HIS A -3 UNP P21980 EXPRESSION TAG
SEQADV 3S3P HIS A -2 UNP P21980 EXPRESSION TAG
SEQADV 3S3P HIS A -1 UNP P21980 EXPRESSION TAG
SEQADV 3S3P HIS A 0 UNP P21980 EXPRESSION TAG
SEQADV 3S3P HIS A 1 UNP P21980 EXPRESSION TAG
SEQRES 1 A 694 MET ALA HIS HIS HIS HIS HIS HIS ALA GLU GLU LEU VAL
SEQRES 2 A 694 LEU GLU ARG CYS ASP LEU GLU LEU GLU THR ASN GLY ARG
SEQRES 3 A 694 ASP HIS HIS THR ALA ASP LEU CYS ARG GLU LYS LEU VAL
SEQRES 4 A 694 VAL ARG ARG GLY GLN PRO PHE TRP LEU THR LEU HIS PHE
SEQRES 5 A 694 GLU GLY ARG ASN TYR GLU ALA SER VAL ASP SER LEU THR
SEQRES 6 A 694 PHE SER VAL VAL THR GLY PRO ALA PRO SER GLN GLU ALA
SEQRES 7 A 694 GLY THR LYS ALA ARG PHE PRO LEU ARG ASP ALA VAL GLU
SEQRES 8 A 694 GLU GLY ASP TRP THR ALA THR VAL VAL ASP GLN GLN ASP
SEQRES 9 A 694 CYS THR LEU SER LEU GLN LEU THR THR PRO ALA ASN ALA
SEQRES 10 A 694 PRO ILE GLY LEU TYR ARG LEU SER LEU GLU ALA SER THR
SEQRES 11 A 694 GLY TYR GLN GLY SER SER PHE VAL LEU GLY HIS PHE ILE
SEQRES 12 A 694 LEU LEU PHE ASN ALA TRP CYS PRO ALA ASP ALA VAL TYR
SEQRES 13 A 694 LEU ASP SER GLU GLU GLU ARG GLN GLU TYR VAL LEU THR
SEQRES 14 A 694 GLN GLN GLY PHE ILE TYR GLN GLY SER ALA LYS PHE ILE
SEQRES 15 A 694 LYS ASN ILE PRO TRP ASN PHE GLY GLN PHE GLU ASP GLY
SEQRES 16 A 694 ILE LEU ASP ILE CYS LEU ILE LEU LEU ASP VAL ASN PRO
SEQRES 17 A 694 LYS PHE LEU LYS ASN ALA GLY ARG ASP CYS SER ARG ARG
SEQRES 18 A 694 SER SER PRO VAL TYR VAL GLY ARG VAL VAL SER GLY MET
SEQRES 19 A 694 VAL ASN CYS ASN ASP ASP GLN GLY VAL LEU LEU GLY ARG
SEQRES 20 A 694 TRP ASP ASN ASN TYR GLY ASP GLY VAL SER PRO MET SER
SEQRES 21 A 694 TRP ILE GLY SER VAL ASP ILE LEU ARG ARG TRP LYS ASN
SEQRES 22 A 694 HIS GLY CYS GLN ARG VAL LYS TYR GLY GLN CYS TRP VAL
SEQRES 23 A 694 PHE ALA ALA VAL ALA CYS THR VAL LEU ARG CYS LEU GLY
SEQRES 24 A 694 ILE PRO THR ARG VAL VAL THR ASN TYR ASN SER ALA HIS
SEQRES 25 A 694 ASP GLN ASN SER ASN LEU LEU ILE GLU TYR PHE ARG ASN
SEQRES 26 A 694 GLU PHE GLY GLU ILE GLN GLY ASP LYS SER GLU MET ILE
SEQRES 27 A 694 TRP ASN PHE HIS CYS TRP VAL GLU SER TRP MET THR ARG
SEQRES 28 A 694 PRO ASP LEU GLN PRO GLY TYR GLU GLY TRP GLN ALA LEU
SEQRES 29 A 694 ASP PRO THR PRO GLN GLU LYS SER GLU GLY THR TYR CYS
SEQRES 30 A 694 CYS GLY PRO VAL PRO VAL ARG ALA ILE LYS GLU GLY ASP
SEQRES 31 A 694 LEU SER THR LYS TYR ASP ALA PRO PHE VAL PHE ALA GLU
SEQRES 32 A 694 VAL ASN ALA ASP VAL VAL ASP TRP ILE GLN GLN ASP ASP
SEQRES 33 A 694 GLY SER VAL HIS LYS SER ILE ASN ARG SER LEU ILE VAL
SEQRES 34 A 694 GLY LEU LYS ILE SER THR LYS SER VAL GLY ARG ASP GLU
SEQRES 35 A 694 ARG GLU ASP ILE THR HIS THR TYR LYS TYR PRO GLU GLY
SEQRES 36 A 694 SER SER GLU GLU ARG GLU ALA PHE THR ARG ALA ASN HIS
SEQRES 37 A 694 LEU ASN LYS LEU ALA GLU LYS GLU GLU THR GLY MET ALA
SEQRES 38 A 694 MET ARG ILE ARG VAL GLY GLN SER MET ASN MET GLY SER
SEQRES 39 A 694 ASP PHE ASP VAL PHE ALA HIS ILE THR ASN ASN THR ALA
SEQRES 40 A 694 GLU GLU TYR VAL CYS ARG LEU LEU LEU CYS ALA ARG THR
SEQRES 41 A 694 VAL SER TYR ASN GLY ILE LEU GLY PRO GLU CYS GLY THR
SEQRES 42 A 694 LYS TYR LEU LEU ASN LEU ASN LEU GLU PRO PHE SER GLU
SEQRES 43 A 694 LYS SER VAL PRO LEU CYS ILE LEU TYR GLU LYS TYR ARG
SEQRES 44 A 694 ASP CYS LEU THR GLU SER ASN LEU ILE LYS VAL ARG ALA
SEQRES 45 A 694 LEU LEU VAL GLU PRO VAL ILE ASN SER TYR LEU LEU ALA
SEQRES 46 A 694 GLU ARG ASP LEU TYR LEU GLU ASN PRO GLU ILE LYS ILE
SEQRES 47 A 694 ARG ILE LEU GLY GLU PRO LYS GLN LYS ARG LYS LEU VAL
SEQRES 48 A 694 ALA GLU VAL SER LEU GLN ASN PRO LEU PRO VAL ALA LEU
SEQRES 49 A 694 GLU GLY CYS THR PHE THR VAL GLU GLY ALA GLY LEU THR
SEQRES 50 A 694 GLU GLU GLN LYS THR VAL GLU ILE PRO ASP PRO VAL GLU
SEQRES 51 A 694 ALA GLY GLU GLU VAL LYS VAL ARG MET ASP LEU LEU PRO
SEQRES 52 A 694 LEU HIS MET GLY LEU HIS LYS LEU VAL VAL ASN PHE GLU
SEQRES 53 A 694 SER ASP LYS LEU LYS ALA VAL LYS GLY PHE ARG ASN VAL
SEQRES 54 A 694 ILE ILE GLY PRO ALA
SEQRES 1 B 5 PHQ XW1 GLN PRO LEU
MODRES 3S3P XW1 B 2 ALA
HET PHQ B 1 10
HET XW1 B 2 13
HET SO4 A 701 5
HET SO4 A 702 5
HET SO4 A 703 5
HET SO4 A 704 5
HET SO4 A 705 5
HET SO4 A 706 5
HETNAM PHQ BENZYL CHLOROCARBONATE
HETNAM XW1 (2S)-2-AMINO-7-ETHOXY-7-OXOHEPTANOIC ACID
HETNAM SO4 SULFATE ION
FORMUL 2 PHQ C8 H7 CL O2
FORMUL 2 XW1 C9 H17 N O4
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 9 HOH *50(H2 O)
HELIX 1 1 GLU A 13 HIS A 21 1 9
HELIX 2 2 THR A 23 CYS A 27 5 5
HELIX 3 3 SER A 152 VAL A 160 1 9
HELIX 4 4 GLY A 188 VAL A 199 1 12
HELIX 5 5 ASN A 200 ASN A 206 1 7
HELIX 6 6 ASN A 206 ARG A 214 1 9
HELIX 7 7 SER A 216 GLY A 226 1 11
HELIX 8 8 SER A 257 ASN A 266 1 10
HELIX 9 9 CYS A 277 GLY A 292 1 16
HELIX 10 10 ASN A 310 ARG A 317 1 8
HELIX 11 11 VAL A 376 GLU A 381 1 6
HELIX 12 12 ASP A 389 ASN A 398 1 10
HELIX 13 13 ILE A 439 LYS A 444 1 6
HELIX 14 14 SER A 449 HIS A 461 1 13
HELIX 15 15 LEU A 547 ARG A 552 1 6
SHEET 1 A 4 LEU A 7 ASP A 11 0
SHEET 2 A 4 PHE A 39 PHE A 45 -1 O THR A 42 N ASP A 11
SHEET 3 A 4 THR A 99 THR A 105 -1 O LEU A 102 N LEU A 41
SHEET 4 A 4 THR A 89 GLN A 95 -1 N ASP A 94 O SER A 101
SHEET 1 B 5 LEU A 31 ARG A 34 0
SHEET 2 B 5 GLY A 127 LEU A 138 1 O ILE A 136 N VAL A 33
SHEET 3 B 5 GLY A 113 SER A 122 -1 N LEU A 117 O GLY A 133
SHEET 4 B 5 SER A 56 THR A 63 -1 N SER A 60 O SER A 118
SHEET 5 B 5 LYS A 74 PRO A 78 -1 O PHE A 77 N PHE A 59
SHEET 1 C 2 GLN A 164 GLY A 170 0
SHEET 2 C 2 ILE A 175 ASN A 181 -1 O LYS A 176 N GLN A 169
SHEET 1 D 6 VAL A 374 PRO A 375 0
SHEET 2 D 6 GLY A 353 LEU A 357 -1 N ALA A 356 O VAL A 374
SHEET 3 D 6 PHE A 334 MET A 342 -1 N SER A 340 O GLN A 355
SHEET 4 D 6 THR A 295 SER A 303 -1 N ARG A 296 O GLU A 339
SHEET 5 D 6 ILE A 421 LYS A 429 -1 O SER A 427 N THR A 299
SHEET 6 D 6 ARG A 436 ASP A 438 -1 O GLU A 437 N THR A 428
SHEET 1 E 6 SER A 415 ILE A 416 0
SHEET 2 E 6 ASP A 400 TRP A 404 -1 N ASP A 403 O SER A 415
SHEET 3 E 6 SER A 574 TYR A 583 1 O TYR A 575 N ASP A 400
SHEET 4 E 6 LEU A 560 GLU A 569 -1 N ILE A 561 O LEU A 582
SHEET 5 E 6 TYR A 503 VAL A 514 -1 N ARG A 512 O LYS A 562
SHEET 6 E 6 LEU A 520 LEU A 534 -1 O LEU A 532 N CYS A 505
SHEET 1 F 3 MET A 473 ARG A 478 0
SHEET 2 F 3 PHE A 489 ASN A 497 -1 O HIS A 494 N ARG A 476
SHEET 3 F 3 SER A 538 ILE A 546 -1 O SER A 538 N ASN A 497
SHEET 1 G 3 LYS A 590 ARG A 592 0
SHEET 2 G 3 ALA A 605 GLN A 610 -1 O GLU A 606 N ARG A 592
SHEET 3 G 3 GLU A 647 MET A 652 -1 O VAL A 650 N VAL A 607
SHEET 1 H 4 VAL A 636 ILE A 638 0
SHEET 2 H 4 CYS A 620 GLU A 625 -1 N CYS A 620 O ILE A 638
SHEET 3 H 4 HIS A 662 GLU A 669 -1 O VAL A 665 N GLU A 625
SHEET 4 H 4 VAL A 676 VAL A 682 -1 O GLY A 678 N VAL A 666
LINK SG CYS A 277 C15 XW1 B 2 1555 1555 1.78
LINK C1 PHQ B 1 N XW1 B 2 1555 1555 1.49
LINK C XW1 B 2 N GLN B 3 1555 1555 1.54
CISPEP 1 GLN A 234 GLY A 235 0 -1.23
CISPEP 2 GLY A 372 PRO A 373 0 3.37
CISPEP 3 LYS A 387 TYR A 388 0 -0.50
SITE 1 AC1 2 LYS A 202 ARG A 222
SITE 1 AC2 3 LYS A 202 ARG A 209 TYR A 219
SITE 1 AC3 1 ARG A 80
SITE 1 AC4 3 ARG A 80 ASP A 81 ALA A 82
SITE 1 AC5 4 ARG A 478 VAL A 479 GLY A 480 ARG A 580
SITE 1 AC6 3 SER A 68 GLN A 69 LYS A 74
SITE 1 AC7 14 GLN A 169 GLY A 170 CYS A 277 SER A 303
SITE 2 AC7 14 MET A 330 ILE A 331 TRP A 332 ASN A 333
SITE 3 AC7 14 PHE A 334 HIS A 335 LEU A 420 TYR A 516
SITE 4 AC7 14 ASN A 517 GLU A 557
CRYST1 71.000 71.000 310.360 90.00 90.00 90.00 P 41 21 2 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 0.014085 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014085 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003222 0.00000
(ATOM LINES ARE NOT SHOWN.)
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